ID   CP2K3_ONCMY             Reviewed;         491 AA.
AC   O93299;
DT   15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1998, sequence version 1.
DT   03-AUG-2022, entry version 89.
DE   RecName: Full=Cytochrome P450 2K3;
DE            EC=1.14.14.1;
DE   AltName: Full=CYPIIK3;
DE   AltName: Full=Cytochrome P450 LMC2;
GN   Name=cyp2k3;
OS   Oncorhynchus mykiss (Rainbow trout) (Salmo gairdneri).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Protacanthopterygii; Salmoniformes;
OC   Salmonidae; Salmoninae; Oncorhynchus.
OX   NCBI_TaxID=8022;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Liver;
RA   Yang Y.-H., Miranda C.L., Wang J.-L., Buhler D.R.;
RT   "Cloning, sequencing and heterologous expression of CYP2K1 and CYP2K3 from
RT   sexually mature rainbow trout liver and their roles in aflatoxin B1
RT   activation.";
RL   Submitted (JAN-1998) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=an organic molecule + O2 + reduced [NADPH--hemoprotein
CC         reductase] = an alcohol + H(+) + H2O + oxidized [NADPH--hemoprotein
CC         reductase]; 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   -!- COFACTOR:
CC       Name=heme; Xref=ChEBI:CHEBI:30413; Evidence={ECO:0000250};
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250};
CC       Peripheral membrane protein {ECO:0000250}. Microsome membrane
CC       {ECO:0000250}; Peripheral membrane protein {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
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DR   EMBL; AF043551; AAC26494.1; -; mRNA.
DR   AlphaFoldDB; O93299; -.
DR   SMR; O93299; -.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0070330; F:aromatase activity; IEA:UniProtKB-EC.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR   Gene3D; 1.10.630.10; -; 1.
DR   InterPro; IPR001128; Cyt_P450.
DR   InterPro; IPR017972; Cyt_P450_CS.
DR   InterPro; IPR002401; Cyt_P450_E_grp-I.
DR   InterPro; IPR036396; Cyt_P450_sf.
DR   Pfam; PF00067; p450; 1.
DR   PRINTS; PR00463; EP450I.
DR   PRINTS; PR00385; P450.
DR   SUPFAM; SSF48264; SSF48264; 1.
DR   PROSITE; PS00086; CYTOCHROME_P450; 1.
PE   2: Evidence at transcript level;
KW   Endoplasmic reticulum; Heme; Iron; Membrane; Metal-binding; Microsome;
KW   Monooxygenase; Oxidoreductase.
FT   CHAIN           1..491
FT                   /note="Cytochrome P450 2K3"
FT                   /id="PRO_0000051774"
FT   BINDING         434
FT                   /ligand="heme"
FT                   /ligand_id="ChEBI:CHEBI:30413"
FT                   /ligand_part="Fe"
FT                   /ligand_part_id="ChEBI:CHEBI:18248"
FT                   /note="axial binding residue"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   491 AA;  55288 MW;  2194A1054FFE928E CRC64;
     MSLIEGLLQT SSTVTLLGTV LFLLVLYLRS SGSSSEGQGK EPPGPRPLPL LGNMLQLDLK
     KPYCTLCELS KKYGSIFTFH FGPKKVVVLA GYKTVKQALV NQAEDFGDRD ITPVFYDFNQ
     GHGILFANGD SWKEMRRFAL TNLRDFGMGK KGSEEKILEE IPYLIEVFEK HEGKAFDTTQ
     SVLYAVSNII SAIVYGSRFE YTDPLFTGMA DRAKESIHLT GSASIQMYNM FPWLGPWINN
     LTRLKKNIAD MKMEVTELVR GLKETLNPHM CRGFVDSFLV RKQTLEESGH MDSFYHDDNL
     VFSVGNLFSA GTDTTGTTLR WGLLLMTKYP HIQDQVQEEI SGVIGSRQTL VEDRKNLPYT
     DAVIHETQRL ANIAPMSIPH TTSRDVTFQG YFIKKDDSEW ESPHTLTPSH FLDEKGGFVK
     RDAFMAFSAG RRVCLGEGLA RMELFLFFTS LLQHFRFSPP PGVTEDDLDL TPSVEFTHNP
     SPHQLCAVSR V