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 27-MAR-2024, entry version 104. 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 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 -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; U72071; AAB16814.1; -; mRNA. DR RefSeq; NP_001266515.1; NM_001279586.1. DR AlphaFoldDB; P70091; -. DR SMR; P70091; -. DR STRING; 8128.ENSONIP00000077498; -. DR GeneID; 100708217; -. DR KEGG; onl:100708217; -. DR eggNOG; KOG0157; Eukaryota. DR InParanoid; P70091; -. DR OrthoDB; 5385594at2759; -. 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: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; 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 //