ID   CP19A_COTJA             Reviewed;         327 AA.
AC   P79699; Q92150;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   15-DEC-1998, sequence version 2.
DT   03-AUG-2022, entry version 105.
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;
DE   Flags: Fragments;
GN   Name=CYP19A1; Synonyms=CYP19;
OS   Coturnix japonica (Japanese quail) (Coturnix coturnix japonica).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC   Perdicinae; Coturnix.
OX   NCBI_TaxID=93934;
RN   [1]
RP   NUCLEOTIDE SEQUENCE OF 1-97.
RA   Kudo T., Yamamoto H., Sato S., Sutou S.;
RT   "Comparison of 5' upstream regions of chicken and quail aromatase genes.";
RL   J. Reprod. Dev. 42:101-107(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 98-327.
RC   TISSUE=Brain;
RX   PubMed=1331667; DOI=10.1016/0169-328x(92)90146-3;
RA   Harada N., Yamada K., Foidart A., Balthazart J.;
RT   "Regulation of aromatase cytochrome P-450 (estrogen synthetase) transcripts
RT   in the quail brain by testosterone.";
RL   Brain Res. Mol. Brain Res. 15:19-26(1992).
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; D50336; BAA08872.1; -; Genomic_DNA.
DR   EMBL; S46949; AAB23955.1; -; mRNA.
DR   PIR; A48977; A48977.
DR   AlphaFoldDB; P79699; -.
DR   SMR; P79699; -.
DR   Proteomes; UP000694412; 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; IPR002397; Cyt_P450_B.
DR   InterPro; IPR017972; Cyt_P450_CS.
DR   InterPro; IPR036396; Cyt_P450_sf.
DR   Pfam; PF00067; p450; 1.
DR   PRINTS; PR00359; BP450.
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..>327
FT                   /note="Aromatase"
FT                   /id="PRO_0000051965"
FT   BINDING         315
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"
FT   NON_CONS        97..98
FT                   /evidence="ECO:0000305"
FT   NON_TER         327
SQ   SEQUENCE   327 AA;  37445 MW;  CF568A94BA23127B CRC64;
     MIPETLNPLN YYTSLVPDLI PAATVPIIIL ICVLFLIWNH EGTSSIPGPG YCMGIGPLIS
     HGRFLWMGVG NACNYYNKTY GEFVRVWFSG EETFIISYFD AWQALLLKPD IFFKISWLCK
     KYEEAAKDLK GAMEILIEQK RQKLSTVEKL DEHMDFASQL IFAQNRGDLT AENVNQCVLE
     MMIAAPDTLS VTLFIMLILI AEHPTVEEKM MREIETVMGD RDVQSDDMPN LKIVENFIYE
     SMRYQPVVDL IMRKALQDDV IDGYPVKKGT NIILNIGRMH KLEFFPKPNE FSLENFEKNV
     PSRYFQPFGF GPRGCVGKFI AMVMMKA