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{
    "count": 876,
    "next": "https://mitotox.org/api/targets/list?format=api&page=4",
    "previous": "https://mitotox.org/api/targets/list?format=api&page=2",
    "results": [
        {
            "targ_id": "T058",
            "parent_targ_id": "T",
            "full_name": "Succinyl-CoA:3-ketoacid coenzyme A transferase 2, mitochondrial",
            "abbrev": "SCOT-t",
            "protein_names": "Succinyl-CoA:3-ketoacid coenzyme A transferase 2, mitochondrial (EC 2.8.3.5) (3-oxoacid CoA-transferase 2A) (Testis-specific succinyl-CoA:3-oxoacid CoA-transferase) (SCOT-t)",
            "related_func_ids": "F02060202",
            "category": "enzyme",
            "subcategories": "Transferase",
            "Uniport_ID": "Q9BYC2",
            "Uniprot_name": "SCOT2_HUMAN",
            "EC_numbers": "2.8.3.5",
            "gene_symbol": "OXCT2",
            "gene_synonyms": "FKSG25, FLJ00030, SCOT-T",
            "gene_synonyms_links": "",
            "gene_name": "3-oxoacid CoA-transferase 2",
            "hgnc_id": "",
            "entrez_id": "",
            "ensembl_id": "ENSG00000198754",
            "omim_id": "",
            "genecard_link": "",
            "locs": "Mitochondrion",
            "reaction": "a 3-oxo acid + succinyl-CoA = a 3-oxoacyl-CoA + succinate",
            "targ_desciption": "Key enzyme for ketone body catabolism. Transfers the CoAmoiety from succinate to acetoacetate. Formation of the enzyme-CoAintermediate proceeds via an unstable anhydride species formed betweenthe carboxylate groups of the enzyme and substrate (By similarity).{ECO:0000250}.",
            "references": []
        },
        {
            "targ_id": "T059",
            "parent_targ_id": "T",
            "full_name": "Trimethyllysine dioxygenase, mitochondrial",
            "abbrev": "TMLD",
            "protein_names": "Trimethyllysine dioxygenase, mitochondrial (EC 1.14.11.8) (Epsilon-trimethyllysine 2-oxoglutarate dioxygenase) (Epsilon-trimethyllysine hydroxylase) (TML hydroxylase) (TML-alpha-ketoglutarate dioxygenase) (TML dioxygenase) (TMLD)",
            "related_func_ids": "F02060104",
            "category": "enzyme",
            "subcategories": "Dioxygenase, Oxidoreductase",
            "Uniport_ID": "Q9NVH6",
            "Uniprot_name": "TMLH_HUMAN",
            "EC_numbers": "1.14.11.8",
            "gene_symbol": "TMLHE",
            "gene_synonyms": "BBOX2, FLJ10727, TMLH, XAP130",
            "gene_synonyms_links": "",
            "gene_name": "Trimethyllysine hydroxylase, epsilon",
            "hgnc_id": "",
            "entrez_id": "",
            "ensembl_id": "ENSG00000185973",
            "omim_id": "",
            "genecard_link": "",
            "locs": "Mitochondrion matrix",
            "reaction": "2-oxoglutarate + N(6),N(6),N(6)-trimethyl-L-lysine + O2 =(3S)-3-hydroxy-N(6),N(6),N(6)-trimethyl-L-lysine + CO2 + succinate",
            "targ_desciption": "Converts trimethyllysine (TML) into hydroxytrimethyllysine(HTML) (PubMed:11431483, PubMed:23092983).{ECO:0000269|PubMed:11431483, ECO:0000269|PubMed:23092983}.",
            "references": []
        },
        {
            "targ_id": "T060",
            "parent_targ_id": "T",
            "full_name": "Adrenodoxin, mitochondrial",
            "abbrev": "Adrenal ferredoxin",
            "protein_names": "Adrenodoxin, mitochondrial (Adrenal ferredoxin) (Ferredoxin-1) (Hepatoredoxin)",
            "related_func_ids": "F020604",
            "category": "protein",
            "subcategories": "electron transfer protein",
            "Uniport_ID": "P10109",
            "Uniprot_name": "ADX_HUMAN",
            "EC_numbers": "",
            "gene_symbol": "FDX1",
            "gene_synonyms": "ADX, FDX",
            "gene_synonyms_links": "",
            "gene_name": "Ferredoxin 1",
            "hgnc_id": "",
            "entrez_id": "",
            "ensembl_id": "ENSG00000137714",
            "omim_id": "",
            "genecard_link": "",
            "locs": "Mitochondrion matrix",
            "reaction": "",
            "targ_desciption": "Essential for the synthesis of various steroid hormones(PubMed:20547883, PubMed:21636783). Participates in the reduction ofmitochondrial cytochrome P450 for steroidogenesis (PubMed:20547883,PubMed:21636783). Transfers electrons from adrenodoxin reductase toCYP11A1, a cytochrome P450 that catalyzes cholesterol side-chaincleavage (PubMed:20547883, PubMed:21636783). Does not form a ternarycomplex with adrenodoxin reductase and CYP11A1 but shuttles between thetwo enzymes to transfer electrons (By similarity).{ECO:0000250|UniProtKB:P00257, ECO:0000269|PubMed:20547883,ECO:0000269|PubMed:21636783}.",
            "references": []
        },
        {
            "targ_id": "T061",
            "parent_targ_id": "T",
            "full_name": "Cytochrome P450 1A1",
            "abbrev": "CYPIA1",
            "protein_names": "Cytochrome P450 1A1 (CYPIA1) (EC 1.14.14.1) (Cytochrome P450 form 6) (Cytochrome P450-C) (Cytochrome P450-P1) (Hydroperoxy icosatetraenoate dehydratase) (EC 4.2.1.152)",
            "related_func_ids": "F02060105; F020604",
            "category": "enzyme",
            "subcategories": "Lyase, Monooxygenase, Oxidoreductase",
            "Uniport_ID": "P04798",
            "Uniprot_name": "CP1A1_HUMAN",
            "EC_numbers": "1.14.14.1; 4.2.1.152",
            "gene_symbol": "CYP1A1",
            "gene_synonyms": "",
            "gene_synonyms_links": "",
            "gene_name": "",
            "hgnc_id": "",
            "entrez_id": "",
            "ensembl_id": "",
            "omim_id": "",
            "genecard_link": "",
            "locs": "Endoplasmic reticulum membrane; Peripheral membrane protein; Mitochondrion inner membrane; Peripheral membrane protein; Microsome membrane; Peripheral membrane protein; Cytoplasm",
            "reaction": "an organic molecule + O2 + reduced [NADPH--hemoproteinreductase] = an alcohol + H(+) + H2O + oxidized [NADPH--hemoproteinreductase]; estrone + O2 + reduced [NADPH--hemoprotein reductase] = 2-hydroxyestrone + H(+) + H2O + oxidized [NADPH--hemoproteinreductase]; estrone + O2 + reduced [NADPH--hemoprotein reductase] = 4-hydroxyestrone + H(+) + H2O + oxidized [NADPH--hemoproteinreductase]; estrone + O2 + reduced [NADPH--hemoprotein reductase] =6alpha-hydroxyestrone + H(+) + H2O + oxidized [NADPH--hemoproteinreductase]; estrone + O2 + reduced [NADPH--hemoprotein reductase] =15alpha-hydroxyestrone + H(+) + H2O + oxidized [NADPH--hemoproteinreductase]; estrone + O2 + reduced [NADPH--hemoprotein reductase] =16alpha-hydroxyestrone + H(+) + H2O + oxidized [NADPH--hemoproteinreductase]; 17beta-estradiol + O2 + reduced [NADPH--hemoprotein reductase]= 2-hydroxy-17beta-estradiol + H(+) + H2O + oxidized [NADPH--hemoprotein reductase]; 17beta-estradiol + O2 + reduced [NADPH--hemoprotein reductase]= 4-hydroxy-17beta-estradiol + H(+) + H2O + oxidized [NADPH--hemoprotein reductase]; 17beta-estradiol + O2 + reduced [NADPH--hemoprotein reductase]= 6alpha-hydroxy-17beta-estradiol + H(+) + H2O + oxidized [NADPH--hemoprotein reductase]; 17beta-estradiol + O2 + reduced [NADPH--hemoprotein reductase]= 7alpha-hydroxy-17beta-estradiol + H(+) + H2O + oxidized [NADPH--hemoprotein reductase]; 17beta-estradiol + O2 + reduced [NADPH--hemoprotein reductase]= 15alpha-hydroxy-17beta-estradiol + H(+) + H2O + oxidized [NADPH--hemoprotein reductase]; (5Z,8Z,11Z)-eicosatrienoate + O2 + reduced [NADPH--hemoproteinreductase] = 19-hydroxy-(5Z,8Z,11Z)-eicosatrienoate + H(+) + H2O +oxidized [NADPH--hemoprotein reductase]; (5Z,8Z,11Z,14Z)-eicosatetraenoate + O2 + reduced [NADPH--hemoprotein reductase] = 16-hydroxy-(5Z,8Z,11Z,14Z)-eicosatetraenoate+ H(+) + H2O + oxidized [NADPH--hemoprotein reductase]; (5Z,8Z,11Z,14Z)-eicosatetraenoate + O2 + reduced [NADPH--hemoprotein reductase] = 17-hydroxy-(5Z,8Z,11Z,14Z)-eicosatetraenoate+ H(+) + H2O + oxidized [NADPH--hemoprotein reductase]; (5Z,8Z,11Z,14Z)-eicosatetraenoate + O2 + reduced [NADPH--hemoprotein reductase] = 18-hydroxy-(5Z,8Z,11Z,14Z)-eicosatetraenoate+ H(+) + H2O + oxidized [NADPH--hemoprotein reductase]; (5Z,8Z,11Z,14Z)-eicosatetraenoate + O2 + reduced [NADPH--hemoprotein reductase] = 19-hydroxy-(5Z,8Z,11Z,14Z)-eicosatetraenoate+ H(+) + H2O + oxidized [NADPH--hemoprotein reductase]; (5Z,8Z,11Z,14Z,17Z)-eicosapentaenoate + O2 + reduced [NADPH--hemoprotein reductase] = 19-hydroxy-(5Z,8Z,11Z,14Z,17Z)-eicosapentaenoate + H(+) + H2O + oxidized [NADPH--hemoproteinreductase]; (5Z,8Z,11Z,14Z)-eicosatetraenoate + O2 + reduced [NADPH--hemoprotein reductase] = (8R,9S)-epoxy-(5Z,11Z,14Z)-eicosatrienoate +H(+) + H2O + oxidized [NADPH--hemoprotein reductase]; (5Z,8Z,11Z,14Z)-eicosatetraenoate + O2 + reduced [NADPH--hemoprotein reductase] = (11R,12S)-epoxy-(5Z,8Z,14Z)-eicosatrienoate+ H(+) + H2O + oxidized [NADPH--hemoprotein reductase]; (5Z,8Z,11Z,14Z)-eicosatetraenoate + O2 + reduced [NADPH--hemoprotein reductase] = (14S,15R)-epoxy-(5Z,8Z,11Z)-eicosatrienoate+ H(+) + H2O + oxidized [NADPH--hemoprotein reductase]; (5Z,8Z,11Z,14Z)-eicosatetraenoate + O2 + reduced [NADPH--hemoprotein reductase] = (14R,15S)-epoxy-(5Z,8Z,11Z)-eicosatrienoate+ H(+) + H2O + oxidized [NADPH--hemoprotein reductase]; (5Z,8Z,11Z,14Z,17Z)-eicosapentaenoate + O2 + reduced [NADPH--hemoprotein reductase] = (17R,18S)-epoxy-(5Z,8Z,11Z,14Z)-eicosatetraenoate + H(+) + H2O + oxidized [NADPH--hemoproteinreductase]; (4Z,7Z,10Z,13Z,16Z,19Z)-docosahexaenoate + O2 + reduced[NADPH--hemoprotein reductase] = (19S,20R)-epoxy-(4Z,7Z,10Z,13Z,16Z)-docosapentaenoate + H(+) + H2O + oxidized [NADPH--hemoproteinreductase]; (4Z,7Z,10Z,13Z,16Z,19Z)-docosahexaenoate + O2 + reduced[NADPH--hemoprotein reductase] = (19R,20S)-epoxy-(4Z,7Z,10Z,13Z,16Z)-docosapentaenoate + H(+) + H2O + oxidized [NADPH--hemoproteinreductase]; all-trans-retinol + O2 + reduced [NADPH--hemoproteinreductase] = all-trans-retinal + H(+) + 2 H2O + oxidized [NADPH--hemoprotein reductase]; all-trans-retinal + O2 + reduced [NADPH--hemoproteinreductase] = all-trans-retinoate + 2 H(+) + H2O + oxidized [NADPH--hemoprotein reductase]; (13S)-hydroperoxy-(9Z,11E)-octadecadienoate = 13-oxo-(9Z,11E)-octadecadienoate + H2O; (12S)-hydroperoxy-(5Z,8Z,10E,14Z)-eicosatetraenoate = 12-oxo-(5Z,8Z,10E,14Z)-eicosatetraenoate + H2O; (15S)-hydroperoxy-(5Z,8Z,11Z,13E)-eicosatetraenoate = 15-oxo-(5Z,8Z,11Z,13E)-eicosatetraenoate + H2O; (5S)-hydroperoxy-(6E,8Z,11Z,14Z)-eicosatetraenoate = 5-oxo-(6E,8Z,11Z,14Z)-eicosatetraenoate + H2O",
            "targ_desciption": "A cytochrome P450 monooxygenase involved in the metabolism ofvarious endogenous substrates, including fatty acids, steroid hormonesand vitamins (PubMed:11555828, PubMed:14559847, PubMed:12865317,PubMed:15805301, PubMed:15041462, PubMed:18577768, PubMed:19965576,PubMed:20972997, PubMed:10681376). Mechanistically, uses molecularoxygen inserting one oxygen atom into a substrate, and reducing thesecond into a water molecule, with two electrons provided by NADPH viacytochrome P450 reductase (NADPH--hemoprotein reductase)(PubMed:11555828, PubMed:14559847, PubMed:12865317, PubMed:15805301,PubMed:15041462, PubMed:18577768, PubMed:19965576, PubMed:20972997,PubMed:10681376). Catalyzes the hydroxylation of carbon-hydrogen bonds.Exhibits high catalytic activity for the formation of hydroxyestrogensfrom estrone (E1) and 17beta-estradiol (E2), namely 2-hydroxy E1 andE2, as well as D-ring hydroxylated E1 and E2 at the C15-alpha and C16-alpha positions (PubMed:11555828, PubMed:14559847, PubMed:12865317,PubMed:15805301). Displays different regioselectivities forpolyunsaturated fatty acids (PUFA) hydroxylation (PubMed:15041462,PubMed:18577768). Catalyzes the epoxidation of double bonds of certainPUFA (PubMed:15041462, PubMed:19965576, PubMed:20972997). Convertsarachidonic acid toward epoxyeicosatrienoic acid (EET) regioisomers,8,9-, 11,12-, and 14,15-EET, that function as lipid mediators in thevascular system (PubMed:20972997). Displays an absolutestereoselectivity in the epoxidation of eicosapentaenoic acid (EPA)producing the 17(R),18(S) enantiomer (PubMed:15041462). May play animportant role in all-trans retinoic acid biosynthesis in extrahepatictissues. Catalyzes two successive oxidative transformation of all-transretinol to all-trans retinal and then to the active form all-transretinoic acid (PubMed:10681376). May also participate in eicosanoidsmetabolism by converting hydroperoxide species into oxo metabolites(lipoxygenase-like reaction, NADPH-independent) (PubMed:21068195).{ECO:0000269|PubMed:10681376, ECO:0000269|PubMed:11555828,ECO:0000269|PubMed:12865317, ECO:0000269|PubMed:14559847,ECO:0000269|PubMed:15041462, ECO:0000269|PubMed:15805301,ECO:0000269|PubMed:18577768, ECO:0000269|PubMed:19965576,ECO:0000269|PubMed:20972997, ECO:0000269|PubMed:21068195}.",
            "references": []
        },
        {
            "targ_id": "T062",
            "parent_targ_id": "T",
            "full_name": "Cytochrome P450 2E1",
            "abbrev": "CYPIIE1",
            "protein_names": "Cytochrome P450 2E1 (EC 1.14.14.1) (4-nitrophenol 2-hydroxylase) (EC 1.14.13.n7) (CYPIIE1) (Cytochrome P450-J)",
            "related_func_ids": "F02060105; F020604",
            "category": "enzyme",
            "subcategories": "Monooxygenase, Oxidoreductase",
            "Uniport_ID": "P05181",
            "Uniprot_name": "CP2E1_HUMAN",
            "EC_numbers": "1.14.14.1; 1.14.13.n7",
            "gene_symbol": "CYP2E1",
            "gene_synonyms": "CYP2E",
            "gene_synonyms_links": "",
            "gene_name": "",
            "hgnc_id": "",
            "entrez_id": "",
            "ensembl_id": "ENSG00000130649",
            "omim_id": "",
            "genecard_link": "",
            "locs": "Endoplasmic reticulum membrane; Peripheral membrane protein; Microsome membrane; Peripheral membrane protein; Mitochondrion inner membrane; Peripheral membrane protein",
            "reaction": "an organic molecule + O2 + reduced [NADPH--hemoproteinreductase] = an alcohol + H(+) + H2O + oxidized [NADPH--hemoproteinreductase]; (5Z,8Z,11Z)-eicosatrienoate + O2 + reduced [NADPH--hemoproteinreductase] = 19-hydroxy-(5Z,8Z,11Z)-eicosatrienoate + H(+) + H2O +oxidized [NADPH--hemoprotein reductase]; (5Z,8Z,11Z,14Z,17Z)-eicosapentaenoate + O2 + reduced [NADPH--hemoprotein reductase] = 19-hydroxy-(5Z,8Z,11Z,14Z,17Z)-eicosapentaenoate + H(+) + H2O + oxidized [NADPH--hemoproteinreductase]; (4Z,7Z,10Z,13Z,16Z,19Z)-docosahexaenoate + O2 + reduced[NADPH--hemoprotein reductase] = 21-hydroxy-(4Z,7Z,10Z,13Z,16Z,19Z)-docosahexaenoate + H(+) + H2O + oxidized [NADPH--hemoproteinreductase]; dodecanoate + O2 + reduced [NADPH--hemoprotein reductase] =11-hydroxydodecanoate + H(+) + H2O + oxidized [NADPH--hemoproteinreductase]; O2 + reduced [NADPH--hemoprotein reductase] + tetradecanoate =13-hydroxytetradecanoate + H(+) + H2O + oxidized [NADPH--hemoproteinreductase]; 4-nitrophenol + H(+) + NADPH + O2 = 4-nitrocatechol + H2O +NADP(+)",
            "targ_desciption": "A cytochrome P450 monooxygenase involved in the metabolism of fatty acids (PubMed:10553002, PubMed:18577768). Mechanistically, usesmolecular oxygen inserting one oxygen atom into a substrate, andreducing the second into a water molecule, with two electrons providedby NADPH via cytochrome P450 reductase (NADPH--hemoprotein reductase)(PubMed:10553002, PubMed:18577768). Catalyzes the hydroxylation ofcarbon-hydrogen bonds. Hydroxylates fatty acids specifically at theomega-1 position displaying the highest catalytic activity forsaturated fatty acids (PubMed:10553002, PubMed:18577768). May beinvolved in the oxidative metabolism of xenobiotics (Probable).{ECO:0000269|PubMed:10553002, ECO:0000269|PubMed:18577768,ECO:0000305|PubMed:9348445}.",
            "references": []
        },
        {
            "targ_id": "T063",
            "parent_targ_id": "T",
            "full_name": "Cytochrome P450 2C8",
            "abbrev": "CYPIIC8",
            "protein_names": "Cytochrome P450 2C8 (EC 1.14.14.1) (CYPIIC8) (Cytochrome P450 IIC2) (Cytochrome P450 MP-12) (Cytochrome P450 MP-20) (Cytochrome P450 form 1) (S-mephenytoin 4-hydroxylase)",
            "related_func_ids": "F02060105; F020604",
            "category": "enzyme",
            "subcategories": "Monooxygenase, Oxidoreductase",
            "Uniport_ID": "P10632",
            "Uniprot_name": "CP2C8_HUMAN",
            "EC_numbers": "1.14.14.1",
            "gene_symbol": "CYP2C8",
            "gene_synonyms": "",
            "gene_synonyms_links": "",
            "gene_name": "",
            "hgnc_id": "",
            "entrez_id": "",
            "ensembl_id": "",
            "omim_id": "",
            "genecard_link": "",
            "locs": "Endoplasmic reticulum membrane; Peripheral membrane protein; Microsome membrane; Peripheral membrane protein",
            "reaction": "an organic molecule + O2 + reduced [NADPH--hemoproteinreductase] = an alcohol + H(+) + H2O + oxidized [NADPH--hemoproteinreductase]; (5Z,8Z,11Z,14Z)-eicosatetraenoate + O2 + reduced [NADPH--hemoprotein reductase] = (11R,12S)-epoxy-(5Z,8Z,14Z)-eicosatrienoate+ H(+) + H2O + oxidized [NADPH--hemoprotein reductase]; (5Z,8Z,11Z,14Z)-eicosatetraenoate + O2 + reduced [NADPH--hemoprotein reductase] = (11S,12R)-epoxy-(5Z,8Z,14Z)-eicosatrienoate+ H(+) + H2O + oxidized [NADPH--hemoprotein reductase]; (5Z,8Z,11Z,14Z)-eicosatetraenoate + O2 + reduced [NADPH--hemoprotein reductase] = (14R,15S)-epoxy-(5Z,8Z,11Z)-eicosatrienoate+ H(+) + H2O + oxidized [NADPH--hemoprotein reductase]; (5Z,8Z,11Z,14Z)-eicosatetraenoate + O2 + reduced [NADPH--hemoprotein reductase] = (14S,15R)-epoxy-(5Z,8Z,11Z)-eicosatrienoate+ H(+) + H2O + oxidized [NADPH--hemoprotein reductase]; (5Z,8Z,11Z,14Z,17Z)-eicosapentaenoate + O2 + reduced [NADPH--hemoprotein reductase] = 11,12-epoxy-(5Z,8Z,14Z,17Z)-eicosatetraenoate + H(+) + H2O + oxidized [NADPH--hemoproteinreductase]; (5Z,8Z,11Z,14Z,17Z)-eicosapentaenoate + O2 + reduced [NADPH--hemoprotein reductase] = 14,15-epoxy-(5Z,8Z,11Z,17Z)-eicosatetraenoate + H(+) + H2O + oxidized [NADPH--hemoproteinreductase]; (5Z,8Z,11Z,14Z,17Z)-eicosapentaenoate + O2 + reduced [NADPH--hemoprotein reductase] = (17R,18S)-epoxy-(5Z,8Z,11Z,14Z)-eicosatetraenoate + H(+) + H2O + oxidized [NADPH--hemoproteinreductase]; (5Z,8Z,11Z,14Z,17Z)-eicosapentaenoate + O2 + reduced [NADPH--hemoprotein reductase] = (17S,18R)-epoxy-(5Z,8Z,11Z,14Z)-eicosatetraenoate + H(+) + H2O + oxidized [NADPH--hemoproteinreductase]; (4Z,7Z,10Z,13Z,16Z,19Z)-docosahexaenoate + O2 + reduced[NADPH--hemoprotein reductase] = (19R,20S)-epoxy-(4Z,7Z,10Z,13Z,16Z)-docosapentaenoate + H(+) + H2O + oxidized [NADPH--hemoproteinreductase]; (4Z,7Z,10Z,13Z,16Z,19Z)-docosahexaenoate + O2 + reduced[NADPH--hemoprotein reductase] = (19S,20R)-epoxy-(4Z,7Z,10Z,13Z,16Z)-docosapentaenoate + H(+) + H2O + oxidized [NADPH--hemoproteinreductase]; all-trans-retinoate + O2 + reduced [NADPH--hemoproteinreductase] = all-trans-4-hydroxyretinoate + H(+) + H2O + oxidized[NADPH--hemoprotein reductase]; 17beta-estradiol + O2 + reduced [NADPH--hemoprotein reductase]= 16alpha,17beta-estriol + H(+) + H2O + oxidized [NADPH--hemoproteinreductase]; estrone + O2 + reduced [NADPH--hemoprotein reductase] =16alpha-hydroxyestrone + H(+) + H2O + oxidized [NADPH--hemoproteinreductase]",
            "targ_desciption": "A cytochrome P450 monooxygenase involved in the metabolism ofvarious endogenous substrates, including fatty acids, steroid hormonesand vitamins (PubMed:7574697, PubMed:11093772, PubMed:14559847,PubMed:15766564, PubMed:19965576). Mechanistically, uses molecularoxygen inserting one oxygen atom into a substrate, and reducing thesecond into a water molecule, with two electrons provided by NADPH viacytochrome P450 reductase (NADPH--hemoprotein reductase)(PubMed:7574697, PubMed:11093772, PubMed:14559847, PubMed:15766564,PubMed:19965576). Primarily catalyzes the epoxidation of double bondsof polyunsaturated fatty acids (PUFA) with a preference for the lastdouble bond (PubMed:7574697, PubMed:15766564, PubMed:19965576).Catalyzes the hydroxylation of carbon-hydrogen bonds. Metabolizes alltrans-retinoic acid toward its 4-hydroxylated form (PubMed:11093772).Displays 16-alpha hydroxylase activity toward estrogen steroidhormones, 17beta-estradiol (E2) and estrone (E1) (PubMed:14559847).Plays a role in the oxidative metabolism of xenobiotics. It is theprincipal enzyme responsible for the metabolism of the anti-cancer drugpaclitaxel (taxol) (PubMed:26427316). {ECO:0000269|PubMed:11093772,ECO:0000269|PubMed:14559847, ECO:0000269|PubMed:15766564,ECO:0000269|PubMed:19965576, ECO:0000269|PubMed:26427316,ECO:0000269|PubMed:7574697}.",
            "references": []
        },
        {
            "targ_id": "T064",
            "parent_targ_id": "T",
            "full_name": "Cytochrome P450 2D6",
            "abbrev": "CYPIID6",
            "protein_names": "Cytochrome P450 2D6 (EC 1.14.14.-) (CYPIID6) (Cholesterol 25-hydroxylase) (Cytochrome P450-DB1) (Debrisoquine 4-hydroxylase)",
            "related_func_ids": "F02060105; F020604",
            "category": "enzyme",
            "subcategories": "Monooxygenase, Oxidoreductase",
            "Uniport_ID": "P10635",
            "Uniprot_name": "CP2D6_HUMAN",
            "EC_numbers": "1.14.14.-",
            "gene_symbol": "CYP2D6",
            "gene_synonyms": "CYP2DL1",
            "gene_synonyms_links": "",
            "gene_name": "",
            "hgnc_id": "",
            "entrez_id": "",
            "ensembl_id": "",
            "omim_id": "",
            "genecard_link": "",
            "locs": "Endoplasmic reticulum membrane; Peripheral membrane protein; Microsome membrane; Peripheral membrane protein",
            "reaction": "(5Z,8Z,11Z,14Z)-eicosatetraenoate + O2 + reduced [NADPH--hemoprotein reductase] = (8R,9S)-epoxy-(5Z,11Z,14Z)-eicosatrienoate +H(+) + H2O + oxidized [NADPH--hemoprotein reductase]; (5Z,8Z,11Z,14Z)-eicosatetraenoate + O2 + reduced [NADPH--hemoprotein reductase] = (11R,12S)-epoxy-(5Z,8Z,14Z)-eicosatrienoate+ H(+) + H2O + oxidized [NADPH--hemoprotein reductase]; (5Z,8Z,11Z,14Z)-eicosatetraenoate + O2 + reduced [NADPH--hemoprotein reductase] = (14S,15R)-epoxy-(5Z,8Z,11Z)-eicosatrienoate+ H(+) + H2O + oxidized [NADPH--hemoprotein reductase]; N-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-ethanolamine + O2 + reduced[NADPH--hemoprotein reductase] = H(+) + H2O + N-(8,9-epoxy-5Z,11Z,14Z-eicosatrienoyl)-ethanolamine + oxidized [NADPH--hemoprotein reductase]; N-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-ethanolamine + O2 + reduced[NADPH--hemoprotein reductase] = H(+) + H2O + N-(11,12-epoxy-5Z,8Z,14Z-eicosatrienoyl)-ethanolamine + oxidized [NADPH--hemoproteinreductase]; N-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-ethanolamine + O2 + reduced[NADPH--hemoprotein reductase] = H(+) + H2O + N-(14,15-epoxy-5Z,8Z,11Z-eicosatrienoyl)-ethanolamine + oxidized [NADPH--hemoproteinreductase]; N-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-ethanolamine + O2 + reduced[NADPH--hemoprotein reductase] = H(+) + H2O + N-(20-hydroxy-5Z,8Z,11Z,14Z-eicosatetraenoyl)-ethanolamine + oxidized [NADPH--hemoprotein reductase]; (5Z,8Z,11Z,14Z,17Z)-eicosapentaenoate + O2 + reduced [NADPH--hemoprotein reductase] = (17S,18R)-epoxy-(5Z,8Z,11Z,14Z)-eicosatetraenoate + H(+) + H2O + oxidized [NADPH--hemoproteinreductase]; (4Z,7Z,10Z,13Z,16Z,19Z)-docosahexaenoate + O2 + reduced[NADPH--hemoprotein reductase] = (19R,20S)-epoxy-(4Z,7Z,10Z,13Z,16Z)-docosapentaenoate + H(+) + H2O + oxidized [NADPH--hemoproteinreductase]; (4Z,7Z,10Z,13Z,16Z,19Z)-docosahexaenoate + O2 + reduced[NADPH--hemoprotein reductase] = (19S,20R)-epoxy-(4Z,7Z,10Z,13Z,16Z)-docosapentaenoate + H(+) + H2O + oxidized [NADPH--hemoproteinreductase]; cholesterol + O2 + reduced [NADPH--hemoprotein reductase] =25-hydroxycholesterol + H(+) + H2O + oxidized [NADPH--hemoproteinreductase]; all-trans-retinol + O2 + reduced [NADPH--hemoproteinreductase] = all-trans-retinal + H(+) + 2 H2O + oxidized [NADPH--hemoprotein reductase]",
            "targ_desciption": "A cytochrome P450 monooxygenase involved in the metabolism offatty acids, steroids and retinoids (PubMed:18698000, PubMed:19965576,PubMed:20972997, PubMed:21289075, PubMed:21576599). Mechanistically,uses molecular oxygen inserting one oxygen atom into a substrate, andreducing the second into a water molecule, with two electrons providedby NADPH via cytochrome P450 reductase (NADPH--hemoprotein reductase)(PubMed:18698000, PubMed:19965576, PubMed:20972997, PubMed:21289075,PubMed:21576599). Catalyzes the epoxidation of double bonds ofpolyunsaturated fatty acids (PUFA) (PubMed:19965576, PubMed:20972997).Metabolizes endocannabinoid arachidonoylethanolamide (anandamide) to20-hydroxyeicosatetraenoic acid ethanolamide (20-HETE-EA) and 8,9-,11,12-, and 14,15-epoxyeicosatrienoic acid ethanolamides (EpETrE-EAs),potentially modulating endocannabinoid system signaling(PubMed:18698000, PubMed:21289075). Catalyzes the hydroxylation ofcarbon-hydrogen bonds. Metabolizes cholesterol toward 25-hydroxycholesterol, a physiological regulator of cellular cholesterolhomeostasis (PubMed:21576599). Catalyzes the oxidative transformationsof all-trans retinol to all-trans retinal, a precursor for the activeform all-trans-retinoic acid (PubMed:10681376). Also involved in theoxidative metabolism of drugs such as antiarrhythmics, adrenoceptorantagonists, and tricyclic antidepressants.{ECO:0000269|PubMed:10681376, ECO:0000269|PubMed:16352597,ECO:0000269|PubMed:18698000, ECO:0000269|PubMed:19965576,ECO:0000269|PubMed:20972997, ECO:0000269|PubMed:21289075,ECO:0000269|PubMed:21576599}.",
            "references": []
        },
        {
            "targ_id": "T065",
            "parent_targ_id": "T",
            "full_name": "Cytochrome P450 1B1",
            "abbrev": "CYPIB1",
            "protein_names": "Cytochrome P450 1B1 (EC 1.14.14.1) (CYPIB1) (Hydroperoxy icosatetraenoate dehydratase) (EC 4.2.1.152)",
            "related_func_ids": "F020604; F0701",
            "category": "enzyme",
            "subcategories": "Lyase, Monooxygenase, Oxidoreductase",
            "Uniport_ID": "Q16678",
            "Uniprot_name": "CP1B1_HUMAN",
            "EC_numbers": "1.14.14.1; 4.2.1.152",
            "gene_symbol": "CYP1B1",
            "gene_synonyms": "",
            "gene_synonyms_links": "",
            "gene_name": "",
            "hgnc_id": "",
            "entrez_id": "",
            "ensembl_id": "ENSG00000138061",
            "omim_id": "",
            "genecard_link": "",
            "locs": "Endoplasmic reticulum membrane; Peripheral membrane protein; Microsome membrane; Peripheral membrane protein; Mitochondrion",
            "reaction": "an organic molecule + O2 + reduced [NADPH--hemoproteinreductase] = an alcohol + H(+) + H2O + oxidized [NADPH--hemoproteinreductase]; 17beta-estradiol + O2 + reduced [NADPH--hemoprotein reductase]= 2-hydroxy-17beta-estradiol + H(+) + H2O + oxidized [NADPH--hemoprotein reductase]; 17beta-estradiol + O2 + reduced [NADPH--hemoprotein reductase]= 4-hydroxy-17beta-estradiol + H(+) + H2O + oxidized [NADPH--hemoprotein reductase]; estrone + O2 + reduced [NADPH--hemoprotein reductase] = 2-hydroxyestrone + H(+) + H2O + oxidized [NADPH--hemoproteinreductase]; estrone + O2 + reduced [NADPH--hemoprotein reductase] = 4-hydroxyestrone + H(+) + H2O + oxidized [NADPH--hemoproteinreductase]; O2 + reduced [NADPH--hemoprotein reductase] + testosterone =6beta,17beta-dihydroxyandrost-4-en-3-one + H(+) + H2O + oxidized[NADPH--hemoprotein reductase]; O2 + progesterone + reduced [NADPH--hemoprotein reductase] =6beta-hydroxyprogesterone + H(+) + H2O + oxidized [NADPH--hemoproteinreductase]; O2 + progesterone + reduced [NADPH--hemoprotein reductase] =16alpha-hydroxyprogesterone + H(+) + H2O + oxidized [NADPH--hemoprotein reductase]; all-trans-retinol + O2 + reduced [NADPH--hemoproteinreductase] = all-trans-retinal + H(+) + 2 H2O + oxidized [NADPH--hemoprotein reductase]; all-trans-retinal + O2 + reduced [NADPH--hemoproteinreductase] = all-trans-retinoate + 2 H(+) + H2O + oxidized [NADPH--hemoprotein reductase]; (5Z,8Z,11Z,14Z)-eicosatetraenoate + O2 + reduced [NADPH--hemoprotein reductase] = (8R,9S)-epoxy-(5Z,11Z,14Z)-eicosatrienoate +H(+) + H2O + oxidized [NADPH--hemoprotein reductase]; (5Z,8Z,11Z,14Z)-eicosatetraenoate + O2 + reduced [NADPH--hemoprotein reductase] = (11R,12S)-epoxy-(5Z,8Z,14Z)-eicosatrienoate+ H(+) + H2O + oxidized [NADPH--hemoprotein reductase]; (5Z,8Z,11Z,14Z)-eicosatetraenoate + O2 + reduced [NADPH--hemoprotein reductase] = (11S,12R)-epoxy-(5Z,8Z,14Z)-eicosatrienoate+ H(+) + H2O + oxidized [NADPH--hemoprotein reductase]; (5Z,8Z,11Z,14Z)-eicosatetraenoate + O2 + reduced [NADPH--hemoprotein reductase] = (14R,15S)-epoxy-(5Z,8Z,11Z)-eicosatrienoate+ H(+) + H2O + oxidized [NADPH--hemoprotein reductase]; (5S)-hydroperoxy-(6E,8Z,11Z,14Z)-eicosatetraenoate = 5-oxo-(6E,8Z,11Z,14Z)-eicosatetraenoate + H2O; (12S)-hydroperoxy-(5Z,8Z,10E,14Z)-eicosatetraenoate = 12-oxo-(5Z,8Z,10E,14Z)-eicosatetraenoate + H2O; (13S)-hydroperoxy-(9Z,11E)-octadecadienoate = 13-oxo-(9Z,11E)-octadecadienoate + H2O; (15S)-hydroperoxy-(5Z,8Z,11Z,13E)-eicosatetraenoate = 15-oxo-(5Z,8Z,11Z,13E)-eicosatetraenoate + H2O",
            "targ_desciption": "A cytochrome P450 monooxygenase involved in the metabolism ofvarious endogenous substrates, including fatty acids, steroid hormonesand vitamins (PubMed:20972997, PubMed:11555828, PubMed:12865317,PubMed:10681376, PubMed:15258110). Mechanistically, uses molecularoxygen inserting one oxygen atom into a substrate, and reducing thesecond into a water molecule, with two electrons provided by NADPH viacytochrome P450 reductase (NADPH--hemoprotein reductase)(PubMed:20972997, PubMed:11555828, PubMed:12865317, PubMed:10681376,PubMed:15258110). Exhibits catalytic activity for the formation ofhydroxyestrogens from estrone (E1) and 17beta-estradiol (E2), namely2- and 4-hydroxy E1 and E2. Displays a predominant hydroxylase activitytoward E2 at the C-4 position (PubMed:11555828, PubMed:12865317).Metabolizes testosterone and progesterone to B or D ring hydroxylatedmetabolites (PubMed:10426814). May act as a major enzyme for all-transretinoic acid biosynthesis in extrahepatic tissues. Catalyzes twosuccessive oxidative transformation of all-trans retinol to all-transretinal and then to the active form all-trans retinoic acid(PubMed:10681376, PubMed:15258110). Catalyzes the epoxidation of doublebonds of certain PUFA. Converts arachidonic acid towardepoxyeicosatrienoic acid (EpETrE) regioisomers, 8,9-, 11,12-, and14,15- EpETrE, that function as lipid mediators in the vascular system(PubMed:20972997). Additionally, displays dehydratase activity towardoxygenated eicosanoids hydroperoxyeicosatetraenoates (HpETEs). Thisactivity is independent of cytochrome P450 reductase, NADPH, and O2(PubMed:21068195). Also involved in the oxidative metabolism ofxenobiotics, particularly converting polycyclic aromatic hydrocarbonsand heterocyclic aryl amines procarcinogens to DNA-damaging products(PubMed:10426814). Plays an important role in retinal vasculardevelopment. Under hyperoxic O2 conditions, promotes retinalangiogenesis and capillary morphogenesis, likely by metabolizing theoxygenated products generated during the oxidative stress. Also,contributes to oxidative homeostasis and ultrastructural organizationand function of trabecular meshwork tissue through modulation of POSTNexpression (By similarity). {ECO:0000250|UniProtKB:Q64429,ECO:0000269|PubMed:10426814, ECO:0000269|PubMed:10681376,ECO:0000269|PubMed:11555828, ECO:0000269|PubMed:12865317,ECO:0000269|PubMed:15258110, ECO:0000269|PubMed:20972997,ECO:0000269|PubMed:21068195}.",
            "references": []
        },
        {
            "targ_id": "T066",
            "parent_targ_id": "T",
            "full_name": "Solute carrier family 2, facilitated glucose transporter member 1",
            "abbrev": "GLUT-1",
            "protein_names": "Solute carrier family 2, facilitated glucose transporter member 1 (Glucose transporter type 1, erythrocyte/brain) (GLUT-1) (HepG2 glucose transporter)",
            "related_func_ids": "F02110115",
            "category": "protein",
            "subcategories": "transporter",
            "Uniport_ID": "P11166",
            "Uniprot_name": "GTR1_HUMAN",
            "EC_numbers": "",
            "gene_symbol": "SLC2A1",
            "gene_synonyms": "GLUT1",
            "gene_synonyms_links": "",
            "gene_name": "",
            "hgnc_id": "",
            "entrez_id": "",
            "ensembl_id": "",
            "omim_id": "",
            "genecard_link": "",
            "locs": "Cell membrane; Multi-pass membrane protein; Melanosome",
            "reaction": "D-glucose(out) = D-glucose(in)",
            "targ_desciption": "Facilitative glucose transporter, which is responsible forconstitutive or basal glucose uptake (PubMed:18245775, PubMed:19449892,PubMed:25982116, PubMed:27078104, PubMed:10227690). Has a very broadsubstrate specificity. can transport a wide range of aldoses includingboth pentoses and hexoses (PubMed:18245775, PubMed:19449892). Mostimportant energy carrier of the brain: present at the blood-brainbarrier and assures the energy-independent, facilitative transport ofglucose into the brain (PubMed:10227690). {ECO:0000269|PubMed:10227690,ECO:0000269|PubMed:18245775, ECO:0000269|PubMed:19449892,ECO:0000269|PubMed:25982116, ECO:0000269|PubMed:27078104}.",
            "references": []
        },
        {
            "targ_id": "T067",
            "parent_targ_id": "T",
            "full_name": "Hexokinase-1",
            "abbrev": "HK I",
            "protein_names": "Hexokinase-1 (EC 2.7.1.1) (Brain form hexokinase) (Hexokinase type I) (HK I) (Hexokinase-A)",
            "related_func_ids": "F020401",
            "category": "enzyme",
            "subcategories": "Allosteric enzyme, Kinase, Transferase",
            "Uniport_ID": "P19367",
            "Uniprot_name": "HXK1_HUMAN",
            "EC_numbers": "2.7.1.1",
            "gene_symbol": "HK1",
            "gene_synonyms": "",
            "gene_synonyms_links": "",
            "gene_name": "",
            "hgnc_id": "",
            "entrez_id": "",
            "ensembl_id": "ENSG00000156515",
            "omim_id": "",
            "genecard_link": "",
            "locs": "Mitochondrion outer membrane; Peripheral membrane protein; Cytoplasm, cytosol",
            "reaction": "ATP + D-hexose = ADP + D-hexose 6-phosphate + H(+); ATP + D-fructose = ADP + D-fructose 6-phosphate + H(+); ATP + D-glucose = ADP + D-glucose 6-phosphate + H(+); ATP + D-mannose = ADP + D-mannose 6-phosphate + H(+); ATP + D-glucosamine = ADP + D-glucosamine 6-phosphate + H(+)",
            "targ_desciption": "Catalyzes the phosphorylation of various hexoses, such as D-glucose, D-glucosamine, D-fructose, D-mannose and 2-deoxy-D-glucose, tohexose 6-phosphate (D-glucose 6-phosphate, D-glucosamine 6-phosphate,D-fructose 6-phosphate, D-mannose 6-phosphate and 2-deoxy-D-glucose 6-phosphate, respectively) (PubMed:1637300, PubMed:25316723,PubMed:27374331). Does not phosphorylate N-acetyl-D-glucosamine(PubMed:27374331). Mediates the initial step of glycolysis bycatalyzing phosphorylation of D-glucose to D-glucose 6-phosphate (Bysimilarity). Involved in innate immunity and inflammation by acting asa pattern recognition receptor for bacterial peptidoglycan(PubMed:27374331). When released in the cytosol, N-acetyl-D-glucosaminecomponent of bacterial peptidoglycan inhibits the hexokinase activityof HK1 and causes its dissociation from mitochondrial outer membrane,thereby activating the NLRP3 inflammasome (PubMed:27374331).{ECO:0000250|UniProtKB:P05708, ECO:0000269|PubMed:1637300,ECO:0000269|PubMed:25316723, ECO:0000269|PubMed:27374331}.",
            "references": [
                "RC03684",
                "RC03686",
                "RC03687"
            ]
        },
        {
            "targ_id": "T068",
            "parent_targ_id": "T",
            "full_name": "Glucose-6-phosphate isomerase",
            "abbrev": "GPI",
            "protein_names": "Glucose-6-phosphate isomerase (GPI) (EC 5.3.1.9) (Autocrine motility factor) (AMF) (Neuroleukin) (NLK) (Phosphoglucose isomerase) (PGI) (Phosphohexose isomerase) (PHI) (Sperm antigen 36) (SA-36)",
            "related_func_ids": "F020401",
            "category": "enzyme",
            "subcategories": "Cytokine, Growth factor, Isomerase",
            "Uniport_ID": "P06744",
            "Uniprot_name": "G6PI_HUMAN",
            "EC_numbers": "5.3.1.9",
            "gene_symbol": "GPI",
            "gene_synonyms": "",
            "gene_synonyms_links": "",
            "gene_name": "",
            "hgnc_id": "",
            "entrez_id": "",
            "ensembl_id": "",
            "omim_id": "",
            "genecard_link": "",
            "locs": "Cytoplasm; Secreted",
            "reaction": "aldehydo-D-glucose 6-phosphate = keto-D-fructose 6-phosphate",
            "targ_desciption": "In the cytoplasm, catalyzes the conversion of glucose-6-phosphate to fructose-6-phosphate, the second step in glycolysis, andthe reverse reaction during gluconeogenesis (PubMed:28803808). Besidesit's role as a glycolytic enzyme, also acts as a secreted cytokine:acts as an angiogenic factor (AMF) that stimulates endothelial cellmotility (PubMed:11437381). Acts as a neurotrophic factor, neuroleukin,for spinal and sensory neurons (PubMed:3352745, PubMed:11004567). It issecreted by lectin-stimulated T-cells and induces immunoglobulinsecretion (PubMed:3352745, PubMed:11004567).{ECO:0000269|PubMed:11004567, ECO:0000269|PubMed:11437381,ECO:0000269|PubMed:28803808, ECO:0000269|PubMed:3352745}.",
            "references": []
        },
        {
            "targ_id": "T069",
            "parent_targ_id": "T",
            "full_name": "Phosphofructokinase",
            "abbrev": "PFK",
            "protein_names": "",
            "related_func_ids": "F020401",
            "category": "enzyme family",
            "subcategories": "",
            "Uniport_ID": "",
            "Uniprot_name": "",
            "EC_numbers": "2.7.1.11",
            "gene_symbol": "PFK",
            "gene_synonyms": "",
            "gene_synonyms_links": "",
            "gene_name": "",
            "hgnc_id": "",
            "entrez_id": "",
            "ensembl_id": "",
            "omim_id": "",
            "genecard_link": "",
            "locs": "",
            "reaction": "",
            "targ_desciption": "",
            "references": []
        },
        {
            "targ_id": "T069001",
            "parent_targ_id": "T069",
            "full_name": "ATP-dependent 6-phosphofructokinase, liver type",
            "abbrev": "PFK-L",
            "protein_names": "ATP-dependent 6-phosphofructokinase, liver type",
            "related_func_ids": "F020401",
            "category": "enzyme",
            "subcategories": "Allosteric enzyme, Kinase, Transferase",
            "Uniport_ID": "P17858",
            "Uniprot_name": "PFKAL_HUMAN",
            "EC_numbers": "2.7.1.11",
            "gene_symbol": "PFKL",
            "gene_synonyms": "",
            "gene_synonyms_links": "",
            "gene_name": "",
            "hgnc_id": "",
            "entrez_id": "",
            "ensembl_id": "ENSG00000141959",
            "omim_id": "",
            "genecard_link": "",
            "locs": "Cytoplasm",
            "reaction": "ATP + beta-D-fructose 6-phosphate = ADP + beta-D-fructose 1,6-bisphosphate + H+",
            "targ_desciption": "Catalyzes the phosphorylation of D-fructose 6-phosphate to fructose 1,6-bisphosphate by ATP, the first committing step of glycolysis (PubMed:22923583). Negatively regulates the phagocyte oxidative burst in response to bacterial infection by controlling cellular NADPH biosynthesis and NADPH oxidase-derived reactive oxygen species. Upon macrophage activation, drives the metabolic switch toward glycolysis, thus preventing glucose turnover that produces NADPH via pentose phosphate pathway (By similarity).",
            "references": []
        },
        {
            "targ_id": "T069002",
            "parent_targ_id": "T069",
            "full_name": "ATP-dependent 6-phosphofructokinase, muscle type",
            "abbrev": "PFK-M",
            "protein_names": "ATP-dependent 6-phosphofructokinase, muscle type",
            "related_func_ids": "F020401",
            "category": "enzyme",
            "subcategories": "Allosteric enzyme, Kinase, Transferase",
            "Uniport_ID": "P08237",
            "Uniprot_name": "PFKAM_HUMAN",
            "EC_numbers": "2.7.1.11",
            "gene_symbol": "PFKM",
            "gene_synonyms": "",
            "gene_synonyms_links": "",
            "gene_name": "",
            "hgnc_id": "",
            "entrez_id": "",
            "ensembl_id": "",
            "omim_id": "",
            "genecard_link": "",
            "locs": "Cytoplasm",
            "reaction": "ATP + beta-D-fructose 6-phosphate = ADP + beta-D-fructose 1,6-bisphosphate + H+",
            "targ_desciption": "Catalyzes the phosphorylation of D-fructose 6-phosphate to fructose 1,6-bisphosphate by ATP, the first committing step of glycolysis.",
            "references": []
        },
        {
            "targ_id": "T069003",
            "parent_targ_id": "T069",
            "full_name": "ATP-dependent 6-phosphofructokinase, platelet type",
            "abbrev": "PFK-P",
            "protein_names": "ATP-dependent 6-phosphofructokinase, platelet type",
            "related_func_ids": "F020401",
            "category": "enzyme",
            "subcategories": "Allosteric enzyme, Kinase, Transferase",
            "Uniport_ID": "Q01813",
            "Uniprot_name": "PFKAP_HUMAN",
            "EC_numbers": "2.7.1.11",
            "gene_symbol": "PFKP",
            "gene_synonyms": "",
            "gene_synonyms_links": "",
            "gene_name": "",
            "hgnc_id": "",
            "entrez_id": "",
            "ensembl_id": "",
            "omim_id": "",
            "genecard_link": "",
            "locs": "Cytoplasm",
            "reaction": "ATP + beta-D-fructose 6-phosphate = ADP + beta-D-fructose 1,6-bisphosphate + H+",
            "targ_desciption": "Catalyzes the phosphorylation of D-fructose 6-phosphate to fructose 1,6-bisphosphate by ATP, the first committing step of glycolysis.",
            "references": []
        },
        {
            "targ_id": "T070",
            "parent_targ_id": "T",
            "full_name": "Fructose-bisphosphate aldolase",
            "abbrev": "ALDO",
            "protein_names": "",
            "related_func_ids": "F020401",
            "category": "enzyme family",
            "subcategories": "",
            "Uniport_ID": "",
            "Uniprot_name": "",
            "EC_numbers": "4.1.2.13",
            "gene_symbol": "",
            "gene_synonyms": "",
            "gene_synonyms_links": "",
            "gene_name": "",
            "hgnc_id": "",
            "entrez_id": "",
            "ensembl_id": "",
            "omim_id": "",
            "genecard_link": "",
            "locs": "",
            "reaction": "",
            "targ_desciption": "",
            "references": []
        },
        {
            "targ_id": "T070001",
            "parent_targ_id": "T070",
            "full_name": "Fructose-bisphosphate aldolase A",
            "abbrev": "ALDOA",
            "protein_names": "Fructose-bisphosphate aldolase A (EC 4.1.2.13) (Lung cancer antigen NY-LU-1) (Muscle-type aldolase)",
            "related_func_ids": "F020401",
            "category": "enzyme",
            "subcategories": "Lyase",
            "Uniport_ID": "P04075",
            "Uniprot_name": "ALDOA_HUMAN",
            "EC_numbers": "4.1.2.13",
            "gene_symbol": "ALDOA ALDA",
            "gene_synonyms": "",
            "gene_synonyms_links": "",
            "gene_name": "",
            "hgnc_id": "",
            "entrez_id": "",
            "ensembl_id": "",
            "omim_id": "",
            "genecard_link": "",
            "locs": "Cytoplasm, myofibril, sarcomere, I band; Cytoplasm, myofibril, sarcomere, M line",
            "reaction": "beta-D-fructose 1,6-bisphosphate = D-glyceraldehyde 3-phosphate + dihydroxyacetone phosphate",
            "targ_desciption": "Plays a key role in glycolysis and gluconeogenesis. Inaddition, may also function as scaffolding protein (By similarity).{ECO:0000250}.",
            "references": []
        },
        {
            "targ_id": "T070002",
            "parent_targ_id": "T070",
            "full_name": "Fructose-bisphosphate aldolase B",
            "abbrev": "ALDOB",
            "protein_names": "Fructose-bisphosphate aldolase B (EC 4.1.2.13) (Liver-type aldolase)",
            "related_func_ids": "F020401",
            "category": "enzyme",
            "subcategories": "Lyase",
            "Uniport_ID": "P05062",
            "Uniprot_name": "ALDOB_HUMAN",
            "EC_numbers": "4.1.2.13",
            "gene_symbol": "ALDOB ALDB",
            "gene_synonyms": "",
            "gene_synonyms_links": "",
            "gene_name": "",
            "hgnc_id": "",
            "entrez_id": "",
            "ensembl_id": "",
            "omim_id": "",
            "genecard_link": "",
            "locs": "Cytoplasm, cytoskeleton, microtubule organizingcenter, centrosome, centriolar satellite",
            "reaction": "beta-D-fructose 1,6-bisphosphate = D-glyceraldehyde 3-phosphate + dihydroxyacetone phosphate",
            "targ_desciption": "",
            "references": []
        },
        {
            "targ_id": "T071",
            "parent_targ_id": "T",
            "full_name": "Triosephosphate isomerase",
            "abbrev": "TPI",
            "protein_names": "Triosephosphate isomerase (TIM) (EC 5.3.1.1) (Methylglyoxal synthase) (EC 4.2.3.3) (Triose-phosphate isomerase)",
            "related_func_ids": "F020401",
            "category": "enzyme",
            "subcategories": "Isomerase, Lyase",
            "Uniport_ID": "P60174",
            "Uniprot_name": "TPIS_HUMAN",
            "EC_numbers": "5.3.1.1; 4.2.3.3",
            "gene_symbol": "TPI1 TPI",
            "gene_synonyms": "",
            "gene_synonyms_links": "",
            "gene_name": "",
            "hgnc_id": "",
            "entrez_id": "",
            "ensembl_id": "",
            "omim_id": "",
            "genecard_link": "",
            "locs": "Cytoplasm",
            "reaction": "D-glyceraldehyde 3-phosphate = dihydroxyacetone phosphate; dihydroxyacetone phosphate = methylglyoxal + phosphate",
            "targ_desciption": "Triosephosphate isomerase is an extremely efficient metabolicenzyme that catalyzes the interconversion between dihydroxyacetonephosphate (DHAP) and D-glyceraldehyde-3-phosphate (G3P) in glycolysisand gluconeogenesis. {ECO:0000269|PubMed:18562316}.; It is also responsible for the non-negligible production ofmethylglyoxal a reactive cytotoxic side-product that modifies and canalter proteins, DNA and lipids. {ECO:0000250|UniProtKB:P00939}.",
            "references": []
        },
        {
            "targ_id": "T072",
            "parent_targ_id": "T",
            "full_name": "Glyceraldehyde-3-phosphate dehydrogenase",
            "abbrev": "G3P",
            "protein_names": "Glyceraldehyde-3-phosphate dehydrogenase (GAPDH) (EC 1.2.1.12) (Peptidyl-cysteine S-nitrosylase GAPDH) (EC 2.6.99.-)",
            "related_func_ids": "F020401",
            "category": "enzyme",
            "subcategories": "Oxidoreductase, Transferase",
            "Uniport_ID": "P04406",
            "Uniprot_name": "G3P_HUMAN",
            "EC_numbers": "1.2.1.12; 2.6.99.-",
            "gene_symbol": "GAPDH GAPD CDABP0047 OK/SW-cl.12",
            "gene_synonyms": "",
            "gene_synonyms_links": "",
            "gene_name": "",
            "hgnc_id": "",
            "entrez_id": "",
            "ensembl_id": "",
            "omim_id": "",
            "genecard_link": "",
            "locs": "Cytoplasm, cytosol; Nucleus; Cytoplasm, perinuclear region; Membrane; Cytoplasm, cytoskeleton; Postnuclear and Perinuclear regions",
            "reaction": "D-glyceraldehyde 3-phosphate + NAD(+) + phosphate = (2R)-3-phospho-glyceroyl phosphate + H(+) + NADH",
            "targ_desciption": "Has both glyceraldehyde-3-phosphate dehydrogenase andnitrosylase activities, thereby playing a role in glycolysis andnuclear functions, respectively. Participates in nuclear eventsincluding transcription, RNA transport, DNA replication and apoptosis.Nuclear functions are probably due to the nitrosylase activity thatmediates cysteine S-nitrosylation of nuclear target proteins such asSIRT1, HDAC2 and PRKDC. Modulates the organization and assembly of thecytoskeleton. Facilitates the CHP1-dependent microtubule and membraneassociations through its ability to stimulate the binding of CHP1 tomicrotubules (By similarity). Glyceraldehyde-3-phosphate dehydrogenaseis a key enzyme in glycolysis that catalyzes the first step of thepathway by converting D-glyceraldehyde 3-phosphate (G3P) into 3-phospho-D-glyceroyl phosphate. Component of the GAIT (gamma interferon-activated inhibitor of translation) complex which mediates interferon-gamma-induced transcript-selective translation inhibition ininflammation processes. Upon interferon-gamma treatment assembles intothe GAIT complex which binds to stem loop-containing GAIT elements inthe 3'-UTR of diverse inflammatory mRNAs (such as ceruplasmin) andsuppresses their translation. {ECO:0000250,ECO:0000269|PubMed:11724794, ECO:0000269|PubMed:23071094,ECO:0000269|PubMed:3170585}.",
            "references": [
                "RC03809",
                "RC03810"
            ]
        },
        {
            "targ_id": "T073",
            "parent_targ_id": "T",
            "full_name": "Phosphoglycerate kinase",
            "abbrev": "PGK",
            "protein_names": "Phosphoglycerate kinase 1 (EC 2.7.2.3) (Cell migration-inducing gene 10 protein) (Primer recognition protein 2) (PRP 2)",
            "related_func_ids": "F020401",
            "category": "enzyme",
            "subcategories": "Kinase, Transferase",
            "Uniport_ID": "P00558",
            "Uniprot_name": "PGK1_HUMAN",
            "EC_numbers": "2.7.2.3",
            "gene_symbol": "PGK1 PGKA MIG10 OK/SW-cl.110",
            "gene_synonyms": "",
            "gene_synonyms_links": "",
            "gene_name": "",
            "hgnc_id": "",
            "entrez_id": "",
            "ensembl_id": "",
            "omim_id": "",
            "genecard_link": "",
            "locs": "Cytoplasm",
            "reaction": "(2R)-3-phosphoglycerate + ATP = (2R)-3-phospho-glyceroylphosphate + ADP",
            "targ_desciption": "Catalyzes one of the two ATP producing reactions in theglycolytic pathway via the reversible conversion of 1,3-diphosphoglycerate to 3-phosphoglycerate (PubMed:30323285,PubMed:7391028). In addition to its role as a glycolytic enzyme, itseems that PGK-1 acts as a polymerase alpha cofactor protein (primerrecognition protein) (PubMed:2324090). May play a role in spermmotility (PubMed:26677959). {ECO:0000269|PubMed:2324090,ECO:0000269|PubMed:26677959, ECO:0000269|PubMed:30323285,ECO:0000269|PubMed:7391028}.",
            "references": []
        },
        {
            "targ_id": "T074",
            "parent_targ_id": "T",
            "full_name": "Phosphoglycerate mutase",
            "abbrev": "PGM",
            "protein_names": "Phosphoglucomutase-1 (PGM 1) (EC 5.4.2.2) (Glucose phosphomutase 1)",
            "related_func_ids": "F020401",
            "category": "enzyme",
            "subcategories": "Isomerase",
            "Uniport_ID": "P36871",
            "Uniprot_name": "PGM1_HUMAN",
            "EC_numbers": "5.4.2.2",
            "gene_symbol": "PGM1",
            "gene_synonyms": "",
            "gene_synonyms_links": "",
            "gene_name": "",
            "hgnc_id": "",
            "entrez_id": "",
            "ensembl_id": "",
            "omim_id": "",
            "genecard_link": "",
            "locs": "[Isoform 1]: Cytoplasm",
            "reaction": "alpha-D-glucose 1-phosphate = alpha-D-glucose 6-phosphate",
            "targ_desciption": "This enzyme participates in both the breakdown and synthesisof glucose.",
            "references": []
        },
        {
            "targ_id": "T075",
            "parent_targ_id": "T",
            "full_name": "enolase",
            "abbrev": "ENO",
            "protein_names": "Alpha-enolase (EC 4.2.1.11) (2-phospho-D-glycerate hydro-lyase) (C-myc promoter-binding protein) (Enolase 1) (MBP-1) (MPB-1) (Non-neural enolase) (NNE) (Phosphopyruvate hydratase) (Plasminogen-binding protein)",
            "related_func_ids": "F020401",
            "category": "enzyme",
            "subcategories": "Lyase",
            "Uniport_ID": "P06733",
            "Uniprot_name": "ENOA_HUMAN",
            "EC_numbers": "4.2.1.11",
            "gene_symbol": "ENO1 ENO1L1 MBPB1 MPB1",
            "gene_synonyms": "",
            "gene_synonyms_links": "",
            "gene_name": "",
            "hgnc_id": "",
            "entrez_id": "",
            "ensembl_id": "",
            "omim_id": "",
            "genecard_link": "",
            "locs": "Cytoplasm; Cell membrane; Cytoplasm, myofibril,sarcomere, M line; ENO1 is localized to the M line; [Isoform MBP-1]: Nucleus",
            "reaction": "(2R)-2-phosphoglycerate = H2O + phosphoenolpyruvate",
            "targ_desciption": "Glycolytic enzyme the catalyzes the conversion of 2-phosphoglycerate to phosphoenolpyruvate (PubMed:29775581,PubMed:1369209). In addition to glycolysis, involved in variousprocesses such as growth control, hypoxia tolerance and allergicresponses (PubMed:2005901, PubMed:10802057, PubMed:12666133,PubMed:29775581). May also function in the intravascular andpericellular fibrinolytic system due to its ability to serve as areceptor and activator of plasminogen on the cell surface of severalcell-types such as leukocytes and neurons (PubMed:12666133). Stimulatesimmunoglobulin production (PubMed:1369209).{ECO:0000269|PubMed:10802057, ECO:0000269|PubMed:12666133,ECO:0000269|PubMed:1369209, ECO:0000269|PubMed:2005901,ECO:0000269|PubMed:29775581}.; MBP1 binds to the myc promoter and acts as a transcriptionalrepressor. May be a tumor suppressor. {ECO:0000269|PubMed:10082554}.",
            "references": []
        },
        {
            "targ_id": "T076",
            "parent_targ_id": "T",
            "full_name": "Lactate dehydrogenase",
            "abbrev": "LDH",
            "protein_names": "",
            "related_func_ids": "F020201; F020401; F0701",
            "category": "enzyme",
            "subcategories": "",
            "Uniport_ID": "",
            "Uniprot_name": "",
            "EC_numbers": "1.1.1.27",
            "gene_symbol": "",
            "gene_synonyms": "",
            "gene_synonyms_links": "",
            "gene_name": "",
            "hgnc_id": "",
            "entrez_id": "",
            "ensembl_id": "",
            "omim_id": "",
            "genecard_link": "",
            "locs": "",
            "reaction": "",
            "targ_desciption": "",
            "references": [
                "RC00564",
                "RC00565",
                "RC00566",
                "RC00567",
                "RC00568",
                "RC00569",
                "RC00570",
                "RC00571",
                "RC00572",
                "RC00573",
                "RC00574",
                "RC00575",
                "RC00576",
                "RC00577",
                "RC00578",
                "RC00579",
                "RC00580",
                "RC00581",
                "RC00582",
                "RC00583",
                "RC00584",
                "RC00585",
                "RC00586",
                "RC00587",
                "RC00588",
                "RC00589",
                "RC00590",
                "RC00591",
                "RC00592",
                "RC00593"
            ]
        },
        {
            "targ_id": "T076001",
            "parent_targ_id": "T076",
            "full_name": "L-lactate dehydrogenase A chain (LDH-A) (EC 1.1.1.27) (Cell proliferation-inducing gene 19 protein) (LDH muscle subunit) (LDH-M) (Renal carcinoma antigen NY-REN-59)",
            "abbrev": "LDHA",
            "protein_names": "L-lactate dehydrogenase A chain (LDH-A) (EC 1.1.1.27) (Cell proliferation-inducing gene 19 protein) (LDH muscle subunit) (LDH-M) (Renal carcinoma antigen NY-REN-59)",
            "related_func_ids": "F020201; F020401; F0701",
            "category": "protein subunit",
            "subcategories": "Oxidoreductase",
            "Uniport_ID": "P00338",
            "Uniprot_name": "LDHA_HUMAN",
            "EC_numbers": "1.1.1.27",
            "gene_symbol": "LDHA PIG19",
            "gene_synonyms": "",
            "gene_synonyms_links": "",
            "gene_name": "",
            "hgnc_id": "",
            "entrez_id": "",
            "ensembl_id": "",
            "omim_id": "",
            "genecard_link": "",
            "locs": "Cytoplasm",
            "reaction": "(S)-lactate + NAD(+) = H(+) + NADH + pyruvate",
            "targ_desciption": "",
            "references": []
        },
        {
            "targ_id": "T076002",
            "parent_targ_id": "T076",
            "full_name": "L-lactate dehydrogenase A-like 6B (EC 1.1.1.27)",
            "abbrev": "LDHAL6",
            "protein_names": "L-lactate dehydrogenase A-like 6B (EC 1.1.1.27)",
            "related_func_ids": "F020201",
            "category": "protein subunit",
            "subcategories": "Oxidoreductase",
            "Uniport_ID": "Q9BYZ2",
            "Uniprot_name": "LDH6B_HUMAN",
            "EC_numbers": "1.1.1.27",
            "gene_symbol": "LDHAL6B",
            "gene_synonyms": "LDH6B, LDHAL6, LDHL",
            "gene_synonyms_links": "",
            "gene_name": "Lactate dehydrogenase A like 6B",
            "hgnc_id": "",
            "entrez_id": "",
            "ensembl_id": "ENSG00000171989",
            "omim_id": "",
            "genecard_link": "",
            "locs": "",
            "reaction": "(S)-lactate + NAD(+) = H(+) + NADH + pyruvate",
            "targ_desciption": "",
            "references": []
        },
        {
            "targ_id": "T076003",
            "parent_targ_id": "T076",
            "full_name": "L-lactate dehydrogenase B chain (LDH-B) (EC 1.1.1.27) (LDH heart subunit) (LDH-H) (Renal carcinoma antigen NY-REN-46)",
            "abbrev": "LDHB",
            "protein_names": "L-lactate dehydrogenase B chain (LDH-B) (EC 1.1.1.27) (LDH heart subunit) (LDH-H) (Renal carcinoma antigen NY-REN-46)",
            "related_func_ids": "F020201; F020401; F0701",
            "category": "protein subunit",
            "subcategories": "Oxidoreductase",
            "Uniport_ID": "P07195",
            "Uniprot_name": "LDHB_HUMAN",
            "EC_numbers": "1.1.1.27",
            "gene_symbol": "LDHB",
            "gene_synonyms": "",
            "gene_synonyms_links": "",
            "gene_name": "",
            "hgnc_id": "",
            "entrez_id": "",
            "ensembl_id": "",
            "omim_id": "",
            "genecard_link": "",
            "locs": "Cytoplasm",
            "reaction": "(S)-lactate + NAD(+) = H(+) + NADH + pyruvate",
            "targ_desciption": "",
            "references": []
        },
        {
            "targ_id": "T076004",
            "parent_targ_id": "T076",
            "full_name": "L-lactate dehydrogenase C chain (LDH-C) (EC 1.1.1.27) (Cancer/testis antigen 32) (CT32) (LDH testis subunit) (LDH-X)",
            "abbrev": "LDHC",
            "protein_names": "L-lactate dehydrogenase C chain (LDH-C) (EC 1.1.1.27) (Cancer/testis antigen 32) (CT32) (LDH testis subunit) (LDH-X)",
            "related_func_ids": "F020201; F020401; F0701",
            "category": "protein subunit",
            "subcategories": "Oxidoreductase",
            "Uniport_ID": "P07864",
            "Uniprot_name": "LDHC_HUMAN",
            "EC_numbers": "1.1.1.27",
            "gene_symbol": "LDHC LDH3 LDHX",
            "gene_synonyms": "",
            "gene_synonyms_links": "",
            "gene_name": "",
            "hgnc_id": "",
            "entrez_id": "",
            "ensembl_id": "",
            "omim_id": "",
            "genecard_link": "",
            "locs": "Cytoplasm",
            "reaction": "(S)-lactate + NAD(+) = H(+) + NADH + pyruvate",
            "targ_desciption": "Possible role in sperm motility.",
            "references": []
        },
        {
            "targ_id": "T077",
            "parent_targ_id": "T",
            "full_name": "lactate",
            "abbrev": "",
            "protein_names": "",
            "related_func_ids": "",
            "category": "metabolite",
            "subcategories": "",
            "Uniport_ID": "",
            "Uniprot_name": "",
            "EC_numbers": "",
            "gene_symbol": "",
            "gene_synonyms": "",
            "gene_synonyms_links": "",
            "gene_name": "",
            "hgnc_id": "",
            "entrez_id": "",
            "ensembl_id": "",
            "omim_id": "",
            "genecard_link": "",
            "locs": "",
            "reaction": "",
            "targ_desciption": "",
            "references": [
                "RC00680",
                "RC00681"
            ]
        },
        {
            "targ_id": "T078",
            "parent_targ_id": "T",
            "full_name": "Acetyl-coenzyme A synthetase 2-like, mitochondrial",
            "abbrev": "Acetate--CoA ligase 2",
            "protein_names": "Acetyl-coenzyme A synthetase 2-like, mitochondrial (EC 6.2.1.1) (Acetate--CoA ligase 2) (Acetyl-CoA synthetase 2) (AceCS2) (Acyl-CoA synthetase short-chain family member 1) (Propionate--CoA ligase) (EC 6.2.1.17)",
            "related_func_ids": "F02060105",
            "category": "enzyme",
            "subcategories": "ligase",
            "Uniport_ID": "Q9NUB1",
            "Uniprot_name": "ACS2L_HUMAN",
            "EC_numbers": "6.2.1.1; 6.2.1.17",
            "gene_symbol": "ACSS1",
            "gene_synonyms": "ACAS2L, AceCS2L, dJ568C11.3, MGC33843",
            "gene_synonyms_links": "",
            "gene_name": "Acyl-CoA synthetase short chain family member 1",
            "hgnc_id": "",
            "entrez_id": "",
            "ensembl_id": "ENSG00000154930",
            "omim_id": "",
            "genecard_link": "",
            "locs": "Mitochondrion matrix",
            "reaction": "acetate + ATP + CoA = acetyl-CoA + AMP + diphosphate; ATP + CoA + propanoate = AMP + diphosphate + propanoyl-CoA",
            "targ_desciption": "Catalyzes the synthesis of acetyl-CoA from short-chain fattyacids (PubMed:16788062). Acetate is the preferred substrate(PubMed:16788062). Can also utilize propionate with a much loweraffinity (By similarity). Provides acetyl-CoA that is utilized mainlyfor oxidation under ketogenic conditions (By similarity). Involved inthermogenesis under ketogenic conditions, using acetate as a vital fuelwhen carbohydrate availability is insufficient (By similarity).{ECO:0000250|UniProtKB:Q99NB1, ECO:0000269|PubMed:16788062}.",
            "references": []
        },
        {
            "targ_id": "T079",
            "parent_targ_id": "T",
            "full_name": "Sorbitol dehydrogenase",
            "abbrev": "SDH",
            "protein_names": "Sorbitol dehydrogenase (SDH) (EC 1.1.1.-) ((R,R)-butanediol dehydrogenase) (EC 1.1.1.4) (L-iditol 2-dehydrogenase) (EC 1.1.1.14) (Polyol dehydrogenase) (Ribitol dehydrogenase) (RDH) (EC 1.1.1.56) (Xylitol dehydrogenase) (XDH) (EC 1.1.1.9)",
            "related_func_ids": "F022401",
            "category": "enzyme",
            "subcategories": "Oxidoreductase",
            "Uniport_ID": "Q00796",
            "Uniprot_name": "DHSO_HUMAN",
            "EC_numbers": "1.1.1.-; 1.1.1.4; 1.1.1.14; 1.1.1.56; 1.1.1.9",
            "gene_symbol": "SORD",
            "gene_synonyms": "",
            "gene_synonyms_links": "",
            "gene_name": "Sorbitol dehydrogenase",
            "hgnc_id": "",
            "entrez_id": "",
            "ensembl_id": "ENSG00000140263",
            "omim_id": "",
            "genecard_link": "",
            "locs": "Mitochondrion membrane; Peripheral membrane protein; Cell projection, cilium, flagellum",
            "reaction": "D-fructose + H(+) + NADH = D-sorbitol + NAD(+); L-threitol + NAD(+) = H(+) + L-erythrulose + NADH; NAD(+) + xylitol = D-xylulose + H(+) + NADH; NAD(+) + ribitol = D-ribulose + H(+) + NADH; (R,R)-butane-2,3-diol + NAD(+) = (R)-acetoin + H(+) + NADH; L-iditol + NAD(+) = H(+) + keto-L-sorbose + NADH",
            "targ_desciption": "Polyol dehydrogenase that catalyzes the reversible NAD(+)-dependent oxidation of various sugar alcohols. Is mostly active with D-sorbitol (D-glucitol), L-threitol, xylitol and ribitol as substrates,leading to the C2-oxidized products D-fructose, L-erythrulose, D-xylulose, and D-ribulose, respectively (PubMed:3365415). Is a keyenzyme in the polyol pathway that interconverts glucose and fructosevia sorbitol, which constitutes an important alternate route forglucose metabolism. The polyol pathway is believed to be involved inthe etiology of diabetic complications, such as diabetic neuropathy andretinopathy, induced by hyperglycemia (PubMed:12962626,PubMed:29966615, PubMed:25105142). May play a role in sperm motility byusing sorbitol as an alternative energy source for sperm motility(PubMed:16278369). May have a more general function in the metabolismof secondary alcohols since it also catalyzes the stereospecificoxidation of (2R,3R)-2,3-butanediol. To a lesser extent, can alsooxidize L-arabinitol, galactitol and D-mannitol and glycerol in vitro.Oxidizes neither ethanol nor other primary alcohols. Cannot use NADP(+)as the electron acceptor (PubMed:3365415).{ECO:0000269|PubMed:16278369, ECO:0000269|PubMed:3365415,ECO:0000303|PubMed:25105142, ECO:0000303|PubMed:29966615,ECO:0000305|PubMed:12962626}.",
            "references": []
        },
        {
            "targ_id": "T080",
            "parent_targ_id": "T",
            "full_name": "Pyruvate dehydrogenase kinase",
            "abbrev": "PDK",
            "protein_names": "",
            "related_func_ids": "F0202",
            "category": "enzyme family",
            "subcategories": "",
            "Uniport_ID": "",
            "Uniprot_name": "",
            "EC_numbers": "2.7.11.2",
            "gene_symbol": "",
            "gene_synonyms": "",
            "gene_synonyms_links": "",
            "gene_name": "",
            "hgnc_id": "",
            "entrez_id": "",
            "ensembl_id": "",
            "omim_id": "",
            "genecard_link": "",
            "locs": "",
            "reaction": "",
            "targ_desciption": "",
            "references": [
                "RC03689",
                "RC03744"
            ]
        },
        {
            "targ_id": "T080001",
            "parent_targ_id": "T080",
            "full_name": "[Pyruvate dehydrogenase (acetyl-transferring)] kinase isozyme 1, mitochondrial (EC 2.7.11.2) (Pyruvate dehydrogenase kinase isoform 1) (PDH kinase 1)",
            "abbrev": "PDK1",
            "protein_names": "[Pyruvate dehydrogenase (acetyl-transferring)] kinase isozyme 1, mitochondrial (EC 2.7.11.2) (Pyruvate dehydrogenase kinase isoform 1) (PDH kinase 1)",
            "related_func_ids": "F0202",
            "category": "enzyme",
            "subcategories": "Kinase, Transferase",
            "Uniport_ID": "Q15118",
            "Uniprot_name": "PDK1_HUMAN",
            "EC_numbers": "2.7.11.2",
            "gene_symbol": "PDK1",
            "gene_synonyms": "",
            "gene_synonyms_links": "",
            "gene_name": "Pyruvate dehydrogenase kinase 1",
            "hgnc_id": "",
            "entrez_id": "",
            "ensembl_id": "ENSG00000152256",
            "omim_id": "",
            "genecard_link": "",
            "locs": "Mitochondrion matrix",
            "reaction": "[pyruvate dehydrogenase E1 alpha subunit]-L-serine + ATP =[pyruvate dehydrogenase E1 alpha subunit]-O-phospho-L-serine + ADP +H(+)",
            "targ_desciption": "Kinase that plays a key role in regulation of glucose andfatty acid metabolism and homeostasis via phosphorylation of thepyruvate dehydrogenase subunits PDHA1 and PDHA2. This inhibits pyruvatedehydrogenase activity, and thereby regulates metabolite flux throughthe tricarboxylic acid cycle, down-regulates aerobic respiration andinhibits the formation of acetyl-coenzyme A from pyruvate. Plays animportant role in cellular responses to hypoxia and is important forcell proliferation under hypoxia. Protects cells against apoptosis inresponse to hypoxia and oxidative stress. {ECO:0000269|PubMed:17683942,ECO:0000269|PubMed:18541534, ECO:0000269|PubMed:22195962,ECO:0000269|PubMed:7499431}.",
            "references": [
                "RC03746",
                "RC03748",
                "RC03749",
                "RC03750",
                "RC03751",
                "RC03752"
            ]
        },
        {
            "targ_id": "T080002",
            "parent_targ_id": "T080",
            "full_name": "[Pyruvate dehydrogenase (acetyl-transferring)] kinase isozyme 2, mitochondrial (EC 2.7.11.2) (Pyruvate dehydrogenase kinase isoform 2) (PDH kinase 2) (PDKII)",
            "abbrev": "PDK2",
            "protein_names": "[Pyruvate dehydrogenase (acetyl-transferring)] kinase isozyme 2, mitochondrial (EC 2.7.11.2) (Pyruvate dehydrogenase kinase isoform 2) (PDH kinase 2) (PDKII)",
            "related_func_ids": "F0202",
            "category": "enzyme",
            "subcategories": "Kinase, Transferase",
            "Uniport_ID": "Q15119",
            "Uniprot_name": "PDK2_HUMAN",
            "EC_numbers": "2.7.11.2",
            "gene_symbol": "PDK2",
            "gene_synonyms": "PDHK2",
            "gene_synonyms_links": "",
            "gene_name": "Pyruvate dehydrogenase kinase 2",
            "hgnc_id": "",
            "entrez_id": "",
            "ensembl_id": "ENSG00000005882",
            "omim_id": "",
            "genecard_link": "",
            "locs": "Mitochondrion matrix",
            "reaction": "[pyruvate dehydrogenase E1 alpha subunit]-L-serine + ATP =[pyruvate dehydrogenase E1 alpha subunit]-O-phospho-L-serine + ADP +H(+)",
            "targ_desciption": "Kinase that plays a key role in the regulation of glucose andfatty acid metabolism and homeostasis via phosphorylation of thepyruvate dehydrogenase subunits PDHA1 and PDHA2. This inhibits pyruvatedehydrogenase activity, and thereby regulates metabolite flux throughthe tricarboxylic acid cycle, down-regulates aerobic respiration andinhibits the formation of acetyl-coenzyme A from pyruvate. Inhibitionof pyruvate dehydrogenase decreases glucose utilization and increasesfat metabolism. Mediates cellular responses to insulin. Plays animportant role in maintaining normal blood glucose levels and inmetabolic adaptation to nutrient availability. Via its regulation ofpyruvate dehydrogenase activity, plays an important role in maintainingnormal blood pH and in preventing the accumulation of ketone bodiesunder starvation. Plays a role in the regulation of cell proliferationand in resistance to apoptosis under oxidative stress. Plays a role inp53/TP53-mediated apoptosis. {ECO:0000269|PubMed:17222789,ECO:0000269|PubMed:19833728, ECO:0000269|PubMed:21283817,ECO:0000269|PubMed:22123926, ECO:0000269|PubMed:7499431,ECO:0000269|PubMed:9787110}.",
            "references": [
                "RC03742",
                "RC03743",
                "RC03745"
            ]
        },
        {
            "targ_id": "T080003",
            "parent_targ_id": "T080",
            "full_name": "[Pyruvate dehydrogenase (acetyl-transferring)] kinase isozyme 3, mitochondrial (EC 2.7.11.2) (Pyruvate dehydrogenase kinase isoform 3)",
            "abbrev": "PDK3",
            "protein_names": "[Pyruvate dehydrogenase (acetyl-transferring)] kinase isozyme 3, mitochondrial (EC 2.7.11.2) (Pyruvate dehydrogenase kinase isoform 3)",
            "related_func_ids": "F0202",
            "category": "enzyme",
            "subcategories": "Kinase, Transferase",
            "Uniport_ID": "Q15120",
            "Uniprot_name": "PDK3_HUMAN",
            "EC_numbers": "2.7.11.2",
            "gene_symbol": "PDK3",
            "gene_synonyms": "",
            "gene_synonyms_links": "",
            "gene_name": "Pyruvate dehydrogenase kinase 3",
            "hgnc_id": "",
            "entrez_id": "",
            "ensembl_id": "ENSG00000067992",
            "omim_id": "",
            "genecard_link": "",
            "locs": "Mitochondrion matrix",
            "reaction": "[pyruvate dehydrogenase E1 alpha subunit]-L-serine + ATP =[pyruvate dehydrogenase E1 alpha subunit]-O-phospho-L-serine + ADP +H(+)",
            "targ_desciption": "Inhibits pyruvate dehydrogenase activity by phosphorylationof the E1 subunit PDHA1, and thereby regulates glucose metabolism andaerobic respiration. Can also phosphorylate PDHA2. Decreases glucoseutilization and increases fat metabolism in response to prolongedfasting, and as adaptation to a high-fat diet. Plays a role in glucosehomeostasis and in maintaining normal blood glucose levels in functionof nutrient levels and under starvation. Plays a role in the generationof reactive oxygen species. {ECO:0000269|PubMed:10748134,ECO:0000269|PubMed:11486000, ECO:0000269|PubMed:15861126,ECO:0000269|PubMed:16436377, ECO:0000269|PubMed:17683942,ECO:0000269|PubMed:18718909, ECO:0000269|PubMed:22865452}.",
            "references": [
                "RC03747"
            ]
        },
        {
            "targ_id": "T080004",
            "parent_targ_id": "T080",
            "full_name": "[Pyruvate dehydrogenase (acetyl-transferring)] kinase isozyme 4, mitochondrial (EC 2.7.11.2) (Pyruvate dehydrogenase kinase isoform 4)",
            "abbrev": "PDK4",
            "protein_names": "[Pyruvate dehydrogenase (acetyl-transferring)] kinase isozyme 4, mitochondrial (EC 2.7.11.2) (Pyruvate dehydrogenase kinase isoform 4)",
            "related_func_ids": "F0202",
            "category": "enzyme",
            "subcategories": "Kinase, Transferase",
            "Uniport_ID": "Q16654",
            "Uniprot_name": "PDK4_HUMAN",
            "EC_numbers": "2.7.11.2",
            "gene_symbol": "PDK4",
            "gene_synonyms": "",
            "gene_synonyms_links": "",
            "gene_name": "Pyruvate dehydrogenase kinase 4",
            "hgnc_id": "",
            "entrez_id": "",
            "ensembl_id": "ENSG00000004799",
            "omim_id": "",
            "genecard_link": "",
            "locs": "Mitochondrion matrix",
            "reaction": "[pyruvate dehydrogenase E1 alpha subunit]-L-serine + ATP =[pyruvate dehydrogenase E1 alpha subunit]-O-phospho-L-serine + ADP +H(+)",
            "targ_desciption": "Kinase that plays a key role in regulation of glucose andfatty acid metabolism and homeostasis via phosphorylation of thepyruvate dehydrogenase subunits PDHA1 and PDHA2. This inhibits pyruvatedehydrogenase activity, and thereby regulates metabolite flux throughthe tricarboxylic acid cycle, down-regulates aerobic respiration andinhibits the formation of acetyl-coenzyme A from pyruvate. Inhibitionof pyruvate dehydrogenase decreases glucose utilization and increasesfat metabolism in response to prolonged fasting and starvation. Playsan important role in maintaining normal blood glucose levels understarvation, and is involved in the insulin signaling cascade. Via itsregulation of pyruvate dehydrogenase activity, plays an important rolein maintaining normal blood pH and in preventing the accumulation ofketone bodies under starvation. In the fed state, mediates cellularresponses to glucose levels and to a high-fat diet. Regulates bothfatty acid oxidation and de novo fatty acid biosynthesis. Plays a rolein the generation of reactive oxygen species. Protects detachedepithelial cells against anoikis. Plays a role in cell proliferationvia its role in regulating carbohydrate and fatty acid metabolism.{ECO:0000269|PubMed:15955060, ECO:0000269|PubMed:18658136,ECO:0000269|PubMed:21816445, ECO:0000269|PubMed:21852536}.",
            "references": []
        },
        {
            "targ_id": "T081",
            "parent_targ_id": "T",
            "full_name": "Pyruvate kinase PKLR",
            "abbrev": "PYK",
            "protein_names": "Pyruvate kinase PKLR (EC 2.7.1.40) (Pyruvate kinase 1) (Pyruvate kinase isozymes L/R) (R-type/L-type pyruvate kinase) (Red cell/liver pyruvate kinase)",
            "related_func_ids": "F0202",
            "category": "enzyme",
            "subcategories": "Allosteric enzyme, Kinase, Transferase",
            "Uniport_ID": "P30613",
            "Uniprot_name": "KPYR_HUMAN",
            "EC_numbers": "2.7.1.40",
            "gene_symbol": "PKLR PK1 PKL",
            "gene_synonyms": "",
            "gene_synonyms_links": "",
            "gene_name": "",
            "hgnc_id": "",
            "entrez_id": "",
            "ensembl_id": "",
            "omim_id": "",
            "genecard_link": "",
            "locs": "",
            "reaction": "ATP + pyruvate = ADP + H(+) + phosphoenolpyruvate",
            "targ_desciption": "Plays a key role in glycolysis. {ECO:0000250}.",
            "references": [
                "RC03771",
                "RC04745"
            ]
        },
        {
            "targ_id": "T082",
            "parent_targ_id": "T",
            "full_name": "Dihydrolipoyl dehydrogenase, mitochondrial (EC 1.8.1.4) (Dihydrolipoamide dehydrogenase) (Glycine cleavage system L protein)",
            "abbrev": "DLD",
            "protein_names": "Dihydrolipoyl dehydrogenase, mitochondrial (EC 1.8.1.4) (Dihydrolipoamide dehydrogenase) (Glycine cleavage system L protein)",
            "related_func_ids": "F0202",
            "category": "enzyme",
            "subcategories": "Oxidoreductase",
            "Uniport_ID": "P09622",
            "Uniprot_name": "DLDH_HUMAN",
            "EC_numbers": "1.8.1.4",
            "gene_symbol": "DLD",
            "gene_synonyms": "DLDH, GCSL, LAD",
            "gene_synonyms_links": "",
            "gene_name": "Dihydrolipoamide dehydrogenase",
            "hgnc_id": "",
            "entrez_id": "",
            "ensembl_id": "ENSG00000091140",
            "omim_id": "",
            "genecard_link": "",
            "locs": "Mitochondrion matrix; Nucleus; Cell projection, cilium, flagellum; Cytoplasmic vesicle, secretory vesicle,acrosome",
            "reaction": "(R)-N(6)-dihydrolipoyl-L-lysyl-[protein] + NAD(+) = (R)-N(6)-lipoyl-L-lysyl-[protein] + H(+) + NADH",
            "targ_desciption": "Lipoamide dehydrogenase is a component of the glycinecleavage system as well as an E3 component of three alpha-ketoaciddehydrogenase complexes (pyruvate-, alpha-ketoglutarate-, and branched-chain amino acid-dehydrogenase complex) (PubMed:15712224,PubMed:16442803, PubMed:16770810, PubMed:17404228, PubMed:20160912,PubMed:20385101). The 2-oxoglutarate dehydrogenase complex is mainlyactive in the mitochondrion (PubMed:29211711). A fraction of the 2-oxoglutarate dehydrogenase complex also localizes in the nucleus and isrequired for lysine succinylation of histones: associates with KAT2A onchromatin and provides succinyl-CoA to histone succinyltransferaseKAT2A (PubMed:29211711). In monomeric form may have additionalmoonlighting function as serine protease (PubMed:17404228). Involved inthe hyperactivation of spermatazoa during capacitation and in thespermatazoal acrosome reaction (By similarity).{ECO:0000250|UniProtKB:Q811C4, ECO:0000269|PubMed:15712224,ECO:0000269|PubMed:16442803, ECO:0000269|PubMed:16770810,ECO:0000269|PubMed:17404228, ECO:0000269|PubMed:20160912,ECO:0000269|PubMed:20385101, ECO:0000269|PubMed:29211711}.",
            "references": []
        },
        {
            "targ_id": "T083",
            "parent_targ_id": "T",
            "full_name": "Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex, mitochondrial",
            "abbrev": "PBC",
            "protein_names": "Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex, mitochondrial (EC 2.3.1.12) (70 kDa mitochondrial autoantigen of primary biliary cirrhosis) (PBC) (Dihydrolipoamide acetyltransferase component of pyruvate dehydrogenase complex) (M2 antigen complex 70 kDa subunit) (Pyruvate dehydrogenase complex component E2) (PDC-E2) (PDCE2)",
            "related_func_ids": "F0202",
            "category": "enzyme",
            "subcategories": "Acyltransferase, Transferase",
            "Uniport_ID": "P10515",
            "Uniprot_name": "ODP2_HUMAN",
            "EC_numbers": "2.3.1.12",
            "gene_symbol": "DLAT",
            "gene_synonyms": "DLTA, PDC-E2",
            "gene_synonyms_links": "",
            "gene_name": "Dihydrolipoamide S-acetyltransferase",
            "hgnc_id": "",
            "entrez_id": "",
            "ensembl_id": "ENSG00000150768",
            "omim_id": "",
            "genecard_link": "",
            "locs": "Mitochondrion matrix",
            "reaction": "(R)-N(6)-dihydrolipoyl-L-lysyl-[protein] + acetyl-CoA = (R)-N(6)-(S(8)-acetyldihydrolipoyl)-L-lysyl-[protein] + CoA",
            "targ_desciption": "The pyruvate dehydrogenase complex catalyzes the overallconversion of pyruvate to acetyl-CoA and CO(2), and thereby links theglycolytic pathway to the tricarboxylic cycle.",
            "references": []
        },
        {
            "targ_id": "T084",
            "parent_targ_id": "T",
            "full_name": "Mitochondrial pyruvate carrier 1",
            "abbrev": "Brain protein 44-like protein",
            "protein_names": "Mitochondrial pyruvate carrier 1 (Brain protein 44-like protein)",
            "related_func_ids": "F0202",
            "category": "enzyme",
            "subcategories": "Transporter",
            "Uniport_ID": "Q9Y5U8",
            "Uniprot_name": "MPC1_HUMAN",
            "EC_numbers": "",
            "gene_symbol": "MPC1",
            "gene_synonyms": "BRP44L, CGI-129, dJ68L15.3, SLC54A1",
            "gene_synonyms_links": "",
            "gene_name": "Mitochondrial pyruvate carrier 1",
            "hgnc_id": "",
            "entrez_id": "",
            "ensembl_id": "ENSG00000060762",
            "omim_id": "",
            "genecard_link": "",
            "locs": "Mitochondrion inner membrane; Multi-pass membrane protein",
            "reaction": "",
            "targ_desciption": "Mediates the uptake of pyruvate into mitochondria.{ECO:0000269|PubMed:22628558}.",
            "references": [
                "RC03763"
            ]
        },
        {
            "targ_id": "T085",
            "parent_targ_id": "T",
            "full_name": "Pyruvate carboxylase, mitochondrial",
            "abbrev": "PCB",
            "protein_names": "Pyruvate carboxylase, mitochondrial (EC 6.4.1.1) (Pyruvic carboxylase) (PCB)",
            "related_func_ids": "F0202",
            "category": "enzyme",
            "subcategories": "Ligase, Multifunctional enzyme",
            "Uniport_ID": "P11498",
            "Uniprot_name": "PYC_HUMAN",
            "EC_numbers": "6.4.1.1",
            "gene_symbol": "PC",
            "gene_synonyms": "PCB",
            "gene_synonyms_links": "",
            "gene_name": "Pyruvate carboxylase",
            "hgnc_id": "",
            "entrez_id": "",
            "ensembl_id": "ENSG00000173599",
            "omim_id": "",
            "genecard_link": "",
            "locs": "Mitochondrion matrix",
            "reaction": "ATP + hydrogencarbonate + pyruvate = ADP + H(+) + oxaloacetate+ phosphate",
            "targ_desciption": "Pyruvate carboxylase catalyzes a 2-step reaction, involvingthe ATP-dependent carboxylation of the covalently attached biotin inthe first step and the transfer of the carboxyl group to pyruvate inthe second. Catalyzes in a tissue specific manner, the initialreactions of glucose (liver, kidney) and lipid (adipose tissue, liver,brain) synthesis from pyruvate.",
            "references": [
                "RC03767",
                "RC03768"
            ]
        },
        {
            "targ_id": "T086",
            "parent_targ_id": "T",
            "full_name": "Pyruvate dehydrogenase E1",
            "abbrev": "PD E1",
            "protein_names": "",
            "related_func_ids": "F0202",
            "category": "enzyme",
            "subcategories": "",
            "Uniport_ID": "",
            "Uniprot_name": "",
            "EC_numbers": "1.2.4.1",
            "gene_symbol": "",
            "gene_synonyms": "",
            "gene_synonyms_links": "",
            "gene_name": "",
            "hgnc_id": "",
            "entrez_id": "",
            "ensembl_id": "",
            "omim_id": "",
            "genecard_link": "",
            "locs": "",
            "reaction": "",
            "targ_desciption": "",
            "references": []
        },
        {
            "targ_id": "T086001",
            "parent_targ_id": "T086",
            "full_name": "Pyruvate dehydrogenase E1 component subunit alpha, somatic form, mitochondrial",
            "abbrev": "PDHE1-A type I",
            "protein_names": "Pyruvate dehydrogenase E1 component subunit alpha, somatic form, mitochondrial (EC 1.2.4.1) (PDHE1-A type I)",
            "related_func_ids": "F0202",
            "category": "protein subunit",
            "subcategories": "Oxidoreductase",
            "Uniport_ID": "P08559",
            "Uniprot_name": "ODPA_HUMAN",
            "EC_numbers": "1.2.4.1",
            "gene_symbol": "PDHA1",
            "gene_synonyms": "PDHA",
            "gene_synonyms_links": "",
            "gene_name": "Pyruvate dehydrogenase E1 alpha 1 subunit",
            "hgnc_id": "",
            "entrez_id": "",
            "ensembl_id": "ENSG00000131828",
            "omim_id": "",
            "genecard_link": "",
            "locs": "Mitochondrion matrix",
            "reaction": "[dihydrolipoyllysine-residue acetyltransferase]-(R)-N(6)-lipoyl-L-lysine + H(+) + pyruvate = [dihydrolipoyllysine-residueacetyltransferase]-(R)-N(6)-(S(8)-acetyldihydrolipoyl)-L-lysine +CO2",
            "targ_desciption": "The pyruvate dehydrogenase complex catalyzes the overallconversion of pyruvate to acetyl-CoA and CO(2), and thereby links theglycolytic pathway to the tricarboxylic cycle.{ECO:0000269|PubMed:19081061, ECO:0000269|PubMed:7782287}.",
            "references": [
                "RC03762"
            ]
        },
        {
            "targ_id": "T086002",
            "parent_targ_id": "T086",
            "full_name": "Pyruvate dehydrogenase E1 component subunit beta, mitochondrial",
            "abbrev": "PDHE1-B",
            "protein_names": "Pyruvate dehydrogenase E1 component subunit beta, mitochondrial (PDHE1-B) (EC 1.2.4.1)",
            "related_func_ids": "F0202",
            "category": "protein subunit",
            "subcategories": "Oxidoreductase",
            "Uniport_ID": "P11177",
            "Uniprot_name": "ODPB_HUMAN",
            "EC_numbers": "1.2.4.1",
            "gene_symbol": "PDHB",
            "gene_synonyms": "PDHE1B",
            "gene_synonyms_links": "",
            "gene_name": "Pyruvate dehydrogenase E1 beta subunit",
            "hgnc_id": "",
            "entrez_id": "",
            "ensembl_id": "ENSG00000168291",
            "omim_id": "",
            "genecard_link": "",
            "locs": "Mitochondrion matrix",
            "reaction": "[dihydrolipoyllysine-residue acetyltransferase]-(R)-N(6)-lipoyl-L-lysine + H(+) + pyruvate = [dihydrolipoyllysine-residueacetyltransferase]-(R)-N(6)-(S(8)-acetyldihydrolipoyl)-L-lysine +CO2",
            "targ_desciption": "The pyruvate dehydrogenase complex catalyzes the overallconversion of pyruvate to acetyl-CoA and CO(2), and thereby links theglycolytic pathway to the tricarboxylic cycle.{ECO:0000269|PubMed:17474719, ECO:0000269|PubMed:19081061}.",
            "references": []
        },
        {
            "targ_id": "T086003",
            "parent_targ_id": "T086",
            "full_name": "Pyruvate dehydrogenase E1 component subunit alpha, somatic form, mitochondrial",
            "abbrev": "PDHE1-A type I",
            "protein_names": "Pyruvate dehydrogenase E1 component subunit alpha, somatic form, mitochondrial (EC 1.2.4.1) (PDHE1-A type I)",
            "related_func_ids": "F0202",
            "category": "protein subunit",
            "subcategories": "Oxidoreductase",
            "Uniport_ID": "P08559",
            "Uniprot_name": "ODPA_HUMAN",
            "EC_numbers": "1.2.4.1",
            "gene_symbol": "PDHA1",
            "gene_synonyms": "PDHA",
            "gene_synonyms_links": "",
            "gene_name": "Pyruvate dehydrogenase E1 alpha 1 subunit",
            "hgnc_id": "",
            "entrez_id": "",
            "ensembl_id": "ENSG00000131828",
            "omim_id": "",
            "genecard_link": "",
            "locs": "Mitochondrion matrix",
            "reaction": "[dihydrolipoyllysine-residue acetyltransferase]-(R)-N(6)-lipoyl-L-lysine + H(+) + pyruvate = [dihydrolipoyllysine-residueacetyltransferase]-(R)-N(6)-(S(8)-acetyldihydrolipoyl)-L-lysine +CO2",
            "targ_desciption": "The pyruvate dehydrogenase complex catalyzes the overallconversion of pyruvate to acetyl-CoA and CO(2), and thereby links theglycolytic pathway to the tricarboxylic cycle.{ECO:0000269|PubMed:19081061, ECO:0000269|PubMed:7782287}.",
            "references": []
        },
        {
            "targ_id": "T086004",
            "parent_targ_id": "T086",
            "full_name": "Pyruvate dehydrogenase E1 component subunit alpha, testis-specific form, mitochondrial",
            "abbrev": "PDHE1-A type II",
            "protein_names": "Pyruvate dehydrogenase E1 component subunit alpha, testis-specific form, mitochondrial (EC 1.2.4.1) (PDHE1-A type II)",
            "related_func_ids": "F0202",
            "category": "protein subunit",
            "subcategories": "Oxidoreductase",
            "Uniport_ID": "P29803",
            "Uniprot_name": "ODPAT_HUMAN",
            "EC_numbers": "1.2.4.1",
            "gene_symbol": "PDHA2",
            "gene_synonyms": "PDHAL",
            "gene_synonyms_links": "",
            "gene_name": "Pyruvate dehydrogenase E1 alpha 2 subunit",
            "hgnc_id": "",
            "entrez_id": "",
            "ensembl_id": "ENSG00000163114",
            "omim_id": "",
            "genecard_link": "",
            "locs": "Mitochondrion matrix",
            "reaction": "[dihydrolipoyllysine-residue acetyltransferase]-(R)-N(6)-lipoyl-L-lysine + H(+) + pyruvate = [dihydrolipoyllysine-residueacetyltransferase]-(R)-N(6)-(S(8)-acetyldihydrolipoyl)-L-lysine +CO2",
            "targ_desciption": "The pyruvate dehydrogenase complex catalyzes the overallconversion of pyruvate to acetyl-CoA and CO(2), and thereby links theglycolytic pathway to the tricarboxylic cycle.{ECO:0000269|PubMed:16436377}.",
            "references": []
        },
        {
            "targ_id": "T087",
            "parent_targ_id": "T",
            "full_name": "Pyruvate dehydrogenase protein X component, mitochondrial",
            "abbrev": "E3BP",
            "protein_names": "Pyruvate dehydrogenase protein X component, mitochondrial (Dihydrolipoamide dehydrogenase-binding protein of pyruvate dehydrogenase complex) (E3-binding protein) (E3BP) (Lipoyl-containing pyruvate dehydrogenase complex component X) (proX)",
            "related_func_ids": "F0202",
            "category": "enzyme",
            "subcategories": "",
            "Uniport_ID": "O00330",
            "Uniprot_name": "ODPX_HUMAN",
            "EC_numbers": "",
            "gene_symbol": "PDHX",
            "gene_synonyms": "DLDBP, E3BP, OPDX, PDX1, proX",
            "gene_synonyms_links": "",
            "gene_name": "Pyruvate dehydrogenase complex component X",
            "hgnc_id": "",
            "entrez_id": "",
            "ensembl_id": "ENSG00000110435",
            "omim_id": "",
            "genecard_link": "",
            "locs": "Mitochondrion matrix",
            "reaction": "",
            "targ_desciption": "Required for anchoring dihydrolipoamide dehydrogenase (E3) tothe dihydrolipoamide transacetylase (E2) core of the pyruvatedehydrogenase complexes of eukaryotes. This specific binding isessential for a functional PDH complex.",
            "references": []
        },
        {
            "targ_id": "T088",
            "parent_targ_id": "T",
            "full_name": "[Pyruvate dehydrogenase [acetyl-transferring]]-phosphatase 1, mitochondrial",
            "abbrev": "PDP 1",
            "protein_names": "[Pyruvate dehydrogenase [acetyl-transferring]]-phosphatase 1, mitochondrial (PDP 1) (EC 3.1.3.43) (Protein phosphatase 2C) (Pyruvate dehydrogenase phosphatase catalytic subunit 1) (PDPC 1)",
            "related_func_ids": "F0202",
            "category": "enzyme",
            "subcategories": "Hydrolase, Protein phosphatase",
            "Uniport_ID": "Q9P0J1",
            "Uniprot_name": "PDP1_HUMAN",
            "EC_numbers": "3.1.3.43",
            "gene_symbol": "PDP1",
            "gene_synonyms": "PDH, PDP, PPM2A, PPM2C",
            "gene_synonyms_links": "",
            "gene_name": "Pyruvate dehyrogenase phosphatase catalytic subunit 1",
            "hgnc_id": "",
            "entrez_id": "",
            "ensembl_id": "ENSG00000164951",
            "omim_id": "",
            "genecard_link": "",
            "locs": "Mitochondrion matrix",
            "reaction": "[pyruvate dehydrogenase E1 alpha subunit]-O-phospho-L-serine +H2O = [pyruvate dehydrogenase E1 alpha subunit]-L-serine + phosphate",
            "targ_desciption": "Catalyzes the dephosphorylation and concomitant reactivationof the alpha subunit of the E1 component of the pyruvate dehydrogenasecomplex. {ECO:0000250}.",
            "references": []
        },
        {
            "targ_id": "T089",
            "parent_targ_id": "T",
            "full_name": "Pyruvate dehydrogenase phosphatase regulatory subunit, mitochondrial",
            "abbrev": "PDPr",
            "protein_names": "Pyruvate dehydrogenase phosphatase regulatory subunit, mitochondrial (PDPr)",
            "related_func_ids": "F0202",
            "category": "enzyme",
            "subcategories": "",
            "Uniport_ID": "Q8NCN5",
            "Uniprot_name": "PDPR_HUMAN",
            "EC_numbers": "",
            "gene_symbol": "PDPR",
            "gene_synonyms": "PDP3",
            "gene_synonyms_links": "",
            "gene_name": "Pyruvate dehydrogenase phosphatase regulatory subunit",
            "hgnc_id": "",
            "entrez_id": "",
            "ensembl_id": "ENSG00000090857",
            "omim_id": "",
            "genecard_link": "",
            "locs": "Mitochondrion matrix",
            "reaction": "",
            "targ_desciption": "Decreases the sensitivity of PDP1 to magnesium ions, and thisinhibition is reversed by the polyamine spermine. {ECO:0000250}.",
            "references": []
        },
        {
            "targ_id": "T090",
            "parent_targ_id": "T",
            "full_name": "Hydroxyacylglutathione hydrolase, mitochondrial",
            "abbrev": "Glyoxalase II",
            "protein_names": "Hydroxyacylglutathione hydrolase, mitochondrial (EC 3.1.2.6) (Glyoxalase II) (Glx II)",
            "related_func_ids": "F0202",
            "category": "enzyme",
            "subcategories": "Hydrolase",
            "Uniport_ID": "Q16775",
            "Uniprot_name": "GLO2_HUMAN",
            "EC_numbers": "3.1.2.6",
            "gene_symbol": "HAGH",
            "gene_synonyms": "GLO2, GLXII, HAGH1",
            "gene_synonyms_links": "",
            "gene_name": "Hydroxyacylglutathione hydrolase",
            "hgnc_id": "",
            "entrez_id": "",
            "ensembl_id": "ENSG00000063854",
            "omim_id": "",
            "genecard_link": "",
            "locs": "[Isoform 1]: Mitochondrion matrix; [Isoform 2]: Cytoplasm",
            "reaction": "an S-(2-hydroxyacyl)glutathione + H2O = a 2-hydroxycarboxylate + glutathione + H(+)",
            "targ_desciption": "Thiolesterase that catalyzes the hydrolysis of S-D-lactoyl-glutathione to form glutathione and D-lactic acid.",
            "references": []
        },
        {
            "targ_id": "T091",
            "parent_targ_id": "T",
            "full_name": "Citrate synthase, mitochondrial",
            "abbrev": "CS",
            "protein_names": "Citrate synthase, mitochondrial (EC 2.3.3.1) (Citrate (Si)-synthase)",
            "related_func_ids": "F0203",
            "category": "enzyme",
            "subcategories": "Transferase",
            "Uniport_ID": "O75390",
            "Uniprot_name": "CISY_HUMAN",
            "EC_numbers": "2.3.3.1",
            "gene_symbol": "CS",
            "gene_synonyms": "",
            "gene_synonyms_links": "",
            "gene_name": "Citrate synthase",
            "hgnc_id": "",
            "entrez_id": "",
            "ensembl_id": "ENSG00000062485",
            "omim_id": "",
            "genecard_link": "",
            "locs": "Mitochondrion matrix",
            "reaction": "acetyl-CoA + H2O + oxaloacetate = citrate + CoA + H(+)",
            "targ_desciption": "",
            "references": [
                "RC03452",
                "RC04713",
                "RC04714",
                "RC04715",
                "RC04716"
            ]
        },
        {
            "targ_id": "T092",
            "parent_targ_id": "T",
            "full_name": "Aconitate hydratase, mitochondrial",
            "abbrev": "Aconitase",
            "protein_names": "Aconitate hydratase, mitochondrial (Aconitase) (EC 4.2.1.3) (Citrate hydro-lyase)",
            "related_func_ids": "F0203",
            "category": "enzyme",
            "subcategories": "Lyase",
            "Uniport_ID": "Q99798",
            "Uniprot_name": "ACON_HUMAN",
            "EC_numbers": "4.2.1.3",
            "gene_symbol": "ACO2",
            "gene_synonyms": "ACONM",
            "gene_synonyms_links": "",
            "gene_name": "Aconitase 2",
            "hgnc_id": "",
            "entrez_id": "",
            "ensembl_id": "ENSG00000100412",
            "omim_id": "",
            "genecard_link": "",
            "locs": "Mitochondrion",
            "reaction": "citrate = isocitrate",
            "targ_desciption": "Catalyzes the isomerization of citrate to isocitrate via cis-aconitate. {ECO:0000250|UniProtKB:P16276}.",
            "references": [
                "RC03447",
                "RC03834"
            ]
        },
        {
            "targ_id": "T093",
            "parent_targ_id": "T",
            "full_name": "Isocitrate dehydrogenase [NADP] cytoplasmic",
            "abbrev": "IDH",
            "protein_names": "Isocitrate dehydrogenase [NADP] cytoplasmic (IDH) (EC 1.1.1.42) (Cytosolic NADP-isocitrate dehydrogenase) (IDP) (NADP(+)-specific ICDH) (Oxalosuccinate decarboxylase)",
            "related_func_ids": "F0203",
            "category": "enzyme",
            "subcategories": "Oxidoreductase",
            "Uniport_ID": "O75874",
            "Uniprot_name": "IDHC_HUMAN",
            "EC_numbers": "1.1.1.42",
            "gene_symbol": "IDH1",
            "gene_synonyms": "",
            "gene_synonyms_links": "",
            "gene_name": "Isocitrate dehydrogenase (NADP(+)) 1, cytosolic",
            "hgnc_id": "",
            "entrez_id": "",
            "ensembl_id": "ENSG00000138413",
            "omim_id": "",
            "genecard_link": "",
            "locs": "Cytoplasm, cytosol; Peroxisome",
            "reaction": "isocitrate + NADP(+) = 2-oxoglutarate + CO2 + NADPH",
            "targ_desciption": "",
            "references": []
        },
        {
            "targ_id": "T094",
            "parent_targ_id": "T",
            "full_name": "Isocitrate dehydrogenase [NADP], mitochondrial",
            "abbrev": "IDH",
            "protein_names": "Isocitrate dehydrogenase [NADP], mitochondrial (IDH) (EC 1.1.1.42) (ICD-M) (IDP) (NADP(+)-specific ICDH) (Oxalosuccinate decarboxylase)",
            "related_func_ids": "F0203",
            "category": "enzyme",
            "subcategories": "Oxidoreductase",
            "Uniport_ID": "P48735",
            "Uniprot_name": "IDHP_HUMAN",
            "EC_numbers": "1.1.1.42",
            "gene_symbol": "IDH2",
            "gene_synonyms": "",
            "gene_synonyms_links": "",
            "gene_name": "Isocitrate dehydrogenase (NADP(+)) 2, mitochondrial",
            "hgnc_id": "",
            "entrez_id": "",
            "ensembl_id": "ENSG00000182054",
            "omim_id": "",
            "genecard_link": "",
            "locs": "Mitochondrion",
            "reaction": "isocitrate + NADP(+) = 2-oxoglutarate + CO2 + NADPH",
            "targ_desciption": "Plays a role in intermediary metabolism and energyproduction. It may tightly associate or interact with the pyruvatedehydrogenase complex.",
            "references": [
                "RC03835"
            ]
        },
        {
            "targ_id": "T094001",
            "parent_targ_id": "T094",
            "full_name": "Isocitrate dehydrogenase [NAD] subunit alpha, mitochondrial",
            "abbrev": "Isocitric dehydrogenase subunit alpha",
            "protein_names": "Isocitrate dehydrogenase [NAD] subunit alpha, mitochondrial (EC 1.1.1.41) (Isocitric dehydrogenase subunit alpha) (NAD(+)-specific ICDH subunit alpha)",
            "related_func_ids": "F0203",
            "category": "protein subunit",
            "subcategories": "Oxidoreductase",
            "Uniport_ID": "P50213",
            "Uniprot_name": "IDH3A_HUMAN",
            "EC_numbers": "1.1.1.41",
            "gene_symbol": "IDH3A",
            "gene_synonyms": "",
            "gene_synonyms_links": "",
            "gene_name": "Isocitrate dehydrogenase 3 (NAD(+)) alpha",
            "hgnc_id": "",
            "entrez_id": "",
            "ensembl_id": "ENSG00000166411",
            "omim_id": "",
            "genecard_link": "",
            "locs": "Mitochondrion",
            "reaction": "D-threo-isocitrate + NAD(+) = 2-oxoglutarate + CO2 + NADH",
            "targ_desciption": "Catalytic subunit of the enzyme which catalyzes thedecarboxylation of isocitrate (ICT) into alpha-ketoglutarate. Theheterodimer composed of the alpha (IDH3A) and beta (IDH3B) subunits andthe heterodimer composed of the alpha (IDH3A) and gamma (IDH3G)subunits, have considerable basal activity but the full activity of theheterotetramer (containing two subunits of IDH3A, one of IDH3B and oneof IDH3G) requires the assembly and cooperative function of bothheterodimers. {ECO:0000269|PubMed:28139779}.",
            "references": []
        },
        {
            "targ_id": "T094002",
            "parent_targ_id": "T094",
            "full_name": "Isocitrate dehydrogenase [NAD] subunit beta, mitochondrial",
            "abbrev": "Isocitric dehydrogenase subunit beta",
            "protein_names": "Isocitrate dehydrogenase [NAD] subunit beta, mitochondrial (Isocitric dehydrogenase subunit beta) (NAD(+)-specific ICDH subunit beta)",
            "related_func_ids": "F0203",
            "category": "protein subunit",
            "subcategories": "",
            "Uniport_ID": "O43837",
            "Uniprot_name": "IDH3B_HUMAN",
            "EC_numbers": "",
            "gene_symbol": "IDH3B",
            "gene_synonyms": "RP46",
            "gene_synonyms_links": "",
            "gene_name": "Isocitrate dehydrogenase 3 (NAD(+)) beta",
            "hgnc_id": "",
            "entrez_id": "",
            "ensembl_id": "ENSG00000101365",
            "omim_id": "",
            "genecard_link": "",
            "locs": "Mitochondrion",
            "reaction": "",
            "targ_desciption": "Plays a structural role to facilitate the assembly and ensurethe full activity of the enzyme catalyzing the decarboxylation ofisocitrate (ICT) into alpha-ketoglutarate. The heterodimer composed ofthe alpha (IDH3A) and beta (IDH3B) subunits and the heterodimercomposed of the alpha (IDH3A) and gamma (IDH3G) subunits, haveconsiderable basal activity but the full activity of the heterotetramer(containing two subunits of IDH3A, one of IDH3B and one of IDH3G)requires the assembly and cooperative function of both heterodimers.{ECO:0000269|PubMed:28139779}.",
            "references": []
        },
        {
            "targ_id": "T094003",
            "parent_targ_id": "T094",
            "full_name": "Isocitrate dehydrogenase [NAD] subunit gamma, mitochondrial",
            "abbrev": "Isocitric dehydrogenase subunit gamma",
            "protein_names": "Isocitrate dehydrogenase [NAD] subunit gamma, mitochondrial (Isocitric dehydrogenase subunit gamma) (NAD(+)-specific ICDH subunit gamma)",
            "related_func_ids": "F0203; F021102",
            "category": "protein subunit",
            "subcategories": "",
            "Uniport_ID": "P51553",
            "Uniprot_name": "IDH3G_HUMAN",
            "EC_numbers": "",
            "gene_symbol": "IDH3G",
            "gene_synonyms": "",
            "gene_synonyms_links": "",
            "gene_name": "Isocitrate dehydrogenase 3 (NAD(+)) gamma",
            "hgnc_id": "",
            "entrez_id": "",
            "ensembl_id": "ENSG00000067829",
            "omim_id": "",
            "genecard_link": "",
            "locs": "Mitochondrion",
            "reaction": "",
            "targ_desciption": "Regulatory subunit which plays a role in the allostericregulation of the enzyme catalyzing the decarboxylation of isocitrate(ICT) into alpha-ketoglutarate. The heterodimer composed of the alpha(IDH3A) and beta (IDH3B) subunits and the heterodimer composed of thealpha (IDH3A) and gamma (IDH3G) subunits, have considerable basalactivity but the full activity of the heterotetramer (containing twosubunits of IDH3A, one of IDH3B and one of IDH3G) requires the assemblyand cooperative function of both heterodimers.{ECO:0000269|PubMed:28139779}.",
            "references": []
        },
        {
            "targ_id": "T095",
            "parent_targ_id": "T",
            "full_name": "2-oxoglutarate dehydrogenase, mitochondrial",
            "abbrev": "OGDH",
            "protein_names": "2-oxoglutarate dehydrogenase, mitochondrial (EC 1.2.4.2) (2-oxoglutarate dehydrogenase complex component E1) (OGDC-E1) (Alpha-ketoglutarate dehydrogenase)",
            "related_func_ids": "F0203",
            "category": "enzyme",
            "subcategories": "Oxidoreductase",
            "Uniport_ID": "Q02218",
            "Uniprot_name": "ODO1_HUMAN",
            "EC_numbers": "1.2.4.2",
            "gene_symbol": "OGDH",
            "gene_synonyms": "E1k",
            "gene_synonyms_links": "",
            "gene_name": "Oxoglutarate dehydrogenase",
            "hgnc_id": "",
            "entrez_id": "",
            "ensembl_id": "ENSG00000105953",
            "omim_id": "",
            "genecard_link": "",
            "locs": "Mitochondrion matrix; Nucleus",
            "reaction": "2-oxoglutarate + [dihydrolipoyllysine-residuesuccinyltransferase]-(R)-N(6)-lipoyl-L-lysine + H(+) =[dihydrolipoyllysine-residue succinyltransferase]-(R)-N(6)-(S(8)-succinyldihydrolipoyl)-L-lysine + CO2",
            "targ_desciption": "2-oxoglutarate dehydrogenase (E1) component of the 2-oxoglutarate dehydrogenase complex, which mediates the decarboxylationof alpha-ketoglutarate (PubMed:24495017). The 2-oxoglutaratedehydrogenase complex catalyzes the overall conversion of 2-oxoglutarate to succinyl-CoA and CO(2) (PubMed:24495017). The 2-oxoglutarate dehydrogenase complex is mainly active in themitochondrion (PubMed:29211711). A fraction of the 2-oxoglutaratedehydrogenase complex also localizes in the nucleus and is required forlysine succinylation of histones: associates with KAT2A on chromatinand provides succinyl-CoA to histone succinyltransferase KAT2A(PubMed:29211711). {ECO:0000269|PubMed:24495017,ECO:0000269|PubMed:29211711}.",
            "references": []
        },
        {
            "targ_id": "T096",
            "parent_targ_id": "T",
            "full_name": "Succinate--CoA ligase",
            "abbrev": "SCS",
            "protein_names": "",
            "related_func_ids": "F0203",
            "category": "enzyme",
            "subcategories": "",
            "Uniport_ID": "",
            "Uniprot_name": "",
            "EC_numbers": "",
            "gene_symbol": "",
            "gene_synonyms": "",
            "gene_synonyms_links": "",
            "gene_name": "",
            "hgnc_id": "",
            "entrez_id": "",
            "ensembl_id": "",
            "omim_id": "",
            "genecard_link": "",
            "locs": "",
            "reaction": "",
            "targ_desciption": "",
            "references": []
        },
        {
            "targ_id": "T096001",
            "parent_targ_id": "T096",
            "full_name": "Succinate--CoA ligase [ADP-forming] subunit beta, mitochondrial",
            "abbrev": "SCS-betaA",
            "protein_names": "Succinate--CoA ligase [ADP-forming] subunit beta, mitochondrial (EC 6.2.1.5) (ATP-specific succinyl-CoA synthetase subunit beta) (A-SCS) (Succinyl-CoA synthetase beta-A chain) (SCS-betaA)",
            "related_func_ids": "F0203",
            "category": "protein subunit",
            "subcategories": "Ligase",
            "Uniport_ID": "Q9P2R7",
            "Uniprot_name": "SUCB1_HUMAN",
            "EC_numbers": "6.2.1.5",
            "gene_symbol": "SUCLA2",
            "gene_synonyms": "",
            "gene_synonyms_links": "",
            "gene_name": "Succinate-CoA ligase ADP-forming beta subunit",
            "hgnc_id": "",
            "entrez_id": "",
            "ensembl_id": "ENSG00000136143",
            "omim_id": "",
            "genecard_link": "",
            "locs": "Mitochondrion",
            "reaction": "ATP + CoA + succinate = ADP + phosphate + succinyl-CoA",
            "targ_desciption": "ATP-specific succinyl-CoA synthetase functions in the citricacid cycle (TCA), coupling the hydrolysis of succinyl-CoA to thesynthesis of ATP and thus represents the only step of substrate-levelphosphorylation in the TCA (PubMed:15877282). The beta subunit providesnucleotide specificity of the enzyme and binds the substrate succinate,while the binding sites for coenzyme A and phosphate are found in thealpha subunit (By similarity). {ECO:0000255|HAMAP-Rule:MF_03220,ECO:0000269|PubMed:15877282}.",
            "references": []
        },
        {
            "targ_id": "T096002",
            "parent_targ_id": "T096",
            "full_name": "Succinate--CoA ligase [ADP/GDP-forming] subunit alpha, mitochondrial",
            "abbrev": "SCS-alpha",
            "protein_names": "Succinate--CoA ligase [ADP/GDP-forming] subunit alpha, mitochondrial (EC 6.2.1.4) (EC 6.2.1.5) (Succinyl-CoA synthetase subunit alpha) (SCS-alpha)",
            "related_func_ids": "F0203",
            "category": "protein subunit",
            "subcategories": "Ligase",
            "Uniport_ID": "P53597",
            "Uniprot_name": "SUCA_HUMAN",
            "EC_numbers": "6.2.1.4; 6.2.1.5",
            "gene_symbol": "SUCLG1",
            "gene_synonyms": "",
            "gene_synonyms_links": "",
            "gene_name": "Succinate-CoA ligase alpha subunit",
            "hgnc_id": "",
            "entrez_id": "",
            "ensembl_id": "ENSG00000163541",
            "omim_id": "",
            "genecard_link": "",
            "locs": "Mitochondrion",
            "reaction": "ATP + CoA + succinate = ADP + phosphate + succinyl-CoA; CoA + GTP + succinate = GDP + phosphate + succinyl-CoA",
            "targ_desciption": "Succinyl-CoA synthetase functions in the citric acid cycle(TCA), coupling the hydrolysis of succinyl-CoA to the synthesis ofeither ATP or GTP and thus represents the only step of substrate-levelphosphorylation in the TCA. The alpha subunit of the enzyme binds thesubstrates coenzyme A and phosphate, while succinate binding andspecificity for either ATP or GTP is provided by different betasubunits. {ECO:0000255|HAMAP-Rule:MF_03222}.",
            "references": []
        },
        {
            "targ_id": "T096003",
            "parent_targ_id": "T096",
            "full_name": "Succinate--CoA ligase [GDP-forming] subunit beta, mitochondrial",
            "abbrev": "SCS-betaG",
            "protein_names": "Succinate--CoA ligase [GDP-forming] subunit beta, mitochondrial (EC 6.2.1.4) (GTP-specific succinyl-CoA synthetase subunit beta) (G-SCS) (GTPSCS) (Succinyl-CoA synthetase beta-G chain) (SCS-betaG)",
            "related_func_ids": "F0203",
            "category": "protein subunit",
            "subcategories": "Ligase",
            "Uniport_ID": "Q96I99",
            "Uniprot_name": "SUCB2_HUMAN",
            "EC_numbers": "6.2.1.4",
            "gene_symbol": "SUCLG2",
            "gene_synonyms": "",
            "gene_synonyms_links": "",
            "gene_name": "Succinate-CoA ligase GDP-forming beta subunit",
            "hgnc_id": "",
            "entrez_id": "",
            "ensembl_id": "ENSG00000172340",
            "omim_id": "",
            "genecard_link": "",
            "locs": "Mitochondrion",
            "reaction": "CoA + GTP + succinate = GDP + phosphate + succinyl-CoA",
            "targ_desciption": "GTP-specific succinyl-CoA synthetase functions in the citricacid cycle (TCA), coupling the hydrolysis of succinyl-CoA to thesynthesis of GTP and thus represents the only step of substrate-levelphosphorylation in the TCA. The beta subunit provides nucleotidespecificity of the enzyme and binds the substrate succinate, while thebinding sites for coenzyme A and phosphate are found in the alphasubunit. {ECO:0000255|HAMAP-Rule:MF_03221}.",
            "references": []
        },
        {
            "targ_id": "T098",
            "parent_targ_id": "T",
            "full_name": "Fumarate hydratase, mitochondrial",
            "abbrev": "Fumarase",
            "protein_names": "Fumarate hydratase, mitochondrial (Fumarase) (HsFH) (EC 4.2.1.2)",
            "related_func_ids": "F0203",
            "category": "enzyme",
            "subcategories": "Lyase",
            "Uniport_ID": "P07954",
            "Uniprot_name": "FUMH_HUMAN",
            "EC_numbers": "4.2.1.2",
            "gene_symbol": "FH",
            "gene_synonyms": "fumarase",
            "gene_synonyms_links": "",
            "gene_name": "Fumarate hydratase",
            "hgnc_id": "",
            "entrez_id": "",
            "ensembl_id": "ENSG00000091483",
            "omim_id": "",
            "genecard_link": "",
            "locs": "[Isoform Mitochondrial]: Mitochondrion; [Isoform Cytoplasmic]: Cytoplasm, cytosol; Nucleus; Chromosome;",
            "reaction": "(S)-malate = fumarate + H2O; (S)-malate = fumarate + H2O; (S)-malate = fumarate + H2O",
            "targ_desciption": "Catalyzes the reversible stereospecific interconversion offumarate to L-malate (PubMed:30761759). Experiments in other specieshave demonstrated that specific isoforms of this protein act in definedpathways and favor one direction over the other (Probable).{ECO:0000269|PubMed:30761759, ECO:0000305}.; [Isoform Mitochondrial]: Catalyzes the hydration of fumarateto L-malate in the tricarboxylic acid (TCA) cycle to facilitate atransition step in the production of energy in the form of NADH.{ECO:0000250|UniProtKB:P10173}.; [Isoform Cytoplasmic]: Catalyzes the dehydration of L-malateto fumarate (By similarity). Fumarate metabolism in the cytosol plays arole during urea cycle and arginine metabolism. fumarate being a by-product of the urea cycle and amino-acid catabolism (By similarity).Also plays a role in DNA repair by promoting non-homologous end-joining(NHEJ) (PubMed:20231875, PubMed:26237645). In response to DNA damageand phosphorylation by PRKDC, translocates to the nucleus andaccumulates at DNA double-strand breaks (DSBs): acts by catalyzingformation of fumarate, an inhibitor of KDM2B histone demethylaseactivity, resulting in enhanced dimethylation of histone H3 'Lys-36'(H3K36me2) (PubMed:26237645). {ECO:0000250|UniProtKB:P97807,ECO:0000269|PubMed:20231875, ECO:0000269|PubMed:26237645}.",
            "references": []
        },
        {
            "targ_id": "T099",
            "parent_targ_id": "T",
            "full_name": "Malate dehydrogenase, cytoplasmic",
            "abbrev": "MDH",
            "protein_names": "Malate dehydrogenase, cytoplasmic (EC 1.1.1.37) (Cytosolic malate dehydrogenase) (Diiodophenylpyruvate reductase) (EC 1.1.1.96)",
            "related_func_ids": "F0203",
            "category": "enzyme",
            "subcategories": "Oxidoreductase",
            "Uniport_ID": "P40925",
            "Uniprot_name": "MDHC_HUMAN",
            "EC_numbers": "1.1.1.37; 1.1.1.96",
            "gene_symbol": "MDH1",
            "gene_synonyms": "",
            "gene_synonyms_links": "",
            "gene_name": "Malate dehydrogenase 1",
            "hgnc_id": "",
            "entrez_id": "",
            "ensembl_id": "ENSG00000014641",
            "omim_id": "",
            "genecard_link": "",
            "locs": "Cytoplasm",
            "reaction": "(S)-malate + NAD(+) = H(+) + NADH + oxaloacetate; 3-(3,5-diiodo-4-hydroxyphenyl)lactate + NAD(+) = 3-(3,5-diiodo-4-hydroxyphenyl)pyruvate + H(+) + NADH",
            "targ_desciption": "",
            "references": []
        },
        {
            "targ_id": "T100",
            "parent_targ_id": "T",
            "full_name": "Malate dehydrogenase, mitochondrial",
            "abbrev": "MDH2",
            "protein_names": "Malate dehydrogenase, mitochondrial (EC 1.1.1.37)",
            "related_func_ids": "F0203",
            "category": "enzyme",
            "subcategories": "Oxidoreductase",
            "Uniport_ID": "P40926",
            "Uniprot_name": "MDHM_HUMAN",
            "EC_numbers": "1.1.1.37",
            "gene_symbol": "MDH2",
            "gene_synonyms": "",
            "gene_synonyms_links": "",
            "gene_name": "Malate dehydrogenase 2",
            "hgnc_id": "",
            "entrez_id": "",
            "ensembl_id": "ENSG00000146701",
            "omim_id": "",
            "genecard_link": "",
            "locs": "Mitochondrion matrix",
            "reaction": "(S)-malate + NAD(+) = H(+) + NADH + oxaloacetate",
            "targ_desciption": "",
            "references": [
                "RC04744"
            ]
        },
        {
            "targ_id": "T101",
            "parent_targ_id": "T",
            "full_name": "Malate:quinone oxidoreductase",
            "abbrev": "MQO",
            "protein_names": "Malate:quinone oxidoreductase (Fragment)",
            "related_func_ids": "F0203",
            "category": "enzyme",
            "subcategories": "oxidoreductase",
            "Uniport_ID": "W1Y062",
            "Uniprot_name": "W1Y062_9ZZZZ",
            "EC_numbers": "",
            "gene_symbol": "Q604_UNBC09769G0001",
            "gene_synonyms": "",
            "gene_synonyms_links": "",
            "gene_name": "",
            "hgnc_id": "",
            "entrez_id": "",
            "ensembl_id": "",
            "omim_id": "",
            "genecard_link": "",
            "locs": "",
            "reaction": "",
            "targ_desciption": "",
            "references": [
                "RC01136",
                "RC01137"
            ]
        },
        {
            "targ_id": "T102",
            "parent_targ_id": "T",
            "full_name": "Probable 2-oxoglutarate dehydrogenase E1 component DHKTD1, mitochondrial",
            "abbrev": "Dehydrogenase E1 and transketolase domain-containing protein 1",
            "protein_names": "Probable 2-oxoglutarate dehydrogenase E1 component DHKTD1, mitochondrial (EC 1.2.4.2) (Dehydrogenase E1 and transketolase domain-containing protein 1)",
            "related_func_ids": "F0203",
            "category": "enzyme",
            "subcategories": "Oxidoreductase",
            "Uniport_ID": "Q96HY7",
            "Uniprot_name": "DHTK1_HUMAN",
            "EC_numbers": "1.2.4.2",
            "gene_symbol": "DHTKD1",
            "gene_synonyms": "CMT2Q, DKFZP762M115, KIAA1630, MGC3090",
            "gene_synonyms_links": "",
            "gene_name": "Dehydrogenase E1 and transketolase domain containing 1",
            "hgnc_id": "",
            "entrez_id": "",
            "ensembl_id": "ENSG00000181192",
            "omim_id": "",
            "genecard_link": "",
            "locs": "Mitochondrion",
            "reaction": "2-oxoglutarate + [dihydrolipoyllysine-residuesuccinyltransferase]-(R)-N(6)-lipoyl-L-lysine + H(+) =[dihydrolipoyllysine-residue succinyltransferase]-(R)-N(6)-(S(8)-succinyldihydrolipoyl)-L-lysine + CO2",
            "targ_desciption": "The 2-oxoglutarate dehydrogenase complex catalyzes theoverall conversion of 2-oxoglutarate to succinyl-CoA and CO(2). Itcontains multiple copies of three enzymatic components: 2-oxoglutaratedehydrogenase (E1), dihydrolipoamide succinyltransferase (E2) andlipoamide dehydrogenase (E3) (By similarity). {ECO:0000250}.",
            "references": []
        },
        {
            "targ_id": "T103",
            "parent_targ_id": "T",
            "full_name": "NAD(P)H-hydrate epimerase",
            "abbrev": "NAD(P)HX epimerase",
            "protein_names": "NAD(P)H-hydrate epimerase (EC 5.1.99.6) (Apolipoprotein A-I-binding protein) (AI-BP) (NAD(P)HX epimerase) (YjeF N-terminal domain-containing protein 1) (YjeF_N1)",
            "related_func_ids": "F0203",
            "category": "enzyme",
            "subcategories": "Isomerase",
            "Uniport_ID": "Q8NCW5",
            "Uniprot_name": "NNRE_HUMAN",
            "EC_numbers": "5.1.99.6",
            "gene_symbol": "NAXE",
            "gene_synonyms": "AIBP, APOA1BP, MGC119143, MGC119144, MGC119145, YJEFN1",
            "gene_synonyms_links": "",
            "gene_name": "NAD(P)HX epimerase",
            "hgnc_id": "",
            "entrez_id": "",
            "ensembl_id": "ENSG00000163382",
            "omim_id": "",
            "genecard_link": "",
            "locs": "Mitochondrion; Secreted",
            "reaction": "(6R)-NADHX = (6S)-NADHX; (6R)-NADPHX = (6S)-NADPHX",
            "targ_desciption": "Catalyzes the epimerization of the S- and R-forms ofNAD(P)HX, a damaged form of NAD(P)H that is a result of enzymatic orheat-dependent hydration. This is a prerequisite for the S-specificNAD(P)H-hydrate dehydratase to allow the repair of both epimers ofNAD(P)HX. Accelerates cholesterol efflux from endothelial cells tohigh-density lipoprotein (HDL) and thereby regulates angiogenesis(PubMed:23719382). {ECO:0000255|HAMAP-Rule:MF_03159,ECO:0000269|PubMed:23719382, ECO:0000269|PubMed:27616477}.",
            "references": []
        },
        {
            "targ_id": "T104",
            "parent_targ_id": "T",
            "full_name": "NADP-dependent malic enzyme, mitochondrial",
            "abbrev": "NADP-ME",
            "protein_names": "NADP-dependent malic enzyme, mitochondrial (NADP-ME) (EC 1.1.1.40) (Malic enzyme 3)",
            "related_func_ids": "F0203",
            "category": "enzyme",
            "subcategories": "Oxidoreductase",
            "Uniport_ID": "Q16798",
            "Uniprot_name": "MAON_HUMAN",
            "EC_numbers": "1.1.1.40",
            "gene_symbol": "ME3",
            "gene_synonyms": "",
            "gene_synonyms_links": "",
            "gene_name": "Malic enzyme 3",
            "hgnc_id": "",
            "entrez_id": "",
            "ensembl_id": "ENSG00000151376",
            "omim_id": "",
            "genecard_link": "",
            "locs": "Mitochondrion matrix",
            "reaction": "(S)-malate + NADP(+) = CO2 + NADPH + pyruvate; H(+) + oxaloacetate = CO2 + pyruvate",
            "targ_desciption": "",
            "references": [
                "RC03769",
                "RC03770"
            ]
        },
        {
            "targ_id": "T105",
            "parent_targ_id": "T",
            "full_name": "NAD-dependent malic enzyme, mitochondrial",
            "abbrev": "NAD-ME",
            "protein_names": "NAD-dependent malic enzyme, mitochondrial (NAD-ME) (EC 1.1.1.38) (Malic enzyme 2)",
            "related_func_ids": "F0203",
            "category": "enzyme",
            "subcategories": "Allosteric enzyme, Oxidoreductase",
            "Uniport_ID": "P23368",
            "Uniprot_name": "MAOM_HUMAN",
            "EC_numbers": "1.1.1.38",
            "gene_symbol": "ME2",
            "gene_synonyms": "",
            "gene_synonyms_links": "",
            "gene_name": "Malic enzyme 2",
            "hgnc_id": "",
            "entrez_id": "",
            "ensembl_id": "ENSG00000082212",
            "omim_id": "",
            "genecard_link": "",
            "locs": "Mitochondrion matrix",
            "reaction": "(S)-malate + NAD(+) = CO2 + NADH + pyruvate; H(+) + oxaloacetate = CO2 + pyruvate",
            "targ_desciption": "",
            "references": []
        },
        {
            "targ_id": "T106",
            "parent_targ_id": "T",
            "full_name": "citrate",
            "abbrev": "citrate",
            "protein_names": "",
            "related_func_ids": "F0203",
            "category": "metabolite",
            "subcategories": "",
            "Uniport_ID": "",
            "Uniprot_name": "",
            "EC_numbers": "",
            "gene_symbol": "",
            "gene_synonyms": "",
            "gene_synonyms_links": "",
            "gene_name": "",
            "hgnc_id": "",
            "entrez_id": "",
            "ensembl_id": "",
            "omim_id": "",
            "genecard_link": "",
            "locs": "",
            "reaction": "",
            "targ_desciption": "",
            "references": [
                "RC00668",
                "RC00669",
                "RC00682",
                "RC00683"
            ]
        },
        {
            "targ_id": "T107",
            "parent_targ_id": "T",
            "full_name": "isocitrate",
            "abbrev": "isocitrate",
            "protein_names": "",
            "related_func_ids": "F0203",
            "category": "metabolite",
            "subcategories": "",
            "Uniport_ID": "",
            "Uniprot_name": "",
            "EC_numbers": "",
            "gene_symbol": "",
            "gene_synonyms": "",
            "gene_synonyms_links": "",
            "gene_name": "",
            "hgnc_id": "",
            "entrez_id": "",
            "ensembl_id": "",
            "omim_id": "",
            "genecard_link": "",
            "locs": "",
            "reaction": "",
            "targ_desciption": "",
            "references": [
                "RC00670",
                "RC00671"
            ]
        },
        {
            "targ_id": "T108",
            "parent_targ_id": "T",
            "full_name": "alpha-ketoglutarate",
            "abbrev": "alpha-ketoglutarate",
            "protein_names": "",
            "related_func_ids": "F0203",
            "category": "metabolite",
            "subcategories": "",
            "Uniport_ID": "",
            "Uniprot_name": "",
            "EC_numbers": "",
            "gene_symbol": "",
            "gene_synonyms": "",
            "gene_synonyms_links": "",
            "gene_name": "",
            "hgnc_id": "",
            "entrez_id": "",
            "ensembl_id": "",
            "omim_id": "",
            "genecard_link": "",
            "locs": "",
            "reaction": "",
            "targ_desciption": "",
            "references": [
                "RC00672",
                "RC00673",
                "RC00684",
                "RC00685"
            ]
        },
        {
            "targ_id": "T109",
            "parent_targ_id": "T",
            "full_name": "succinate",
            "abbrev": "succinate",
            "protein_names": "",
            "related_func_ids": "F0203",
            "category": "metabolite",
            "subcategories": "",
            "Uniport_ID": "",
            "Uniprot_name": "",
            "EC_numbers": "",
            "gene_symbol": "",
            "gene_synonyms": "",
            "gene_synonyms_links": "",
            "gene_name": "",
            "hgnc_id": "",
            "entrez_id": "",
            "ensembl_id": "",
            "omim_id": "",
            "genecard_link": "",
            "locs": "",
            "reaction": "",
            "targ_desciption": "",
            "references": [
                "RC00686",
                "RC00687"
            ]
        },
        {
            "targ_id": "T110",
            "parent_targ_id": "T",
            "full_name": "Aspartate aminotransferase, mitochondrial",
            "abbrev": "mAspAT",
            "protein_names": "Aspartate aminotransferase, mitochondrial (mAspAT) (EC 2.6.1.1) (EC 2.6.1.7) (Fatty acid-binding protein) (FABP-1) (Glutamate oxaloacetate transaminase 2) (Kynurenine aminotransferase 4) (Kynurenine aminotransferase IV) (Kynurenine--oxoglutarate transaminase 4) (Kynurenine--oxoglutarate transaminase IV) (Plasma membrane-associated fatty acid-binding protein) (FABPpm) (Transaminase A)",
            "related_func_ids": "F020703; F020704; F020706; F020707; F0216; F020402",
            "category": "enzyme",
            "subcategories": "Aminotransferase, Transferase",
            "Uniport_ID": "P00505",
            "Uniprot_name": "AATM_HUMAN",
            "EC_numbers": "2.6.1.1; 2.6.1.7",
            "gene_symbol": "GOT2",
            "gene_synonyms": "KAT4, KATIV, KYAT4, mitAAT",
            "gene_synonyms_links": "",
            "gene_name": "Glutamic-oxaloacetic transaminase 2",
            "hgnc_id": "",
            "entrez_id": "",
            "ensembl_id": "ENSG00000125166",
            "omim_id": "",
            "genecard_link": "",
            "locs": "Mitochondrion matrix; Cell membrane",
            "reaction": "2-oxoglutarate + L-aspartate = L-glutamate + oxaloacetate; 2-oxoglutarate + L-kynurenine = 4-(2-aminophenyl)-2,4-dioxobutanoate + L-glutamate",
            "targ_desciption": "Catalyzes the irreversible transamination of the L-tryptophanmetabolite L-kynurenine to form kynurenic acid (KA). As a member of themalate-aspartate shuttle, it has a key role in the intracellular NAD(H)redox balance. Is important for metabolite exchange betweenmitochondria and cytosol, and for amino acid metabolism. Facilitatescellular uptake of long-chain free fatty acids.{ECO:0000269|PubMed:31422819, ECO:0000269|PubMed:9537447}.",
            "references": [
                "RC03482"
            ]
        },
        {
            "targ_id": "T111",
            "parent_targ_id": "T",
            "full_name": "Delta-1-pyrroline-5-carboxylate dehydrogenase, mitochondrial",
            "abbrev": "P5C dehydrogenase",
            "protein_names": "Delta-1-pyrroline-5-carboxylate dehydrogenase, mitochondrial (P5C dehydrogenase) (EC 1.2.1.88) (Aldehyde dehydrogenase family 4 member A1) (L-glutamate gamma-semialdehyde dehydrogenase)",
            "related_func_ids": "F020715; F0216",
            "category": "enzyme",
            "subcategories": "Oxidoreductase",
            "Uniport_ID": "P30038",
            "Uniprot_name": "AL4A1_HUMAN",
            "EC_numbers": "1.2.1.88",
            "gene_symbol": "ALDH4A1",
            "gene_synonyms": "ALDH4, P5CDh",
            "gene_synonyms_links": "",
            "gene_name": "Aldehyde dehydrogenase 4 family member A1",
            "hgnc_id": "",
            "entrez_id": "",
            "ensembl_id": "ENSG00000159423",
            "omim_id": "",
            "genecard_link": "",
            "locs": "Mitochondrion matrix",
            "reaction": "H2O + L-glutamate 5-semialdehyde + NAD(+) = 2 H(+) + L-glutamate + NADH",
            "targ_desciption": "Irreversible conversion of delta-1-pyrroline-5-carboxylate(P5C), derived either from proline or ornithine, to glutamate. This isa necessary step in the pathway interconnecting the urea andtricarboxylic acid cycles. The preferred substrate is glutamic gamma-semialdehyde, other substrates include succinic, glutaric and adipicsemialdehydes. {ECO:0000269|PubMed:22516612}.",
            "references": []
        },
        {
            "targ_id": "T112",
            "parent_targ_id": "T",
            "full_name": "Alanine--glyoxylate aminotransferase 2, mitochondrial",
            "abbrev": "AGT 2",
            "protein_names": "Alanine--glyoxylate aminotransferase 2, mitochondrial (AGT 2) (EC 2.6.1.44) ((R)-3-amino-2-methylpropionate--pyruvate transaminase) (EC 2.6.1.40) (Beta-ALAAT II) (Beta-alanine-pyruvate aminotransferase) (D-AIBAT)",
            "related_func_ids": "F0216; F020708; F020701",
            "category": "enzyme",
            "subcategories": "Aminotransferase, Transferase",
            "Uniport_ID": "Q9BYV1",
            "Uniprot_name": "AGT2_HUMAN",
            "EC_numbers": "2.6.1.44; 2.6.1.40",
            "gene_symbol": "AGXT2",
            "gene_synonyms": "AGT2",
            "gene_synonyms_links": "",
            "gene_name": "Alanine--glyoxylate aminotransferase 2",
            "hgnc_id": "",
            "entrez_id": "",
            "ensembl_id": "ENSG00000113492",
            "omim_id": "",
            "genecard_link": "",
            "locs": "Mitochondrion",
            "reaction": "glyoxylate + L-alanine = glycine + pyruvate; (R)-3-amino-2-methylpropanoate + pyruvate = 2-methyl-3-oxopropanoate + L-alanine",
            "targ_desciption": "Can metabolize asymmetric dimethylarginine (ADMA) viatransamination to alpha-keto-delta-(NN-dimethylguanidino) valeric acid(DMGV). ADMA is a potent inhibitor of nitric-oxide (NO) synthase, andthis activity provides mechanism through which the kidney regulatesblood pressure. {ECO:0000269|PubMed:20018850,ECO:0000269|PubMed:23023372, ECO:0000269|PubMed:24586340}.",
            "references": []
        },
        {
            "targ_id": "T113",
            "parent_targ_id": "T",
            "full_name": "Glycine cleavage system H protein, mitochondrial",
            "abbrev": "Lipoic acid-containing protein",
            "protein_names": "Glycine cleavage system H protein, mitochondrial (Lipoic acid-containing protein)",
            "related_func_ids": "F0216; F020708",
            "category": "protein",
            "subcategories": "",
            "Uniport_ID": "P23434",
            "Uniprot_name": "GCSH_HUMAN",
            "EC_numbers": "",
            "gene_symbol": "GCSH",
            "gene_synonyms": "",
            "gene_synonyms_links": "",
            "gene_name": "Glycine cleavage system protein H",
            "hgnc_id": "",
            "entrez_id": "",
            "ensembl_id": "ENSG00000140905",
            "omim_id": "",
            "genecard_link": "",
            "locs": "Mitochondrion",
            "reaction": "",
            "targ_desciption": "The glycine cleavage system catalyzes the degradation ofglycine. The H protein (GCSH) shuttles the methylamine group of glycinefrom the P protein (GLDC) to the T protein (GCST).{ECO:0000269|PubMed:1671321}.",
            "references": []
        },
        {
            "targ_id": "T114",
            "parent_targ_id": "T",
            "full_name": "Transketolase",
            "abbrev": "TKT",
            "protein_names": "Transketolase (TK) (EC 2.2.1.1)",
            "related_func_ids": "F0205",
            "category": "enzyme",
            "subcategories": "",
            "Uniport_ID": "P29401",
            "Uniprot_name": "TKT_HUMAN",
            "EC_numbers": "2.2.1.1",
            "gene_symbol": "TKT",
            "gene_synonyms": "",
            "gene_synonyms_links": "",
            "gene_name": "",
            "hgnc_id": "",
            "entrez_id": "",
            "ensembl_id": "",
            "omim_id": "",
            "genecard_link": "",
            "locs": "",
            "reaction": "D-glyceraldehyde 3-phosphate + D-sedoheptulose 7-phosphate =aldehydo-D-ribose 5-phosphate + D-xylulose 5-phosphate",
            "targ_desciption": "Catalyzes the transfer of a two-carbon ketol group from aketose donor to an aldose acceptor, via a covalent intermediate withthe cofactor thiamine pyrophosphate. {ECO:0000269|PubMed:27259054}.",
            "references": []
        },
        {
            "targ_id": "T115",
            "parent_targ_id": "T",
            "full_name": "Phosphoenolpyruvate carboxykinase [GTP], mitochondrial",
            "abbrev": "PEPCK-M",
            "protein_names": "Phosphoenolpyruvate carboxykinase [GTP], mitochondrial (PEPCK-M) (EC 4.1.1.32)",
            "related_func_ids": "F020402",
            "category": "enzyme",
            "subcategories": "Decarboxylase, Lyase",
            "Uniport_ID": "Q16822",
            "Uniprot_name": "PCKGM_HUMAN",
            "EC_numbers": "4.1.1.32",
            "gene_symbol": "PCK2",
            "gene_synonyms": "PEPCK, PEPCK2",
            "gene_synonyms_links": "",
            "gene_name": "Phosphoenolpyruvate carboxykinase 2, mitochondrial",
            "hgnc_id": "",
            "entrez_id": "",
            "ensembl_id": "ENSG00000100889",
            "omim_id": "",
            "genecard_link": "",
            "locs": "Mitochondrion",
            "reaction": "GTP + oxaloacetate = CO2 + GDP + phosphoenolpyruvate",
            "targ_desciption": "Catalyzes the conversion of oxaloacetate (OAA) tophosphoenolpyruvate (PEP), the rate-limiting step in the metabolicpathway that produces glucose from lactate and other precursors derivedfrom the citric acid cycle. {ECO:0000250}.",
            "references": []
        },
        {
            "targ_id": "T116",
            "parent_targ_id": "T",
            "full_name": "Creatine kinase, mitochondrial",
            "abbrev": "MtCK",
            "protein_names": "",
            "related_func_ids": "F0218",
            "category": "enzyme family",
            "subcategories": "",
            "Uniport_ID": "",
            "Uniprot_name": "",
            "EC_numbers": "",
            "gene_symbol": "",
            "gene_synonyms": "",
            "gene_synonyms_links": "",
            "gene_name": "",
            "hgnc_id": "",
            "entrez_id": "",
            "ensembl_id": "",
            "omim_id": "",
            "genecard_link": "",
            "locs": "",
            "reaction": "",
            "targ_desciption": "",
            "references": []
        },
        {
            "targ_id": "T116001",
            "parent_targ_id": "T116",
            "full_name": "Creatine kinase U-type, mitochondrial",
            "abbrev": "U-MtCK",
            "protein_names": "Creatine kinase U-type, mitochondrial (EC 2.7.3.2) (Acidic-type mitochondrial creatine kinase) (Mia-CK) (Ubiquitous mitochondrial creatine kinase) (U-MtCK)",
            "related_func_ids": "F0218",
            "category": "enzyme",
            "subcategories": "Kinase, Transferase",
            "Uniport_ID": "P12532",
            "Uniprot_name": "KCRU_HUMAN",
            "EC_numbers": "2.7.3.2",
            "gene_symbol": "CKMT1A",
            "gene_synonyms": "CKMT1",
            "gene_synonyms_links": "",
            "gene_name": "Creatine kinase, mitochondrial 1A",
            "hgnc_id": "",
            "entrez_id": "",
            "ensembl_id": "ENSG00000223572",
            "omim_id": "",
            "genecard_link": "",
            "locs": "Mitochondrion inner membrane; Peripheral membrane protein; Intermembrane side",
            "reaction": "ATP + creatine = ADP + H(+) + N-phosphocreatine",
            "targ_desciption": "Reversibly catalyzes the transfer of phosphate between ATPand various phosphogens (e.g. creatine phosphate). Creatine kinaseisoenzymes play a central role in energy transduction in tissues withlarge, fluctuating energy demands, such as skeletal muscle, heart,brain and spermatozoa.",
            "references": []
        },
        {
            "targ_id": "T116002",
            "parent_targ_id": "T116",
            "full_name": "Creatine kinase S-type, mitochondrial",
            "abbrev": "S-MtCK",
            "protein_names": "Creatine kinase S-type, mitochondrial (EC 2.7.3.2) (Basic-type mitochondrial creatine kinase) (Mib-CK) (Sarcomeric mitochondrial creatine kinase) (S-MtCK)",
            "related_func_ids": "F0218",
            "category": "enzyme",
            "subcategories": "Kinase, Transferase",
            "Uniport_ID": "P17540",
            "Uniprot_name": "KCRS_HUMAN",
            "EC_numbers": "2.7.3.2",
            "gene_symbol": "CKMT2",
            "gene_synonyms": "SMTCK",
            "gene_synonyms_links": "",
            "gene_name": "Creatine kinase, mitochondrial 2",
            "hgnc_id": "",
            "entrez_id": "",
            "ensembl_id": "ENSG00000131730",
            "omim_id": "",
            "genecard_link": "",
            "locs": "Mitochondrion inner membrane; Peripheral membrane protein; Intermembrane side",
            "reaction": "ATP + creatine = ADP + H(+) + N-phosphocreatine",
            "targ_desciption": "Reversibly catalyzes the transfer of phosphate between ATPand various phosphogens (e.g. creatine phosphate). Creatine kinaseisoenzymes play a central role in energy transduction in tissues withlarge, fluctuating energy demands, such as skeletal muscle, heart,brain and spermatozoa.",
            "references": []
        },
        {
            "targ_id": "T117",
            "parent_targ_id": "T",
            "full_name": "Glycogen synthase kinase-3 beta",
            "abbrev": "GSK-3 beta",
            "protein_names": "Glycogen synthase kinase-3 beta (GSK-3 beta) (EC 2.7.11.26) (Serine/threonine-protein kinase GSK3B) (EC 2.7.11.1)",
            "related_func_ids": "F0208; F0809",
            "category": "enzyme",
            "subcategories": "Developmental protein, Kinase, Serine/threonine-protein kinase, Signal transduction inhibitor, Transferase",
            "Uniport_ID": "P49841",
            "Uniprot_name": "GSK3B_HUMAN",
            "EC_numbers": "2.7.11.26; 2.7.11.1",
            "gene_symbol": "GSK3B",
            "gene_synonyms": "",
            "gene_synonyms_links": "",
            "gene_name": "Glycogen synthase kinase 3 beta",
            "hgnc_id": "",
            "entrez_id": "",
            "ensembl_id": "ENSG00000082701",
            "omim_id": "",
            "genecard_link": "",
            "locs": "Cytoplasm; Nucleus; Cell membrane",
            "reaction": "[tau protein]-L-serine + ATP = [tau protein]-O-phospho-L-serine + ADP + H(+); [tau protein]-L-threonine + ATP = [tau protein]-O-phospho-L-threonine + ADP + H(+); ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]; ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-threonyl-[protein]",
            "targ_desciption": "Constitutively active protein kinase that acts as a negativeregulator in the hormonal control of glucose homeostasis, Wnt signalingand regulation of transcription factors and microtubules, byphosphorylating and inactivating glycogen synthase (GYS1 or GYS2),EIF2B, CTNNB1/beta-catenin, APC, AXIN1, DPYSL2/CRMP2, JUN,NFATC1/NFATC, MAPT/TAU and MACF1. Requires primed phosphorylation ofthe majority of its substrates. In skeletal muscle, contributes toinsulin regulation of glycogen synthesis by phosphorylating andinhibiting GYS1 activity and hence glycogen synthesis. May also mediatethe development of insulin resistance by regulating activation oftranscription factors. Regulates protein synthesis by controlling theactivity of initiation factor 2B (EIF2BE/EIF2B5) in the same manner asglycogen synthase. In Wnt signaling, GSK3B forms a multimeric complexwith APC, AXIN1 and CTNNB1/beta-catenin and phosphorylates the N-terminus of CTNNB1 leading to its degradation mediated byubiquitin/proteasomes. Phosphorylates JUN at sites proximal to its DNA-binding domain, thereby reducing its affinity for DNA. PhosphorylatesNFATC1/NFATC on conserved serine residues promoting NFATC1/NFATCnuclear export, shutting off NFATC1/NFATC gene regulation, and therebyopposing the action of calcineurin. Phosphorylates MAPT/TAU on 'Thr-548', decreasing significantly MAPT/TAU ability to bind and stabilizemicrotubules. MAPT/TAU is the principal component of neurofibrillarytangles in Alzheimer disease. Plays an important role in ERBB2-dependent stabilization of microtubules at the cell cortex.Phosphorylates MACF1, inhibiting its binding to microtubules which iscritical for its role in bulge stem cell migration and skin woundrepair. Probably regulates NF-kappa-B (NFKB1) at the transcriptionallevel and is required for the NF-kappa-B-mediated anti-apoptoticresponse to TNF-alpha (TNF/TNFA). Negatively regulates replication inpancreatic beta-cells, resulting in apoptosis, loss of beta-cells anddiabetes. Through phosphorylation of the anti-apoptotic protein MCL1,may control cell apoptosis in response to growth factors deprivation.Phosphorylates MUC1 in breast cancer cells, decreasing the interactionof MUC1 with CTNNB1/beta-catenin. Is necessary for the establishment ofneuronal polarity and axon outgrowth. Phosphorylates MARK2, leading toinhibit its activity. Phosphorylates SIK1 at 'Thr-182', leading tosustain its activity. Phosphorylates ZC3HAV1 which enhances itsantiviral activity. Phosphorylates SNAI1, leading to its BTRC-triggeredubiquitination and proteasomal degradation. Phosphorylates SFPQ at'Thr-687' upon T-cell activation. Phosphorylates NR1D1 st 'Ser-55' and'Ser-59' and stabilizes it by protecting it from proteasomaldegradation. Regulates the circadian clock via phosphorylation of themajor clock components including ARNTL/BMAL1, CLOCK and PER2(PubMed:19946213, PubMed:28903391). Phosphorylates CLOCK AT 'Ser-427'and targets it for proteasomal degradation (PubMed:19946213).Phosphorylates ARNTL/BMAL1 at 'Ser-17' and 'Ser-21' and primes it forubiquitination and proteasomal degradation (PubMed:28903391).Phosphorylates OGT at 'Ser-3' or 'Ser-4' which positively regulates itsactivity. Phosphorylates MYCN in neuroblastoma cells which may promoteits degradation (PubMed:24391509). Regulates the circadian rhythmicityof hippocampal long-term potentiation and ARNTL/BMLA1 and PER2expression (By similarity). Acts as a regulator of autophagy bymediating phosphorylation of KAT5/TIP60 under starvation conditions,leading to activate KAT5/TIP60 acetyltransferase activity and promoteacetylation of key autophagy regulators, such as ULK1 and RUBCNL/Pacer(PubMed:30704899). Negatively regulates extrinsic apoptotic signalingpathway via death domain receptors. Promotes the formation of an anti-apoptotic complex, made of DDX3X, BRIC2 and GSK3B, at death receptors,including TNFRSF10B. The anti-apoptotic function is most effective withweak apoptotic signals and can be overcome by stronger stimulation(PubMed:18846110). {ECO:0000250|UniProtKB:Q9WV60,ECO:0000269|PubMed:11430833, ECO:0000269|PubMed:12554650,ECO:0000269|PubMed:14690523, ECO:0000269|PubMed:15448698,ECO:0000269|PubMed:15647282, ECO:0000269|PubMed:16484495,ECO:0000269|PubMed:18348280, ECO:0000269|PubMed:1846781,ECO:0000269|PubMed:18846110, ECO:0000269|PubMed:19946213,ECO:0000269|PubMed:20932480, ECO:0000269|PubMed:20937854,ECO:0000269|PubMed:22514281, ECO:0000269|PubMed:24391509,ECO:0000269|PubMed:28903391, ECO:0000269|PubMed:30704899,ECO:0000269|PubMed:8397507, ECO:0000269|PubMed:9072970,ECO:0000269|PubMed:9819408}.",
            "references": []
        },
        {
            "targ_id": "T118",
            "parent_targ_id": "T",
            "full_name": "Peptidyl-prolyl cis-trans isomerase F, mitochondrial",
            "abbrev": "PPIase F",
            "protein_names": "Peptidyl-prolyl cis-trans isomerase F, mitochondrial (PPIase F) (EC 5.2.1.8) (Cyclophilin D) (CyP-D) (CypD) (Cyclophilin F) (Mitochondrial cyclophilin) (CyP-M) (Rotamase F)",
            "related_func_ids": "F0704; F010401",
            "category": "enzyme",
            "subcategories": "Isomerase, Rotamase",
            "Uniport_ID": "P30405",
            "Uniprot_name": "PPIF_HUMAN",
            "EC_numbers": "5.2.1.8",
            "gene_symbol": "PPIF",
            "gene_synonyms": "Cyp-D, hCyP3",
            "gene_synonyms_links": "",
            "gene_name": "Peptidylprolyl isomerase F",
            "hgnc_id": "",
            "entrez_id": "",
            "ensembl_id": "ENSG00000108179",
            "omim_id": "",
            "genecard_link": "",
            "locs": "Mitochondrion matrix",
            "reaction": "[protein]-peptidylproline (omega=180) = [protein]-peptidylproline (omega=0)",
            "targ_desciption": "PPIase that catalyzes the cis-trans isomerization of prolineimidic peptide bonds in oligopeptides and may therefore assist proteinfolding (PubMed:20676357). Involved in regulation of the mitochondrialpermeability transition pore (mPTP). It is proposed that itsassociation with the mPTP is masking a binding site for inhibitinginorganic phosphate (Pi) and promotes the open probability of the mPTPleading to apoptosis or necrosis. the requirement of the PPIaseactivity for this function is debated. In cooperation withmitochondrial TP53 is involved in activating oxidative stress-inducednecrosis. Involved in modulation of mitochondrial membrane F(1)F(0) ATPsynthase activity and regulation of mitochondrial matrix adeninenucleotide levels. Has anti-apoptotic activity independently of mPTPand in cooperation with BCL2 inhibits cytochrome c-dependent apoptosis.{ECO:0000269|PubMed:19228691, ECO:0000269|PubMed:20676357,ECO:0000269|PubMed:22726440, ECO:0000269|PubMed:26387735}.",
            "references": [
                "RC03726",
                "RC03860",
                "RC03861"
            ]
        },
        {
            "targ_id": "T119",
            "parent_targ_id": "T",
            "full_name": "60 kDa heat shock protein, mitochondrial",
            "abbrev": "HSP-60",
            "protein_names": "60 kDa heat shock protein, mitochondrial (EC 5.6.1.7) (60 kDa chaperonin) (Chaperonin 60) (CPN60) (Heat shock protein 60) (HSP-60) (Hsp60) (HuCHA60) (Mitochondrial matrix protein P1) (P60 lymphocyte protein)",
            "related_func_ids": "F021102; F0701; F0209",
            "category": "protein",
            "subcategories": "Chaperone, Isomerase",
            "Uniport_ID": "P10809",
            "Uniprot_name": "CH60_HUMAN",
            "EC_numbers": "5.6.1.7",
            "gene_symbol": "HSPD1",
            "gene_synonyms": "GroEL, HSP60, SPG13",
            "gene_synonyms_links": "",
            "gene_name": "Heat shock protein family D (Hsp60) member 1",
            "hgnc_id": "",
            "entrez_id": "",
            "ensembl_id": "ENSG00000144381",
            "omim_id": "",
            "genecard_link": "",
            "locs": "Mitochondrion matrix",
            "reaction": "ATP + H(2)O + a folded polypeptide = ADP + phosphate + anunfolded polypeptide.",
            "targ_desciption": "Chaperonin implicated in mitochondrial protein import andmacromolecular assembly. Together with Hsp10, facilitates the correctfolding of imported proteins. May also prevent misfolding and promotethe refolding and proper assembly of unfolded polypeptides generatedunder stress conditions in the mitochondrial matrix (PubMed:1346131,PubMed:11422376). The functional units of these chaperonins consist ofheptameric rings of the large subunit Hsp60, which function as a back-to-back double ring. In a cyclic reaction, Hsp60 ring complexes bindone unfolded substrate protein per ring, followed by the binding of ATPand association with 2 heptameric rings of the co-chaperonin Hsp10.This leads to sequestration of the substrate protein in the innercavity of Hsp60 where, for a certain period of time, it can foldundisturbed by other cell components. Synchronous hydrolysis of ATP inall Hsp60 subunits results in the dissociation of the chaperonin ringsand the release of ADP and the folded substrate protein (Probable).{ECO:0000269|PubMed:11422376, ECO:0000269|PubMed:1346131,ECO:0000305|PubMed:25918392}.",
            "references": []
        },
        {
            "targ_id": "T120",
            "parent_targ_id": "T",
            "full_name": "Stress-70 protein, mitochondrial",
            "abbrev": "GRP-75",
            "protein_names": "Stress-70 protein, mitochondrial (75 kDa glucose-regulated protein) (GRP-75) (Heat shock 70 kDa protein 9) (Mortalin) (MOT) (Peptide-binding protein 74) (PBP74)",
            "related_func_ids": "F021102; F0701; F0806; F0209",
            "category": "protein",
            "subcategories": "Chaperone",
            "Uniport_ID": "P38646",
            "Uniprot_name": "GRP75_HUMAN",
            "EC_numbers": "",
            "gene_symbol": "HSPA9",
            "gene_synonyms": "GRP75, HSPA9B, mot-2, mthsp75, PBP74",
            "gene_synonyms_links": "",
            "gene_name": "Heat shock protein family A (Hsp70) member 9",
            "hgnc_id": "",
            "entrez_id": "",
            "ensembl_id": "ENSG00000113013",
            "omim_id": "",
            "genecard_link": "",
            "locs": "Mitochondrion; Nucleus, nucleolus",
            "reaction": "",
            "targ_desciption": "Chaperone protein which plays an important role inmitochondrial iron-sulfur cluster (ISC) biogenesis. Interacts with andstabilizes ISC cluster assembly proteins FXN, NFU1, NFS1 and ISCU(PubMed:26702583). Regulates erythropoiesis via stabilization of ISCassembly (PubMed:21123823, PubMed:26702583). May play a role in thecontrol of cell proliferation and cellular aging (By similarity).{ECO:0000250|UniProtKB:P38647, ECO:0000269|PubMed:21123823,ECO:0000269|PubMed:26702583}.",
            "references": []
        },
        {
            "targ_id": "T121",
            "parent_targ_id": "T",
            "full_name": "Heat shock protein HSP 90-alpha",
            "abbrev": "HSP 86",
            "protein_names": "Heat shock protein HSP 90-alpha (Heat shock 86 kDa) (HSP 86) (HSP86) (Lipopolysaccharide-associated protein 2) (LAP-2) (LPS-associated protein 2) (Renal carcinoma antigen NY-REN-38)",
            "related_func_ids": "F0807; F0810; F0210",
            "category": "protein",
            "subcategories": "Chaperone",
            "Uniport_ID": "P07900",
            "Uniprot_name": "HS90A_HUMAN",
            "EC_numbers": "",
            "gene_symbol": "HSP90AA1",
            "gene_synonyms": "FLJ31884, Hsp89, Hsp90, HSP90N, HSPC1, HSPCA",
            "gene_synonyms_links": "",
            "gene_name": "Heat shock protein 90 alpha family class A member 1",
            "hgnc_id": "",
            "entrez_id": "",
            "ensembl_id": "ENSG00000080824",
            "omim_id": "",
            "genecard_link": "",
            "locs": "Nucleus; Cytoplasm; Melanosome; Cell membrane",
            "reaction": "",
            "targ_desciption": "Molecular chaperone that promotes the maturation, structuralmaintenance and proper regulation of specific target proteins involvedfor instance in cell cycle control and signal transduction. Undergoes afunctional cycle that is linked to its ATPase activity which isessential for its chaperone activity. This cycle probably inducesconformational changes in the client proteins, thereby causing theiractivation. Interacts dynamically with various co-chaperones thatmodulate its substrate recognition, ATPase cycle and chaperone function(PubMed:11274138, PubMed:15577939, PubMed:15937123, PubMed:27353360,PubMed:29127155). Engages with a range of client protein classes viaits interaction with various co-chaperone proteins or complexes, thatact as adapters, simultaneously able to interact with the specificclient and the central chaperone itself (PubMed:29127155). Recruitmentof ATP and co-chaperone followed by client protein forms a functionalchaperone. After the completion of the chaperoning process, properlyfolded client protein and co-chaperone leave HSP90 in an ADP-boundpartially open conformation and finally, ADP is released from HSP90which acquires an open conformation for the next cycle(PubMed:27295069, PubMed:26991466). Apart from its chaperone activity,it also plays a role in the regulation of the transcription machinery.HSP90 and its co-chaperones modulate transcription at least at threedifferent levels (PubMed:25973397). In the first place, they alter thesteady-state levels of certain transcription factors in response tovarious physiological cues(PubMed:25973397). Second, they modulate theactivity of certain epigenetic modifiers, such as histone deacetylasesor DNA methyl transferases, and thereby respond to the change in theenvironment (PubMed:25973397). Third, they participate in the evictionof histones from the promoter region of certain genes and thereby turnon gene expression (PubMed:25973397). Binds bacteriallipopolysaccharide (LPS) and mediates LPS-induced inflammatoryresponse, including TNF secretion by monocytes (PubMed:11276205).Antagonizes STUB1-mediated inhibition of TGF-beta signaling viainhibition of STUB1-mediated SMAD3 ubiquitination and degradation(PubMed:24613385). {ECO:0000269|PubMed:11274138,ECO:0000269|PubMed:11276205, ECO:0000269|PubMed:15577939,ECO:0000269|PubMed:15937123, ECO:0000269|PubMed:24613385,ECO:0000269|PubMed:27353360, ECO:0000269|PubMed:29127155,ECO:0000303|PubMed:25973397, ECO:0000303|PubMed:26991466,ECO:0000303|PubMed:27295069}.",
            "references": [
                "RC03754"
            ]
        },
        {
            "targ_id": "T122",
            "parent_targ_id": "T",
            "full_name": "Heat shock protein HSP 90-beta",
            "abbrev": "HSP 90",
            "protein_names": "Heat shock protein HSP 90-beta (HSP 90) (Heat shock 84 kDa) (HSP 84) (HSP84)",
            "related_func_ids": "F0210",
            "category": "protein",
            "subcategories": "",
            "Uniport_ID": "P08238",
            "Uniprot_name": "HS90B_HUMAN",
            "EC_numbers": "",
            "gene_symbol": "HSP90AB1 HSP90B HSPC2 HSPCB",
            "gene_synonyms": "",
            "gene_synonyms_links": "",
            "gene_name": "",
            "hgnc_id": "",
            "entrez_id": "",
            "ensembl_id": "",
            "omim_id": "",
            "genecard_link": "",
            "locs": "Cytoplasm; Melanosome; Nucleus; Secreted; Cell membrane",
            "reaction": "",
            "targ_desciption": "Molecular chaperone that promotes the maturation, structuralmaintenance and proper regulation of specific target proteins involvedfor instance in cell cycle control and signal transduction. Undergoes afunctional cycle that is linked to its ATPase activity. This cycleprobably induces conformational changes in the client proteins, therebycausing their activation. Interacts dynamically with various co-chaperones that modulate its substrate recognition, ATPase cycle andchaperone function (PubMed:16478993, PubMed:19696785). Engages with arange of client protein classes via its interaction with various co-chaperone proteins or complexes, that act as adapters, simultaneouslyable to interact with the specific client and the central chaperoneitself. Recruitment of ATP and co-chaperone followed by client proteinforms a functional chaperone. After the completion of the chaperoningprocess, properly folded client protein and co-chaperone leave HSP90 inan ADP-bound partially open conformation and finally, ADP is releasedfrom HSP90 which acquires an open conformation for the next cycle(PubMed:27295069, PubMed:26991466). Apart from its chaperone activity,it also plays a role in the regulation of the transcription machinery.HSP90 and its co-chaperones modulate transcription at least at threedifferent levels. In the first place, they alter the steady-statelevels of certain transcription factors in response to variousphysiological cues. Second, they modulate the activity of certainepigenetic modifiers, such as histone deacetylases or DNA methyltransferases, and thereby respond to the change in the environment.Third, they participate in the eviction of histones from the promoterregion of certain genes and thereby turn on gene expression(PubMed:25973397). Antagonizes STUB1-mediated inhibition of TGF-betasignaling via inhibition of STUB1-mediated SMAD3 ubiquitination anddegradation (PubMed:24613385). Promotes cell differentiation bychaperoning BIRC2 and thereby protecting from auto-ubiquitination anddegradation by the proteasomal machinery (PubMed:18239673). Mainchaperone that is involved in the phosphorylation/activation of theSTAT1 by chaperoning both JAK2 and PRKCE under heat shock and in turn,activates its own transcription (PubMed:20353823).{ECO:0000269|PubMed:16478993, ECO:0000269|PubMed:18239673,ECO:0000269|PubMed:19696785, ECO:0000269|PubMed:20353823,ECO:0000269|PubMed:24613385, ECO:0000303|PubMed:25973397,ECO:0000303|PubMed:26991466, ECO:0000303|PubMed:27295069}.",
            "references": []
        },
        {
            "targ_id": "T123",
            "parent_targ_id": "T",
            "full_name": "Heat shock protein 75 kDa, mitochondrial",
            "abbrev": "HSP 75",
            "protein_names": "Heat shock protein 75 kDa, mitochondrial (HSP 75) (TNFR-associated protein 1) (Tumor necrosis factor type 1 receptor-associated protein) (TRAP-1)",
            "related_func_ids": "F0209; F0504",
            "category": "protein",
            "subcategories": "Chaperone",
            "Uniport_ID": "Q12931",
            "Uniprot_name": "TRAP1_HUMAN",
            "EC_numbers": "",
            "gene_symbol": "TRAP1",
            "gene_synonyms": "HSP75, HSP90L",
            "gene_synonyms_links": "",
            "gene_name": "TNF receptor associated protein 1",
            "hgnc_id": "",
            "entrez_id": "",
            "ensembl_id": "ENSG00000126602",
            "omim_id": "",
            "genecard_link": "",
            "locs": "Mitochondrion; Mitochondrion inner membrane; Mitochondrion matrix",
            "reaction": "",
            "targ_desciption": "Chaperone that expresses an ATPase activity. Involved inmaintaining mitochondrial function and polarization, downstream ofPINK1 and mitochondrial complex I. Is a negative regulator ofmitochondrial respiration able to modulate the balance betweenoxidative phosphorylation and aerobic glycolysis. The impact of TRAP1on mitochondrial respiration is probably mediated by modulation ofmitochondrial SRC and inhibition of SDHA. {ECO:0000269|PubMed:23525905,ECO:0000269|PubMed:23564345, ECO:0000269|PubMed:23747254}.",
            "references": []
        },
        {
            "targ_id": "T124",
            "parent_targ_id": "T",
            "full_name": "Bifunctional coenzyme A synthase",
            "abbrev": "CoA synthase",
            "protein_names": "Bifunctional coenzyme A synthase (CoA synthase) (NBP) (POV-2) [Includes: Phosphopantetheine adenylyltransferase (EC 2.7.7.3) (Dephospho-CoA pyrophosphorylase) (Pantetheine-phosphate adenylyltransferase) (PPAT); Dephospho-CoA kinase (DPCK) (EC 2.7.1.24) (Dephosphocoenzyme A kinase) (DPCOAK)]",
            "related_func_ids": "F021206",
            "category": "enzyme",
            "subcategories": "Kinase, Multifunctional enzyme, Nucleotidyltransferase, Transferase",
            "Uniport_ID": "Q13057",
            "Uniprot_name": "COASY_HUMAN",
            "EC_numbers": "2.7.7.3; 2.7.1.24",
            "gene_symbol": "COASY",
            "gene_synonyms": "CoASY, DPCK, NBP, PPAT",
            "gene_synonyms_links": "",
            "gene_name": "Coenzyme A synthase",
            "hgnc_id": "",
            "entrez_id": "",
            "ensembl_id": "ENSG00000068120",
            "omim_id": "",
            "genecard_link": "",
            "locs": "Cytoplasm; Mitochondrion matrix;",
            "reaction": "ATP + D-pantetheine 4'-phosphate + H(+) = 3'-dephospho-CoA +diphosphate; 3'-dephospho-CoA + ATP = ADP + CoA + H(+)",
            "targ_desciption": "Bifunctional enzyme that catalyzes the fourth and fifthsequential steps of CoA biosynthetic pathway. The fourth reaction iscatalyzed by the phosphopantetheine adenylyltransferase, coded by thecoaD domain. the fifth reaction is catalyzed by the dephospho-CoAkinase, coded by the coaE domain. May act as a point of CoAbiosynthesis regulation. {ECO:0000269|PubMed:11923312,ECO:0000269|PubMed:24360804}.",
            "references": []
        },
        {
            "targ_id": "T125",
            "parent_targ_id": "T",
            "full_name": "Pantothenate kinase 2, mitochondrial",
            "abbrev": "hPanK2",
            "protein_names": "Pantothenate kinase 2, mitochondrial (hPanK2) (EC 2.7.1.33) (Pantothenic acid kinase 2)",
            "related_func_ids": "F021206",
            "category": "enzyme",
            "subcategories": "Kinase, Transferase",
            "Uniport_ID": "Q9BZ23",
            "Uniprot_name": "PANK2_HUMAN",
            "EC_numbers": "2.7.1.33",
            "gene_symbol": "PANK2",
            "gene_synonyms": "C20orf48, FLJ11729, HARP, HSS, NBIA1, PKAN",
            "gene_synonyms_links": "",
            "gene_name": "Pantothenate kinase 2",
            "hgnc_id": "",
            "entrez_id": "",
            "ensembl_id": "ENSG00000125779",
            "omim_id": "",
            "genecard_link": "",
            "locs": "[Isoform 1]: Mitochondrion; [Isoform 2]: Cytoplasm; [Isoform 3]: Cytoplasm; [Isoform 4]: Cytoplasm",
            "reaction": "(R)-pantothenate + ATP = (R)-4'-phosphopantothenate + ADP +H(+)",
            "targ_desciption": "May be the master regulator of the CoA biosynthesis.{ECO:0000250}.",
            "references": []
        },
        {
            "targ_id": "T126",
            "parent_targ_id": "T",
            "full_name": "Mitochondrial coenzyme A transporter SLC25A42",
            "abbrev": "Solute carrier family 25 member 42",
            "protein_names": "Mitochondrial coenzyme A transporter SLC25A42 (Solute carrier family 25 member 42)",
            "related_func_ids": "F021206",
            "category": "protein",
            "subcategories": "transporter",
            "Uniport_ID": "Q86VD7",
            "Uniprot_name": "S2542_HUMAN",
            "EC_numbers": "",
            "gene_symbol": "SLC25A42",
            "gene_synonyms": "MGC26694",
            "gene_synonyms_links": "",
            "gene_name": "Solute carrier family 25 member 42",
            "hgnc_id": "",
            "entrez_id": "",
            "ensembl_id": "ENSG00000181035",
            "omim_id": "",
            "genecard_link": "",
            "locs": "Mitochondrion inner membrane; Multi-pass membrane protein",
            "reaction": "",
            "targ_desciption": "Mitochondrial carrier mediating the transport of coenzyme A(CoA) in mitochondria in exchange for intramitochondrial (deoxy)adeninenucleotides and adenosine 3',5'-diphosphate.{ECO:0000269|PubMed:19429682}.",
            "references": []
        },
        {
            "targ_id": "T127",
            "parent_targ_id": "T",
            "full_name": "4-hydroxybenzoate polyprenyltransferase, mitochondrial",
            "abbrev": "4-HB polyprenyltransferase",
            "protein_names": "4-hydroxybenzoate polyprenyltransferase, mitochondrial (4-HB polyprenyltransferase) (EC 2.5.1.39) (4-hydroxybenzoate decaprenyltransferase) (COQ2 homolog) (hCOQ2) (Para-hydroxybenzoate--polyprenyltransferase) (PHB:PPT) (PHB:polyprenyltransferase)",
            "related_func_ids": "F021207",
            "category": "enzyme",
            "subcategories": "Transferase",
            "Uniport_ID": "Q96H96",
            "Uniprot_name": "COQ2_HUMAN",
            "EC_numbers": "2.5.1.39",
            "gene_symbol": "COQ2",
            "gene_synonyms": "CL640, FLJ26072",
            "gene_synonyms_links": "",
            "gene_name": "Coenzyme Q2, polyprenyltransferase",
            "hgnc_id": "",
            "entrez_id": "",
            "ensembl_id": "ENSG00000173085",
            "omim_id": "",
            "genecard_link": "",
            "locs": "Mitochondrion inner membrane; Multi-pass membrane protein; Matrix side",
            "reaction": "4-hydroxybenzoate + an all-trans-polyprenyl diphosphate = a 4-hydroxy-3-all-trans-polyprenylbenzoate + diphosphate",
            "targ_desciption": "Catalyzes the prenylation of para-hydroxybenzoate (PHB) withan all-trans polyprenyl group. Mediates the second step in the finalreaction sequence of coenzyme Q (CoQ) biosynthesis, which is thecondensation of the polyisoprenoid side chain with PHB, generating thefirst membrane-bound Q intermediate. {ECO:0000255|HAMAP-Rule:MF_03189,ECO:0000269|PubMed:15153069, ECO:0000269|PubMed:16400613,ECO:0000269|PubMed:17374725, ECO:0000269|PubMed:27493029}.",
            "references": []
        },
        {
            "targ_id": "T128",
            "parent_targ_id": "T",
            "full_name": "Ubiquinone biosynthesis protein COQ4 homolog, mitochondrial",
            "abbrev": "Coenzyme Q biosynthesis protein 4 homolog",
            "protein_names": "Ubiquinone biosynthesis protein COQ4 homolog, mitochondrial (Coenzyme Q biosynthesis protein 4 homolog)",
            "related_func_ids": "F021207",
            "category": "protein",
            "subcategories": "",
            "Uniport_ID": "Q9Y3A0",
            "Uniprot_name": "COQ4_HUMAN",
            "EC_numbers": "",
            "gene_symbol": "COQ4",
            "gene_synonyms": "CGI-92",
            "gene_synonyms_links": "",
            "gene_name": "Coenzyme Q4",
            "hgnc_id": "",
            "entrez_id": "",
            "ensembl_id": "ENSG00000167113",
            "omim_id": "",
            "genecard_link": "",
            "locs": "[Isoform 1]: Mitochondrion inner membrane; Peripheral membrane protein; Matrix side",
            "reaction": "",
            "targ_desciption": "Component of the coenzyme Q biosynthetic pathway. May play arole in organizing a multi-subunit COQ enzyme complex required forcoenzyme Q biosynthesis. Required for steady-state levels of other COQpolypeptides. {ECO:0000255|HAMAP-Rule:MF_03111,ECO:0000269|PubMed:18474229}.",
            "references": []
        },
        {
            "targ_id": "T129",
            "parent_targ_id": "T",
            "full_name": "2-methoxy-6-polyprenyl-1,4-benzoquinol methylase, mitochondrial",
            "abbrev": "Ubiquinone biosynthesis methyltransferase COQ5",
            "protein_names": "2-methoxy-6-polyprenyl-1,4-benzoquinol methylase, mitochondrial (EC 2.1.1.201) (Ubiquinone biosynthesis methyltransferase COQ5)",
            "related_func_ids": "F021207",
            "category": "enzyme",
            "subcategories": "Methyltransferase, Transferase",
            "Uniport_ID": "Q5HYK3",
            "Uniprot_name": "COQ5_HUMAN",
            "EC_numbers": "2.1.1.201",
            "gene_symbol": "COQ5",
            "gene_synonyms": "MGC4767",
            "gene_synonyms_links": "",
            "gene_name": "Coenzyme Q5, methyltransferase",
            "hgnc_id": "",
            "entrez_id": "",
            "ensembl_id": "ENSG00000110871",
            "omim_id": "",
            "genecard_link": "",
            "locs": "Mitochondrion inner membrane; Peripheral membrane protein; Matrix side",
            "reaction": "a 2-methoxy-6-all-trans-polyprenyl-1,4-benzoquinol + S-adenosyl-L-methionine = a 6-methoxy-3-methyl-2-all-trans-polyprenyl-1,4-benzoquinol + H(+) + S-adenosyl-L-homocysteine",
            "targ_desciption": "Methyltransferase required for the conversion of 2-polyprenyl-6-methoxy-1,4-benzoquinol (DDMQH2) to 2-polyprenyl-3-methyl-6-methoxy-1,4-benzoquinol (DMQH2). {ECO:0000255|HAMAP-Rule:MF_03191}.",
            "references": []
        },
        {
            "targ_id": "T130",
            "parent_targ_id": "T",
            "full_name": "Ubiquinone biosynthesis monooxygenase COQ6, mitochondrial",
            "abbrev": "Coenzyme Q10 monooxygenase 6",
            "protein_names": "Ubiquinone biosynthesis monooxygenase COQ6, mitochondrial (EC 1.14.13.-) (Coenzyme Q10 monooxygenase 6)",
            "related_func_ids": "F021207",
            "category": "enzyme",
            "subcategories": "Monooxygenase, Oxidoreductase",
            "Uniport_ID": "Q9Y2Z9",
            "Uniprot_name": "COQ6_HUMAN",
            "EC_numbers": "1.14.13.-",
            "gene_symbol": "COQ6",
            "gene_synonyms": "CGI-10",
            "gene_synonyms_links": "",
            "gene_name": "Coenzyme Q6, monooxygenase",
            "hgnc_id": "",
            "entrez_id": "",
            "ensembl_id": "ENSG00000119723",
            "omim_id": "",
            "genecard_link": "",
            "locs": "Mitochondrion inner membrane; Peripheral membrane protein; Matrix side; Golgi apparatus; Cell projection",
            "reaction": "4-hydroxy-3-all-trans-hexaprenylbenzoate + 2 H(+) + O2 + 2reduced [2Fe-2S]-[ferredoxin] = 3,4-dihydroxy-5-all-trans-hexaprenylbenzoate + H2O + 2 oxidized [2Fe-2S]-[ferredoxin]",
            "targ_desciption": "FAD-dependent monooxygenase required for the C5-ringhydroxylation during ubiquinone biosynthesis. Catalyzes thehydroxylation of 3-hexaprenyl-4-hydroxybenzoic acid (HHB) to 3-hexaprenyl-4,5-dihydroxybenzoic acid (DHHB). The electrons required forthe hydroxylation reaction may be funneled indirectly from NADPH via aferredoxin/ferredoxin reductase system to COQ6 (By similarity). Is ableto perform the deamination reaction at C4 of 3-hexaprenyl-4-amino-5-hydroxybenzoic acid (HHAB) to produce DHHB when expressed in yeastcells lacking COQ9, even if utilization of para-aminobenzoic acid(pABA) involving C4-deamination seems not to occur in bacteria, plantsand mammals, where only C5 hydroxylation of HHB has been shown(PubMed:26260787). {ECO:0000255|HAMAP-Rule:MF_03193,ECO:0000269|PubMed:26260787}.",
            "references": []
        },
        {
            "targ_id": "T131",
            "parent_targ_id": "T",
            "full_name": "5-demethoxyubiquinone hydroxylase, mitochondrial",
            "abbrev": "DMQ hydroxylase",
            "protein_names": "5-demethoxyubiquinone hydroxylase, mitochondrial (DMQ hydroxylase) (EC 1.14.99.60) (Timing protein clk-1 homolog) (Ubiquinone biosynthesis monooxygenase COQ7)",
            "related_func_ids": "F021207",
            "category": "enzyme",
            "subcategories": "Monooxygenase, Oxidoreductase",
            "Uniport_ID": "Q99807",
            "Uniprot_name": "COQ7_HUMAN",
            "EC_numbers": "1.14.99.60",
            "gene_symbol": "COQ7",
            "gene_synonyms": "CAT5, CLK-1",
            "gene_synonyms_links": "",
            "gene_name": "Coenzyme Q7, hydroxylase",
            "hgnc_id": "",
            "entrez_id": "",
            "ensembl_id": "ENSG00000167186",
            "omim_id": "",
            "genecard_link": "",
            "locs": "Mitochondrion inner membrane; Peripheral membrane protein; Matrix side",
            "reaction": "a 6-methoxy-3-methyl-2-all-trans-polyprenyl-1,4-benzoquinol +AH2 + O2 = A + a 3-demethylubiquinol + H2O",
            "targ_desciption": "Catalyzes the hydroxylation of 2-polyprenyl-3-methyl-6-methoxy-1,4-benzoquinol (DMQH2) during ubiquinone biosynthesis. Hasalso a structural role in the COQ enzyme complex, stabilizing other COQpolypeptides. Involved in lifespan determination in a ubiquinone-independent manner. {ECO:0000255|HAMAP-Rule:MF_03194}.",
            "references": []
        },
        {
            "targ_id": "T132",
            "parent_targ_id": "T",
            "full_name": "Atypical kinase COQ8A, mitochondrial",
            "abbrev": "Coenzyme Q protein 8A",
            "protein_names": "Atypical kinase COQ8A, mitochondrial (EC 2.7.-.-) (Chaperone activity of bc1 complex-like) (Chaperone-ABC1-like) (Coenzyme Q protein 8A) (aarF domain-containing protein kinase 3)",
            "related_func_ids": "F021207",
            "category": "enzyme",
            "subcategories": "Kinase, Transferase",
            "Uniport_ID": "Q8NI60",
            "Uniprot_name": "COQ8A_HUMAN",
            "EC_numbers": "2.7.-.-",
            "gene_symbol": "COQ8A",
            "gene_synonyms": "ADCK3, CABC1, COQ8, SCAR9",
            "gene_synonyms_links": "",
            "gene_name": "Coenzyme Q8A",
            "hgnc_id": "",
            "entrez_id": "",
            "ensembl_id": "ENSG00000163050",
            "omim_id": "",
            "genecard_link": "",
            "locs": "Mitochondrion; Membrane; Single-pass membrane protein",
            "reaction": "",
            "targ_desciption": "Atypical kinase involved in the biosynthesis of coenzyme Q,also named ubiquinone, an essential lipid-soluble electron transporterfor aerobic cellular respiration (PubMed:25498144, PubMed:21296186,PubMed:25540914, PubMed:27499294). Its substrate specificity isunclear: does not show any protein kinase activity (PubMed:25498144,PubMed:27499294). Probably acts as a small molecule kinase, possibly alipid kinase that phosphorylates a prenyl lipid in the ubiquinonebiosynthesis pathway, as suggested by its ability to bind coenzyme Qlipid intermediates (PubMed:25498144, PubMed:27499294). Shows anunusual selectivity for binding ADP over ATP (PubMed:25498144).{ECO:0000269|PubMed:25498144, ECO:0000269|PubMed:27499294,ECO:0000305|PubMed:21296186, ECO:0000305|PubMed:25540914}.",
            "references": []
        },
        {
            "targ_id": "T133",
            "parent_targ_id": "T",
            "full_name": "Atypical kinase COQ8B, mitochondrial",
            "abbrev": "Coenzyme Q protein 8B",
            "protein_names": "Atypical kinase COQ8B, mitochondrial (EC 2.7.-.-) (AarF domain-containing protein kinase 4) (Coenzyme Q protein 8B)",
            "related_func_ids": "F021207",
            "category": "enzyme",
            "subcategories": "Kinase, Transferase",
            "Uniport_ID": "Q96D53",
            "Uniprot_name": "COQ8B_HUMAN",
            "EC_numbers": "2.7.-.-",
            "gene_symbol": "COQ8B",
            "gene_synonyms": "ADCK4, COQ8, FLJ12229",
            "gene_synonyms_links": "",
            "gene_name": "Coenzyme Q8B",
            "hgnc_id": "",
            "entrez_id": "",
            "ensembl_id": "ENSG00000123815",
            "omim_id": "",
            "genecard_link": "",
            "locs": "Mitochondrion membrane; Single-pass membrane protein; Cytoplasm, cytosol; Cell membrane",
            "reaction": "",
            "targ_desciption": "Atypical kinase involved in the biosynthesis of coenzyme Q,also named ubiquinone, an essential lipid-soluble electron transporterfor aerobic cellular respiration (PubMed:24270420). Its substratespecificity is unclear: does not show any protein kinase activity.Probably acts as a small molecule kinase, possibly a lipid kinase thatphosphorylates a prenyl lipid in the ubiquinone biosynthesis pathway.Required for podocyte migration (PubMed:24270420).{ECO:0000250|UniProtKB:Q8NI60, ECO:0000269|PubMed:24270420}.",
            "references": []
        }
    ]
}