ID Q8NJH0_FUSLU Unreviewed; 492 AA.
AC Q8NJH0;
DT 01-OCT-2002, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2002, sequence version 1.
DT 27-MAR-2024, entry version 68.
DE SubName: Full=Trichothecene C-15 hydroxylase {ECO:0000313|EMBL:AAM48761.1};
GN Name=TRI11 {ECO:0000313|EMBL:AAM48761.1};
OS Fusarium lunulosporum.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium.
OX NCBI_TaxID=56643 {ECO:0000313|EMBL:AAM48761.1};
RN [1] {ECO:0000313|EMBL:AAM48761.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=NRRL 13393 {ECO:0000313|EMBL:AAM48761.1};
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; AY102568; AAM48761.1; -; Genomic_DNA.
DR AlphaFoldDB; Q8NJH0; -.
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 6..30
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
SQ SEQUENCE 492 AA; 55747 MW; 42F86A4DB9CFF042 CRC64;
MFQYSLWPLL ALSGGTAVTY 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 SMGFNELASN ASVLIVAGSE
TTATLLSAAV YFLCSNPRTL ELLTEEVRST YTQADAIDLV STQGLRYMQA VLDEALRMYP
PVAGGGSPRK IAKGGSFVAG YFVPENTLVE NDMWAMHYDP KYFTQPHDFI PERWLGDARF
NSDRLDAVKP FSIGPRNCIG MNLAYAEMRM MLARTVWEFD IRLAESSRDW YQDSRVYLAW
NKPPLNVYLD PR
//
