ID   CP19A_ICTPU             Reviewed;         524 AA.
AC   Q92111;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 101.
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   Ictalurus punctatus (Channel catfish) (Silurus punctatus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Siluriformes;
OC   Ictaluridae; Ictalurus.
OX   NCBI_TaxID=7998;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Ovary;
RX   PubMed=7958747; DOI=10.1006/gcen.1994.1113;
RA   Trant J.M.;
RT   "Isolation and characterization of the cDNA encoding the channel catfish
RT   (Ictalurus punctatus) form of cytochrome P450arom.";
RL   Gen. Comp. Endocrinol. 95:155-168(1994).
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}.
CC   -!- CAUTION: It is uncertain whether Met-1, Met-8 or Met-23 is the
CC       initiator. {ECO:0000305}.
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DR   EMBL; S75715; AAB32613.1; -; mRNA.
DR   PIR; I51268; I51268.
DR   RefSeq; NP_001316189.1; NM_001329260.1.
DR   AlphaFoldDB; Q92111; -.
DR   SMR; Q92111; -.
DR   STRING; 7998.ENSIPUP00000026178; -.
DR   GeneID; 108264511; -.
DR   KEGG; ipu:108264511; -.
DR   Proteomes; UP000221080; Genome assembly.
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.
FT   CHAIN           1..524
FT                   /note="Aromatase"
FT                   /id="PRO_0000051970"
FT   BINDING         457
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   524 AA;  60346 MW;  EB3DE1458F81F5C0 CRC64;
     MAAHVFPMCE RTRKPVHFSE TVMEILLREA RNGTDPRYEN PRGITLLLLL CLVLLLTVWN
     RHEKKCSIPG PSFCLGLGPL MSYCRFIWMG IGTASNYYNE KYGDMVRVWI SGEETLVLSR
     PSAVYHVLKH SQYTSRFGSK LGLQCIGMHE QGIIFNSNVT LWRKVRTYFA KALTGPGLQR
     TLEICTMSTN THLDGLSRLT DAQGHVDVLN LLRCIVVDIS NRLFLDVPLN EQNLLFKIHR
     YFETWQTVLI KPDFYFRLKW LHDKHRNAAQ ELHDAIEDLI EQKRTELQQA EKLDNLNFTE
     ELIFAQSHGE LTAENVRQCV LEMVIAAPDT LSISVFFMLL LLKQNAEVER RILTEIHTVL
     GDTELQHSHL SQLHVLECFI NEALRFHPVV DFSYRRALDD DVIEGFRVPR GTNIILNVGR
     MHRSEFYPKP ADFSLDNFNK PVPSRFFQPF GSGPRSCVGK HIAMVMMKAV LLMVLSRFSV
     CPEESCTVEN IAHTNDLSQQ PVEDKHTLSV RFIPRNTHTR NRKA