ID   CP19A_ORENI             Reviewed;         522 AA.
AC   P70091;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1997, sequence version 1.
DT   03-AUG-2022, entry version 99.
DE   RecName: Full=Aromatase;
DE            EC=1.14.14.14 {ECO:0000250|UniProtKB:P11511};
DE   AltName: Full=CYPXIX;
DE   AltName: Full=Cytochrome P-450AROM;
DE   AltName: Full=Cytochrome P450 19A1;
DE   AltName: Full=Estrogen synthase;
GN   Name=cyp19a1; Synonyms=cyp19;
OS   Oreochromis niloticus (Nile tilapia) (Tilapia nilotica).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Ovalentaria; Cichlomorphae; Cichliformes; Cichlidae; African cichlids;
OC   Pseudocrenilabrinae; Oreochromini; Oreochromis.
OX   NCBI_TaxID=8128;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Ovary;
RX   PubMed=9061607; DOI=10.1677/jme.0.0180057;
RA   Chang X.T., Kobayashi T., Kajiura H., Nakamura M., Nagahama Y.;
RT   "Isolation and characterization of the cDNA encoding the tilapia
RT   (Oreochromis niloticus) cytochrome P450 aromatase (P450arom): changes in
RT   P450arom mRNA, protein and enzyme activity in ovarian follicles during
RT   oogenesis.";
RL   J. Mol. Endocrinol. 18:57-66(1997).
CC   -!- FUNCTION: Catalyzes the formation of aromatic C18 estrogens from C19
CC       androgens.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=3 O2 + 3 reduced [NADPH--hemoprotein reductase] + testosterone
CC         = 17beta-estradiol + formate + 4 H(+) + 4 H2O + 3 oxidized [NADPH--
CC         hemoprotein reductase]; Xref=Rhea:RHEA:38191, Rhea:RHEA-COMP:11964,
CC         Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:15379, ChEBI:CHEBI:15740, ChEBI:CHEBI:16469,
CC         ChEBI:CHEBI:17347, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210;
CC         EC=1.14.14.14; Evidence={ECO:0000250|UniProtKB:P11511};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=androst-4-ene-3,17-dione + 3 O2 + 3 reduced [NADPH--
CC         hemoprotein reductase] = estrone + formate + 4 H(+) + 4 H2O + 3
CC         oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:38195,
CC         Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:15740,
CC         ChEBI:CHEBI:16422, ChEBI:CHEBI:17263, ChEBI:CHEBI:57618,
CC         ChEBI:CHEBI:58210; EC=1.14.14.14;
CC         Evidence={ECO:0000250|UniProtKB:P11511};
CC   -!- COFACTOR:
CC       Name=heme; Xref=ChEBI:CHEBI:30413; Evidence={ECO:0000250};
CC   -!- SUBCELLULAR LOCATION: Membrane; Peripheral membrane protein.
CC   -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
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DR   EMBL; U72071; AAB16814.1; -; mRNA.
DR   RefSeq; NP_001266515.1; NM_001279586.1.
DR   AlphaFoldDB; P70091; -.
DR   SMR; P70091; -.
DR   STRING; 8128.ENSONIP00000000199; -.
DR   GeneID; 100708217; -.
DR   KEGG; onl:100708217; -.
DR   eggNOG; KOG0157; Eukaryota.
DR   InParanoid; P70091; -.
DR   OrthoDB; 1247045at2759; -.
DR   Proteomes; UP000005207; Unplaced.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR   GO; GO:0004497; F:monooxygenase activity; IEA:UniProtKB-KW.
DR   GO; GO:0016705; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen; IEA:InterPro.
DR   GO; GO:0006629; P:lipid metabolic process; IEA:UniProtKB-KW.
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   Heme; Iron; Lipid metabolism; Membrane; Metal-binding; Monooxygenase;
KW   Oxidoreductase; Reference proteome.
FT   CHAIN           1..522
FT                   /note="Aromatase"
FT                   /id="PRO_0000051971"
FT   BINDING         447
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   522 AA;  59428 MW;  EA62E690CF8C06F6 CRC64;
     MDLISACEQA MNPVGLDAVV ARSLCDLKCH PIDGISMATR TLILLVCLLL VAWSHTDKKI
     VPGPSFCLGL GPLLSYLRFI WTGIGTASNY YNNKYGDIVR VWINGEETLI LSRSSAVHHV
     LKNGNYTSRF GSIQGLSYLG MNERGIIFNN NVTLWKKIRT YFAKALTGPN LQQTVDVCVS
     SIQAHLDHLD SLGHVDVLNL LRCTVLDISN RLFLNVPLNE KELMLKIQKY FHTWQDVLIK
     PDIYFKFRWI HHRHKTATQE LQDAIKRLVD QKRKNMEQAD KLDNINFTAE LIFAQNHGEL
     SAENVTQCVL EMVIAAPDTL SLSLFFMLLL LKQNPHVEPQ LLQEIDAVVG ERQLQNQDLH
     KLQVMESFIY ECLSFHPVVD FTMRRALSDD IIEGYRISKG TNIILNTGRM HRTEFFLKGN
     QFNLEHFENN VPRPPTFQPF GSGPRACIGK HMAMVMMKSI LVTLLSQYSV CTHEGPILDC
     LPQTNNLSQQ PVEHQQAETE HLHMRFLPRQ GSSCQTLKDP NL