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Database: UniProt
Entry: Q8NJG7_FUSCE
LinkDB: Q8NJG7_FUSCE
Original site: Q8NJG7_FUSCE 
ID   Q8NJG7_FUSCE            Unreviewed;       492 AA.
AC   Q8NJG7;
DT   01-OCT-2002, integrated into UniProtKB/TrEMBL.
DT   01-OCT-2002, sequence version 1.
DT   27-MAR-2024, entry version 70.
DE   SubName: Full=Trichothecene C-15 hydroxylase {ECO:0000313|EMBL:AAM48769.1};
GN   Name=TRI11 {ECO:0000313|EMBL:AAM48769.1};
OS   Fusarium cerealis (Fusarium crookwellense).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium.
OX   NCBI_TaxID=56641 {ECO:0000313|EMBL:AAM48769.1};
RN   [1] {ECO:0000313|EMBL:AAM48769.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=NRRL 13721 {ECO:0000313|EMBL:AAM48769.1};
RX   PubMed=12080147; DOI=10.1073/pnas.142307199;
RA   Ward T.J., Bielawski J.P., Kistler H.C., Sullivan E., O'Donnell K.;
RT   "Ancestral polymorphism and adaptive evolution in the trichothecene
RT   mycotoxin gene cluster of phytopathogenic Fusarium.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:9278-9283(2002).
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}.
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DR   EMBL; AY102569; AAM48769.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q8NJG7; -.
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; cd11058; CYP60B-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; PTHR24305; CYTOCHROME P450; 1.
DR   PANTHER; PTHR24305:SF230; CYTOCHROME P450 MONOOXYGENASE STHF; 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|ARBA:ARBA00022617, ECO:0000256|RuleBase:RU000461};
KW   Iron {ECO:0000256|RuleBase:RU000461}; 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        7..30
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
SQ   SEQUENCE   492 AA;  55683 MW;  5D9CFECD8DA59C26 CRC64;
     MFQYSPWPLL ALSGGTAVAY FVIMLVYNLF FHPLRNYPGP WLNTMTQIPH TLLMLCGLPH
     KRHLALHMKY GPVVRIGPNM LSFNHPDAMK DVRGHRKSGE AEHGKDPIIV LSNGDNIVGS
     DRENHTRFRR ALAYGFSAQA MLEQEPTFKA YVNQLFQRLH EQSSNGTKTV DISKWYTFTT
     FDMIGDLAFG ESFGCLDNST YHPWVALAFE SLKSLAFMAE MGRYPRIAPY IGFLLPRGLL
     NKFAENKELA SMKVRKRLDT ETDRPDFVGK ITQGLKAKGS SMEFNELASN ASVLIVAGSE
     TTATLLSAAV YFLCSNPRTL ELLAEEVRST YTQADAIDLV STQGLRYMQA VLDEALRMYP
     PVAGGGSPRK IAKGGSFVAG YFVPENTLVE NDMWAMHYDP KYFTQPHDFI PERWLGDARF
     SSDRLDAVKP FSIGPRNCIG VNLAYAEMRM MLARTVWEFD IRLAESSRNW YQDSRVYLAW
     NKPPLNVYLD PR
//
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