ID Q3LS70_MICUN Unreviewed; 518 AA.
AC Q3LS70;
DT 25-OCT-2005, integrated into UniProtKB/TrEMBL.
DT 25-OCT-2005, sequence version 1.
DT 27-MAR-2024, entry version 60.
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};
GN Name=cyp19a1 {ECO:0000313|EMBL:ABA26927.1};
OS Micropogonias undulatus (Atlantic croaker).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Eupercaria; Sciaenidae; Micropogonias.
OX NCBI_TaxID=29154 {ECO:0000313|EMBL:ABA26927.1};
RN [1] {ECO:0000313|EMBL:ABA26927.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=16872606; DOI=10.1016/j.ygcen.2006.06.005;
RA Nunez B.S., Applebaum S.L.;
RT "Tissue- and sex-specific regulation of CYP19A1 expression in the Atlantic
RT croaker (Micropogonias undulatus).";
RL Gen. Comp. Endocrinol. 149:205-216(2006).
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 EMBL; DQ184486; ABA26927.1; -; mRNA.
DR AlphaFoldDB; Q3LS70; -.
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 2: Evidence at transcript level;
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}.
FT COILED 254..281
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 518 AA; 58631 MW; 34DF4304758D173E CRC64;
MDLISACEGA MDPVRLDAMV AELVSMPPNA TAVGSPGISM ATRTLILLTC LLLVAWSHTD
KKTVPGPSFC LGLGPLLSYL RFIWTGIGTA SNYYNNKYGD IVRVWINGEE TLILSRASAV
HHVLKNSHYT SRFGSKEGLS CIGMNESGII FNNNVTLWKK MRTYFTKALT GPGLQQTTEV
CVSSTQTHLD DLDSLDHVDV LSLLRCTVVD ISNRLFLGVP VNEKELLLKI QKYFDTWQTV
LIKPDIYFKC AWIHQRHKTA AQELQDAIKS LVEQKRRDME QADKLDNINF TAELIFARHH
GELSAENVRQ SVLEMVIAAP DTLSISLFFM LLLLKQHPDV ELQLLEEIDT VVGERQLQNG
DLQKLQVLES FINECLRFHP VVDFTMRRAL SDDIIGGYRV PKGTNIILNT GQMHRTEFFL
KPNEFSLENF QRNAPRRYFQ PFGSGPRSCV GKHMAMVMMK SILVTLLSQY SVCPHKGLTL
DCLPQINNLS QQPVEHQQEA EHLSMRFLPR QRGNWQTL
//
