ID   ORDA_ASPFA              Reviewed;         528 AA.
AC   A0A0D9MRV9; P79084; Q5J3B9; Q5VD88; Q5VDD6;
DT   11-MAY-2016, integrated into UniProtKB/Swiss-Prot.
DT   27-MAY-2015, sequence version 1.
DT   03-AUG-2022, entry version 27.
DE   RecName: Full=O-methylsterigmatocystin oxidoreductase;
DE            Short=OMST oxidoreductase;
DE            EC=1.14.14.117 {ECO:0000250|UniProtKB:B8NHY4};
DE   AltName: Full=Aflatoxin B synthase;
DE   AltName: Full=Aflatoxin biosynthesis protein Q;
DE   AltName: Full=Cytochrome P450 64;
GN   Name=ordA; Synonyms=aflQ, cyp64, ord1; ORFNames=P034_01064866;
OS   Aspergillus flavus (strain ATCC MYA-384 / AF70).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Circumdati.
OX   NCBI_TaxID=1392242;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC MYA-384 / AF70;
RX   PubMed=15528514; DOI=10.1128/aem.70.11.6518-6524.2004;
RA   Ehrlich K.C., Chang P.K., Yu J., Cotty P.J.;
RT   "Aflatoxin biosynthesis cluster gene cypA is required for G aflatoxin
RT   formation.";
RL   Appl. Environ. Microbiol. 70:6518-6524(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC MYA-384 / AF70;
RA   Yu J., Fedorova N., Yin Y., Losada L., Zafar N., Taujale R., Ehrlich K.C.,
RA   Bhatnagar D., Cleveland T.E., Bennett J.W., Nierman W.C.;
RT   "Draft genome sequence of Aspergillus flavus AF70.";
RL   Submitted (FEB-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Converts O-methylsterigmatocystin (OMST) to aflatoxin B1 and
CC       converts dihydro-O-methylsterigmatocystin (DHOMST) to aflatoxin B2 in
CC       the aflatoxin biosynthesis pathway. {ECO:0000250|UniProtKB:B8NHY4}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=8-O-methylsterigmatocystin + 2 O2 + 2 reduced [NADPH--
CC         hemoprotein reductase] = aflatoxin B1 + CO2 + 2 H(+) + H2O + methanol
CC         + 2 oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:35759,
CC         Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:2504,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC         ChEBI:CHEBI:16526, ChEBI:CHEBI:17790, ChEBI:CHEBI:18171,
CC         ChEBI:CHEBI:57618, ChEBI:CHEBI:58210; EC=1.14.14.117;
CC         Evidence={ECO:0000250|UniProtKB:B8NHY4};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=8-O-methyldihydrosterigmatocystin + 2 O2 + 2 reduced [NADPH--
CC         hemoprotein reductase] = aflatoxin B2 + CO2 + 2 H(+) + H2O + methanol
CC         + 2 oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:35763,
CC         Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:16526,
CC         ChEBI:CHEBI:17790, ChEBI:CHEBI:48209, ChEBI:CHEBI:57618,
CC         ChEBI:CHEBI:58210, ChEBI:CHEBI:72678; EC=1.14.14.117;
CC         Evidence={ECO:0000250|UniProtKB:B8NHY4};
CC   -!- COFACTOR:
CC       Name=heme; Xref=ChEBI:CHEBI:30413; Evidence={ECO:0000250};
CC   -!- PATHWAY: Mycotoxin biosynthesis; aflatoxin biosynthesis.
CC       {ECO:0000250|UniProtKB:B8NHY4}.
CC   -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
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DR   EMBL; AY510453; AAS90035.1; -; Genomic_DNA.
DR   EMBL; JZDT01000749; KJJ30544.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0D9MRV9; -.
DR   SMR; A0A0D9MRV9; -.
DR   UniPathway; UPA00287; -.
DR   Proteomes; UP000032444; Unassembled WGS sequence.
DR   GO; GO:0140399; F:aflatoxin B synthase activity; IEA:UniProtKB-EC.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0005506; F:iron ion binding; IEA:InterPro.
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   SUPFAM; SSF48264; SSF48264; 1.
DR   PROSITE; PS00086; CYTOCHROME_P450; 1.
PE   3: Inferred from homology;
KW   Heme; Iron; Metal-binding; Monooxygenase; Oxidoreductase.
FT   CHAIN           1..528
FT                   /note="O-methylsterigmatocystin oxidoreductase"
FT                   /id="PRO_0000436151"
FT   BINDING         440
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   528 AA;  60223 MW;  1F459C4AEC48B768 CRC64;
     MIYSIIICAG ALLGLWILEK LLAPKDTRPP LPPGPWRKPI IGNLSDFPPK GTPEWLFWAK
     HQERYGPMSS LEVMGQTIIM INDAQLGIEI MHKKSALSQM IPDAPFAHMA GWGMSLATER
     NRQAWKTIRA NMKQEIGTRR AISTFHPKME IGIRRFLLRT LDNPDDLRFH IRKEANAFMM
     DVAYGYTIAP HGKDELYDLT QQSVRQFSHI FSPGEWSVNF FPILRYVPSW FPGASFQIKA
     AEYKRTIERM TMVPYLWIKD QVARGCSRPS ILLRLLQKGH YESGSHQEQV LVWTNAEFVM
     GGSDTTVSAV SSFFVAMALY PEVQRKAREE LDRVVGPTTL ATFEHRLQLP FIDALVKEVF
     RWHPASPLGA PHITQEDQIW DGYLLPKGAL LLPNIWTFTH DPSVYHDPMV FKPERFLEGK
     DSPPETDPMK FVFGFGRRIC PGRFVTDEKL FLIACHAVSC FFISPKDPGA PEPDWLPGVI
     SQPGAFDLNV VPRSPAHEEL IRSIETDHPW KNADATDISR FMARNQMI