ID   CP2A7_PAPSP             Reviewed;          20 AA.
AC   P80055;
DT   01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1994, sequence version 2.
DT   02-SEP-2026, entry version 85.
DE   RecName: Full=Cytochrome P450 2A7 {ECO:0000250|UniProtKB:P20853};
DE            EC=1.14.14.1 {ECO:0000269|PubMed:1541278};
DE   AltName: Full=CYPIIA7;
DE   AltName: Full=Coumarin 7-hydroxylase;
DE   AltName: Full=Cytochrome P450 FI;
DE   Flags: Fragment;
GN   Name=CYP2A7 {ECO:0000250|UniProtKB:P20853};
OS   Papio sp. (Baboon).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Cercopithecinae; Papio.
OX   NCBI_TaxID=61183;
RN   [1]
RP   PROTEIN SEQUENCE, FUNCTION, AND CATALYTIC ACTIVITY.
RC   TISSUE=Liver;
RX   PubMed=1541278; DOI=10.1111/j.1432-1033.1992.tb16677.x;
RA   Dalet-Beluche I., Boulenc X., Fabre G., Maurel P., Bonfils C.;
RT   "Purification of two cytochrome P450 isozymes related to CYP2A and CYP3A
RT   gene families from monkey (baboon, Papio papio) liver microsomes. Cross
RT   reactivity with human forms.";
RL   Eur. J. Biochem. 204:641-648(1992).
CC   -!- FUNCTION: Exhibits a high coumarin 7-hydroxylase activity.
CC       {ECO:0000269|PubMed:1541278}.
CC   -!- FUNCTION: Xenobiotic-metabolizing enzyme that can catalyze the
CC       hydroxylation of species-specific aromatic amine substrates
CC       (PubMed:1541278). Catalyzes the hydroxylation of coumarin in vitro
CC       (PubMed:1541278). {ECO:0000269|PubMed:1541278}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=an organic molecule + reduced [NADPH--hemoprotein reductase] +
CC         O2 = an alcohol + oxidized [NADPH--hemoprotein reductase] + H2O +
CC         H(+); Xref=Rhea:RHEA:17149, Rhea:RHEA-COMP:11964, Rhea:RHEA-
CC         COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC         ChEBI:CHEBI:30879, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210,
CC         ChEBI:CHEBI:142491; EC=1.14.14.1;
CC         Evidence={ECO:0000269|PubMed:1541278};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:17150;
CC         Evidence={ECO:0000269|PubMed:1541278};
CC   -!- COFACTOR:
CC       Name=heme; Xref=ChEBI:CHEBI:30413; Evidence={ECO:0000250};
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Peripheral
CC       membrane protein. Microsome membrane; Peripheral membrane protein.
CC   -!- INDUCTION: By phenobarbital.
CC   -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
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DR   PIR; S21737; S21737.
DR   AlphaFoldDB; P80055; -.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016712; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, reduced flavin or flavoprotein as one donor, and incorporation of one atom of oxygen; IEA:UniProtKB-EC.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Endoplasmic reticulum; Heme; Iron; Membrane;
KW   Metal-binding; Microsome; Monooxygenase; Oxidoreductase.
FT   CHAIN           1..>20
FT                   /note="Cytochrome P450 2A7"
FT                   /id="PRO_0000051670"
FT   UNSURE          14
FT   NON_TER         20
SQ   SEQUENCE   20 AA;  2045 MW;  693102A1F0B50C96 CRC64;
     MLASGLLLVA LLACLTVMVL
//