ID   ORDA_ASPFN              Reviewed;         528 AA.
AC   B8NHY4; P79084; Q5J3B9;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   03-MAR-2009, sequence version 1.
DT   03-AUG-2022, entry version 64.
DE   RecName: Full=O-methylsterigmatocystin oxidoreductase;
DE            Short=OMST oxidoreductase;
DE            EC=1.14.14.117;
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=AFLA_139200;
OS   Aspergillus flavus (strain ATCC 200026 / FGSC A1120 / IAM 13836 / NRRL 3357
OS   / JCM 12722 / SRRC 167).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Circumdati.
OX   NCBI_TaxID=332952;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], AND FUNCTION.
RX   PubMed=9143099; DOI=10.1128/aem.63.5.1661-1666.1997;
RA   Prieto R., Woloshuk C.P.;
RT   "ord1, an oxidoreductase gene responsible for conversion of O-
RT   methylsterigmatocystin to aflatoxin in Aspergillus flavus.";
RL   Appl. Environ. Microbiol. 63:1661-1666(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 200026 / FGSC A1120 / IAM 13836 / NRRL 3357 / JCM 12722 / SRRC
RC   167;
RX   PubMed=25883274; DOI=10.1128/genomea.00168-15;
RA   Nierman W.C., Yu J., Fedorova-Abrams N.D., Losada L., Cleveland T.E.,
RA   Bhatnagar D., Bennett J.W., Dean R., Payne G.A.;
RT   "Genome sequence of Aspergillus flavus NRRL 3357, a strain that causes
RT   aflatoxin contamination of food and feed.";
RL   Genome Announc. 3:E0016815-E0016815(2015).
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:0000269|PubMed:9143099}.
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   -!- 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   -!- 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; U81806; AAC49709.1; -; Genomic_DNA.
DR   EMBL; U81807; AAC49710.1; -; mRNA.
DR   EMBL; EQ963478; EED51155.1; -; Genomic_DNA.
DR   RefSeq; XP_002379931.1; XM_002379890.1.
DR   AlphaFoldDB; B8NHY4; -.
DR   SMR; B8NHY4; -.
DR   STRING; 5059.CADAFLAP00007796; -.
DR   PRIDE; B8NHY4; -.
DR   EnsemblFungi; EED51155; EED51155; AFLA_139200.
DR   VEuPathDB; FungiDB:AFLA_139200; -.
DR   eggNOG; KOG0156; Eukaryota.
DR   HOGENOM; CLU_001570_2_3_1; -.
DR   OMA; IMINDAQ; -.
DR   UniPathway; UPA00287; -.
DR   Proteomes; UP000001875; 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   2: Evidence at transcript level;
KW   Heme; Iron; Metal-binding; Monooxygenase; Oxidoreductase.
FT   CHAIN           1..528
FT                   /note="O-methylsterigmatocystin oxidoreductase"
FT                   /id="PRO_0000370239"
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;  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