ID   A0A0P7BFP2_9HYPO        Unreviewed;       528 AA.
AC   A0A0P7BFP2;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   27-MAR-2024, entry version 20.
DE   SubName: Full=O-methylsterigmatocystin oxidoreductase {ECO:0000313|EMBL:KPM41882.1};
GN   ORFNames=AK830_g4664 {ECO:0000313|EMBL:KPM41882.1};
OS   Neonectria ditissima.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Nectriaceae; Neonectria.
OX   NCBI_TaxID=78410 {ECO:0000313|EMBL:KPM41882.1, ECO:0000313|Proteomes:UP000050424};
RN   [1] {ECO:0000313|EMBL:KPM41882.1, ECO:0000313|Proteomes:UP000050424}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=R09/05 {ECO:0000313|EMBL:KPM41882.1,
RC   ECO:0000313|Proteomes:UP000050424};
RA   Gomez-Cortecero A., Harrison R.J., Armitage A.D.;
RT   "Draft genome of a European isolate of the apple canker pathogen Neonectria
RT   ditissima.";
RL   Submitted (SEP-2015) 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:KPM41882.1}.
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DR   EMBL; LKCW01000057; KPM41882.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0P7BFP2; -.
DR   STRING; 78410.A0A0P7BFP2; -.
DR   OrthoDB; 2900138at2759; -.
DR   Proteomes; UP000050424; 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|RuleBase:RU000461};
KW   Reference proteome {ECO:0000313|Proteomes:UP000050424}.
SQ   SEQUENCE   528 AA;  59437 MW;  2246535A3F4ED1D4 CRC64;
     MLQAIFALTG IVLYLLYLRK KAHPTLPPGP KPLPIIGNIT DLPSGRTPEY QHWLKFKDAY
     GPISRVSILG QPLVIIHDRH AAHDLLVGTS SKTSGRPYLH FAAKLCGYGT LLSFQQYDAE
     FRQQRKLVHQ QLGTKTAVAR FRDVQDVESR RFLFRVLEDP KNLVDHIKTE ASAIILRITY
     GYSIEPRKAD PLARLIERMM QGASLAFVPL SWPVDILPIL EYFPECLPGM SFKKIAREWN
     GITRKVIETP YNFVRQQMAK GTHRLSYVSS LIEQHDDSSE KGRLNEGSEN AIKNTAAIMY
     AGGSDTTVSS INSLILAMVL FPAVQKKAQQ EIDTVVGTNR LPQFGDRDSL PYVNALVKET
     IRWFPVAPMG AVHQADEDVD YGGFHISKGT QILPAIWWFL HDPQTYPDPS SFNPDRFLEP
     RNEPDPANEA FGYGRRICPG RFLADESLFI TISRLLAAFD IRKAIDKQGN EIDPQIEVTP
     GLISHLLDFP HSIKPRNANY ASLIRSIEVE HPWEKSDAGM LEGDFATV
//