| IED ID | IndEnz0010001117 |
| Enzyme Type ID | esterase001117 |
| Protein Name |
Cytochrome P450 2A13 EC 1.14.14.1 CYPIIA13 |
| Gene Name | CYP2A13 |
| Organism | Homo sapiens (Human) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Metazoa Eumetazoa Bilateria Deuterostomia Chordata Craniata Vertebrata Gnathostomata (jawed vertebrates) Teleostomi Euteleostomi Sarcopterygii Dipnotetrapodomorpha Tetrapoda Amniota Mammalia Theria Eutheria Boreoeutheria Euarchontoglires Primates Haplorrhini Simiiformes Catarrhini Hominoidea (apes) Hominidae (great apes) Homininae Homo Homo sapiens (Human) |
| Enzyme Sequence | MLASGLLLVTLLACLTVMVLMSVWRQRKSRGKLPPGPTPLPFIGNYLQLNTEQMYNSLMKISERYGPVFTIHLGPRRVVVLCGHDAVKEALVDQAEEFSGRGEQATFDWLFKGYGVAFSNGERAKQLRRFSIATLRGFGVGKRGIEERIQEEAGFLIDALRGTHGANIDPTFFLSRTVSNVISSIVFGDRFDYEDKEFLSLLRMMLGSFQFTATSTGQLYEMFSSVMKHLPGPQQQAFKELQGLEDFIAKKVEHNQRTLDPNSPRDFIDSFLIRMQEEEKNPNTEFYLKNLVMTTLNLFFAGTETVSTTLRYGFLLLMKHPEVEAKVHEEIDRVIGKNRQPKFEDRAKMPYTEAVIHEIQRFGDMLPMGLAHRVNKDTKFRDFFLPKGTEVFPMLGSVLRDPRFFSNPRDFNPQHFLDKKGQFKKSDAFVPFSIGKRYCFGEGLARMELFLFFTTIMQNFRFKSPQSPKDIDVSPKHVGFATIPRNYTMSFLPR |
| Enzyme Length | 494 |
| Uniprot Accession Number | Q16696 |
| Absorption | |
| Active Site | |
| Activity Regulation | |
| Binding Site | BINDING 297; /note=Substrate |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=an organic molecule + O2 + reduced [NADPH--hemoprotein reductase] = an alcohol + H(+) + H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:17149, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:30879, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, ChEBI:CHEBI:142491; EC=1.14.14.1; |
| DNA Binding | |
| EC Number | 1.14.14.1 |
| Enzyme Function | FUNCTION: Exhibits a coumarin 7-hydroxylase activity. Active in the metabolic activation of hexamethylphosphoramide, N,N-dimethylaniline, 2'-methoxyacetophenone, N-nitrosomethylphenylamine, and the tobacco-specific carcinogen, 4-(methylnitrosamino)-1-(3-pyridyl)-1-butanone. Possesses phenacetin O-deethylation activity. {ECO:0000269|PubMed:18779312}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Beta strand (11); Binding site (1); Chain (1); Helix (20); Metal binding (1); Mutagenesis (10); Natural variant (8); Sequence conflict (5); Turn (7) |
| Keywords | 3D-structure;Endoplasmic reticulum;Heme;Iron;Membrane;Metal-binding;Microsome;Monooxygenase;Oxidoreductase;Reference proteome |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Peripheral membrane protein. Microsome membrane; Peripheral membrane protein. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | X-ray crystallography (8) |
| Cross Reference PDB | 2P85; 2PG5; 2PG6; 2PG7; 3T3S; 4EJG; 4EJH; 4EJI; |
| Mapped Pubmed ID | 10383923; 10731522; 10741631; 11701230; 12629583; 12920161; 14633739; 15115698; 15196988; 15222883; 15333516; 15665333; 16316926; 16385575; 1664256; 16835796; 18669584; 19290787; 19303722; 19343046; 19414505; 19789190; 19812523; 2025243; 20431511; 20534012; 20568895; 20798279; 20846153; 21473878; 22051186; 22397853; 22696418; 22700965; 22798551; 22890016; 23463547; 23583631; 23602888; 23752126; 23907605; 23917075; 24114584; 24907355; 25667220; 25710941; 27567546; 27725446; 28648140; 29652224; 30807688; 33327254; 33703988; 34830188; 497175; 8627510; 8631948; 8637342; 8647857; 8913342; 8975785; 9028626; 9103523; 9842986; 9884161; |
| Motif | |
| Gene Encoded By | |
| Mass | 56,688 |
| Kinetics | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=10.7 uM for phenacetin {ECO:0000269|PubMed:18779312}; |
| Metal Binding | METAL 439; /note=Iron (heme axial ligand) |
| Rhea ID | RHEA:17149 |
| Cross Reference Brenda |