ID   CP19A_ANGJA             Reviewed;         511 AA.
AC   Q6QHT9;
DT   24-MAY-2005, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   27-MAR-2024, entry version 74.
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   Anguilla japonica (Japanese eel).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Anguilliformes; Anguillidae;
OC   Anguilla.
OX   NCBI_TaxID=7937;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND TISSUE SPECIFICITY.
RC   TISSUE=Ovary;
RX   PubMed=12568797; DOI=10.1016/s0016-6480(02)00589-0;
RA   Ijiri S., Kazeto Y., Lokman P.M., Adachi S., Yamauchi K.;
RT   "Characterization of a cDNA encoding P-450 aromatase (CYP19) from Japanese
RT   eel ovary and its expression in ovarian follicles during induced ovarian
RT   development.";
RL   Gen. Comp. Endocrinol. 130:193-203(2003).
CC   -!- FUNCTION: Catalyzes the formation of aromatic C18 estrogens from C19
CC       androgens. {ECO:0000269|PubMed:12568797}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=3 O2 + 3 reduced [NADPH--hemoprotein reductase] + testosterone
CC         = 17beta-estradiol + formate + 4 H(+) + 4 H2O + 3 oxidized
CC         [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:38191, Rhea:RHEA-
CC         COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:15740,
CC         ChEBI:CHEBI:16469, ChEBI:CHEBI:17347, ChEBI:CHEBI:57618,
CC         ChEBI:CHEBI:58210; EC=1.14.14.14;
CC         Evidence={ECO:0000250|UniProtKB:P11511};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=androst-4-ene-3,17-dione + 3 O2 + 3 reduced
CC         [NADPH--hemoprotein reductase] = estrone + formate + 4 H(+) + 4 H2O +
CC         3 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   -!- TISSUE SPECIFICITY: Expressed in ovary. It is also found in the brain,
CC       but not in the spleen, head kidney, kidney or liver.
CC       {ECO:0000269|PubMed:12568797}.
CC   -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
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DR   EMBL; AY540622; AAS47028.1; -; mRNA.
DR   AlphaFoldDB; Q6QHT9; -.
DR   SMR; Q6QHT9; -.
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:0048856; P:anatomical structure development; IEA:UniProt.
DR   GO; GO:0006629; P:lipid metabolic process; IEA:UniProtKB-KW.
DR   CDD; cd20616; CYP19A1; 1.
DR   Gene3D; 1.10.630.10; Cytochrome P450; 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   PANTHER; PTHR24291:SF43; AROMATASE; 1.
DR   PANTHER; PTHR24291; CYTOCHROME P450 FAMILY 4; 1.
DR   Pfam; PF00067; p450; 1.
DR   PRINTS; PR00463; EP450I.
DR   PRINTS; PR00385; P450.
DR   SUPFAM; SSF48264; Cytochrome P450; 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..511
FT                   /note="Aromatase"
FT                   /id="PRO_0000051966"
SQ   SEQUENCE   511 AA;  58308 MW;  EAB2203A8A48D8C5 CRC64;
     MKHLEEIVME ALMPASRNAT QTAGRVVSGA TAALLSGATA ALLLLLCALL AAWSRSDKSS
     VPGPPFYMGI GPLLSYFRFI WTGIGTASNY YNERYGDIVR VWINGEETII LSRSSAVYQV
     LRKPQYTSRF GSKQGLRCIG MHERGIIFNN NIELWKKVRT YFAKALTGPG LQRTVAICVA
     STDSHLDQLE ELTDLSGQVD ILNLLRCTIV DISNQMFLRV PLNEKELLVK IQKYFEAWQT
     VLIRPDFLFK FEWMYKEHKE AAHELHEAME ILVEKKRKAL EEAEKLDDAD FATDLIFAQN
     HGELSAENVQ QCILEMIIAA PDTMSISLFF MLMLLKQNPE VEQEILKELD TVIGDKKAEN
     SNLQHLIIME SFINESLRYH PVVDFTMRKS LEDDVIEGYK VFKGTNIILN VGRMHKCEFF
     SKPNEFSLEN FEKTVPNRFF QPFGSGPRSC VGKHISMVMM KAILATLLSR YTMCPRDGRT
     LNNIRKTNNL SQQLAEKDSE LTMMFTPRRR Q
//