ID   ORDA_ASPFL              Reviewed;         528 AA.
AC   P0CT93; P79084; Q5J3B9; Q5VD88; Q5VDD6;
DT   11-MAY-2016, integrated into UniProtKB/Swiss-Prot.
DT   11-MAY-2016, sequence version 1.
DT   03-AUG-2022, entry version 23.
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;
OS   Aspergillus flavus.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Circumdati.
OX   NCBI_TaxID=5059;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 96044 / AF13 / SRRC 1273;
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 [GENOMIC DNA].
RC   STRAIN=ATCC 96045 / AF36;
RX   PubMed=16108793; DOI=10.1111/j.1365-2672.2005.02637.x;
RA   Ehrlich K.C., Yu J., Cotty P.J.;
RT   "Aflatoxin biosynthesis gene clusters and flanking regions.";
RL   J. Appl. Microbiol. 99:518-527(2005).
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}.
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   -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
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DR   EMBL; AY510451; AAS90105.1; -; Genomic_DNA.
DR   EMBL; AY510455; AAS90081.1; -; Genomic_DNA.
DR   AlphaFoldDB; P0CT93; -.
DR   SMR; P0CT93; -.
DR   EnsemblFungi; EED51155; EED51155; AFLA_139200.
DR   VEuPathDB; FungiDB:AFLA_139200; -.
DR   VEuPathDB; FungiDB:F9C07_7796; -.
DR   OMA; IMINDAQ; -.
DR   UniPathway; UPA00287; -.
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_0000052052"
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"
FT   VARIANT         423
FT                   /note="P -> L (in strain: ATCC 96044 / SRRC 1273 / AF13)"
FT   VARIANT         517
FT                   /note="D -> H (in strain: ATCC 96044 / SRRC 1273 / AF13)"
SQ   SEQUENCE   528 AA;  60211 MW;  56DEA320008BD5EE CRC64;
     MIYSIIICAG ALLGLWILEK LLAPKDTRPP LPPGPWRKPI IGNLTDFPPK 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 ATFEHRSQLP FIDALVKEVF
     RWHPASPLGA PHITQEDQIW DGYLLPKGAL LLPNIWTFTH DPSVYHDPMV FKPERFLEGK
     DSPPETDPMK FVFGFGRRIC PGRFVTDEKL FLIACHAVSC FFISPKDPGA PEPDWLPGVI
     SQPGAFDLNV VPRSPAHEEL IRSIETDHPW KNADATDISR FMARNQMI