ID A0A135S3I4_9PEZI Unreviewed; 535 AA.
AC A0A135S3I4;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE SubName: Full=O-methylsterigmatocystin oxidoreductase {ECO:0000313|EMBL:KXH30439.1};
GN ORFNames=CNYM01_00607 {ECO:0000313|EMBL:KXH30439.1};
OS Colletotrichum nymphaeae SA-01.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum;
OC Colletotrichum acutatum species complex.
OX NCBI_TaxID=1460502 {ECO:0000313|EMBL:KXH30439.1, ECO:0000313|Proteomes:UP000070054};
RN [1] {ECO:0000313|EMBL:KXH30439.1, ECO:0000313|Proteomes:UP000070054}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SA-01 {ECO:0000313|EMBL:KXH30439.1,
RC ECO:0000313|Proteomes:UP000070054};
RA Baroncelli R., Thon M.R.;
RT "The genome sequence of Colletotrichum nymphaeae SA-01.";
RL Submitted (FEB-2014) to the EMBL/GenBank/DDBJ databases.
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:KXH30439.1}.
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DR EMBL; JEMN01001663; KXH30439.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A135S3I4; -.
DR Proteomes; UP000070054; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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 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 Membrane {ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|RuleBase:RU000461};
KW Monooxygenase {ECO:0000256|RuleBase:RU000461};
KW Oxidoreductase {ECO:0000256|RuleBase:RU000461};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 6..22
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 64..81
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
SQ SEQUENCE 535 AA; 61088 MW; 3F3C008543954553 CRC64;
MTYTLWLFWS ILALASFVIY SRRRTSDQRK LPPGPKPLPL LGNIRDFPPE GTPEHLHWLK
HKDLYGPISS VTVMGMTLII VHDRNMAHEL LDQTASKTSG RPSMVMANKL CGYESIVLCQ
GYTPMFRRYR KFLHQELGTK VSASQFRDVQ ECEVGRQLVR SLERPESLLE HYKTTAAATV
LQMAYGYTIE PHKSDALIEL IEKMMTEFSL AASPMAWLVD IIPVLQHLPE SFPGASFKKT
AREWRKSIQA SAYIPYEFVQ QQLSCFSNRP SYVSKLSQQL AQDEKGELSK EDEKAVIWSA
ASLYGAAADT TVITLSTFAL AMLEFPDVQR KAQAEIDRVI GSGRLPTFED RDKLPYVDAL
VKETARWWPI VPMSFPHTTT EEFEYEGYRI PQDAFILPAV WWFLHDPDVY IKPESFDPDR
FLPPRNEADP TTEVFGYGRR ICPGRFFADS SLFINMAQTL AAFTIAKALD KNGKEIEVDV
RPKPGILTYP TAFQVRVIPR SKEHAELVRQ VGRKYPYEAS DAALLQHPDS FQIRY
//
