ID A0A3P9PVD1_POERE Unreviewed; 518 AA.
AC A0A3P9PVD1;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE RecName: Full=aromatase {ECO:0000256|ARBA:ARBA00038885};
DE EC=1.14.14.14 {ECO:0000256|ARBA:ARBA00038885};
DE AltName: Full=Cytochrome P-450AROM {ECO:0000256|ARBA:ARBA00043174};
DE AltName: Full=Estrogen synthase {ECO:0000256|ARBA:ARBA00042499};
OS Poecilia reticulata (Guppy) (Acanthophacelus reticulatus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Atherinomorphae; Cyprinodontiformes; Poeciliidae; Poeciliinae;
OC Poecilia.
OX NCBI_TaxID=8081 {ECO:0000313|Ensembl:ENSPREP00000025867.1, ECO:0000313|Proteomes:UP000242638};
RN [1] {ECO:0000313|Proteomes:UP000242638}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Guanapo {ECO:0000313|Proteomes:UP000242638};
RA Kuenstner A., Dreyer C.;
RT "The genomic landscape of the Guanapo guppy.";
RL Submitted (NOV-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSPREP00000025867.1}
RP IDENTIFICATION.
RC STRAIN=Guanapo {ECO:0000313|Ensembl:ENSPREP00000025867.1};
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- FUNCTION: Catalyzes the formation of aromatic C18 estrogens from C19
CC androgens. {ECO:0000256|ARBA:ARBA00037202}.
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:0000256|ARBA:ARBA00036685};
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:0000256|ARBA:ARBA00036398};
CC -!- COFACTOR:
CC Name=heme; Xref=ChEBI:CHEBI:30413;
CC Evidence={ECO:0000256|ARBA:ARBA00001971};
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004170};
CC Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004170}.
CC -!- SIMILARITY: Belongs to the cytochrome P450 family.
CC {ECO:0000256|ARBA:ARBA00010617, ECO:0000256|RuleBase:RU000461}.
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DR AlphaFoldDB; A0A3P9PVD1; -.
DR Ensembl; ENSPRET00000026125.1; ENSPREP00000025867.1; ENSPREG00000012213.1.
DR GeneTree; ENSGT00840000129915; -.
DR Proteomes; UP000242638; Unassembled WGS sequence.
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 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 3: Inferred from homology;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Heme {ECO:0000256|ARBA:ARBA00022617, ECO:0000256|RuleBase:RU000461};
KW Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|RuleBase:RU000461};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|RuleBase:RU000461};
KW Monooxygenase {ECO:0000256|RuleBase:RU000461};
KW Oxidoreductase {ECO:0000256|RuleBase:RU000461};
KW Reference proteome {ECO:0000313|Proteomes:UP000242638}.
FT COILED 255..289
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 518 AA; 58656 MW; F19848935E70D536 CRC64;
LMDSIPSCGG TMSTVDMDGA VTDLVSISLN ATTHLSPDIP IATRTLILLV CLLVVAWSQT
EKNTVPGPSF CLGFGPHLSY LRFIWTGIGT ASNYYNKKYG DIVRVWINGE ETLVLCRASA
VNHVLKNGKY TSRFGSKPGL SCLGMNERGI IFNNNVALWK KIRTYFAKAL TGPNLQQTVE
VCVSSTQTHL DNLDSLAHVD VLSLLRCTVV DISNRLFLDV PLDEKELLLK IHRYFETWQT
VLIKPDIYFK FGWIHQRHKT AAQELQDAIE SLVEQKRREM EQADKLDINF TADLIFAQNH
GELSAENVRQ CVLEMVIAAP DTLSISLFFM LLLLKQAPHV ELQLLQEIDT VIGELCKHDV
FARQLQVLES FINECLRFHP VVDFTMRRAL SDDVIDGYRV PKGTNIILNT GRMHRTEFFH
KADEFSLENF QKNTPRRYFQ PFGSGPRACV GKHIAMVMMK SILATLLSQY SVCPHEGLTL
DCLPQTNNLS QQPVEHQEEA EQLSMRFLPR QRGSWQTP
//
