ID A0A124BWY0_ASPNG Unreviewed; 506 AA.
AC A0A124BWY0;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE SubName: Full=O-methylsterigmatocystin oxidoreductase {ECO:0000313|EMBL:GAQ40668.1};
GN ORFNames=ABL_03745 {ECO:0000313|EMBL:GAQ40668.1};
OS Aspergillus niger.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=5061 {ECO:0000313|EMBL:GAQ40668.1, ECO:0000313|Proteomes:UP000068243};
RN [1] {ECO:0000313|Proteomes:UP000068243}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=An76 {ECO:0000313|Proteomes:UP000068243};
RX PubMed=26893421; DOI=10.1128/genomeA.01700-15;
RA Gong W., Cheng Z., Zhang H., Liu L., Gao P., Wang L.;
RT "Draft genome sequence of Aspergillus niger strain An76.";
RL Genome Announc. 4:E0170015-E0170015(2016).
CC -!- COFACTOR:
CC Name=heme; Xref=ChEBI:CHEBI:30413;
CC Evidence={ECO:0000256|ARBA:ARBA00001971};
CC -!- SIMILARITY: Belongs to the cytochrome P450 family.
CC {ECO:0000256|ARBA:ARBA00010617, ECO:0000256|RuleBase:RU000461}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:GAQ40668.1}.
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DR EMBL; BCMY01000005; GAQ40668.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A124BWY0; -.
DR VEuPathDB; FungiDB:An15g03990; -.
DR VEuPathDB; FungiDB:ASPNIDRAFT2_1183607; -.
DR VEuPathDB; FungiDB:ATCC64974_29750; -.
DR VEuPathDB; FungiDB:M747DRAFT_269170; -.
DR OMA; TPEWQHW; -.
DR Proteomes; UP000068243; Unassembled WGS sequence.
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 CDD; cd11065; CYP64-like; 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; PTHR46300:SF7; P450, PUTATIVE (EUROFUNG)-RELATED; 1.
DR PANTHER; PTHR46300; P450, PUTATIVE (EUROFUNG)-RELATED-RELATED; 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 3: Inferred from homology;
KW Heme {ECO:0000256|RuleBase:RU000461}; Iron {ECO:0000256|RuleBase:RU000461};
KW Metal-binding {ECO:0000256|RuleBase:RU000461};
KW Monooxygenase {ECO:0000256|RuleBase:RU000461};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU000461}.
SQ SEQUENCE 506 AA; 56874 MW; 4543FB7282C05B6F CRC64;
MSIVIAVAFA CLFLIPLYLF IYQQSPSLPL PPGPKGKPIV GNLSDLPPPD TPEWQHWMKH
KERYGPITSV TILGQPIIIL HGAHITTELL EKRSLKYSSR PRSVFLGEMI GWNDTLAMQP
YNTRFRLYRK ALHQILGTKN LVSKFNSLQE LEARRLLLRM IDDPRDWVQH LKTEAGAIIL
KIGYGYDINP HGRDHLVDLA DDSMETFSAV LNQTWLVDLI PALKYLPSWL PFSFQKKAQS
WQTQLLTTIE TPYRMVKEQM VSGTAPPSYL RNLLQEEDTK KEKSLAAEEE FTAKWTAGSL
YLAGADTTVS TLTTFILSMA LNPHIQDQAQ AELDTILGPY TLPSLSDREK LPYINAIVKE
SLRWYPVAPM GLPHLCVEGD VYDGYTIPKG AMVMGNIWAI THDPNIYPHP EKFDPERFLG
ENPQPDPSGW VFGFGRRVCP GRVLADASVF VTVGMILSAL RISLEGGMGE VRFTPGVVSH
PVLDGVRVQA RSQRHEEVIR EVSVGV
//
