BUT79_GIBZE
ID BUT79_GIBZE Reviewed; 509 AA.
AC I1RV19;
DT 12-AUG-2020, integrated into UniProtKB/Swiss-Prot.
DT 13-JUN-2012, sequence version 1.
DT 03-AUG-2022, entry version 54.
DE RecName: Full=Cytochrome P450 monooxygenase FG08079 {ECO:0000305};
DE EC=1.-.-.- {ECO:0000305};
DE AltName: Full=Butenolide biosynthesis cluster protein FG08079 {ECO:0000303|PubMed:17175185};
GN ORFNames=FG08079, FGRAMPH1_01T09067;
OS Gibberella zeae (strain ATCC MYA-4620 / CBS 123657 / FGSC 9075 / NRRL 31084
OS / PH-1) (Wheat head blight fungus) (Fusarium graminearum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium.
OX NCBI_TaxID=229533;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4620 / CBS 123657 / FGSC 9075 / NRRL 31084 / PH-1;
RX PubMed=17823352; DOI=10.1126/science.1143708;
RA Cuomo C.A., Gueldener U., Xu J.-R., Trail F., Turgeon B.G., Di Pietro A.,
RA Walton J.D., Ma L.-J., Baker S.E., Rep M., Adam G., Antoniw J., Baldwin T.,
RA Calvo S.E., Chang Y.-L., DeCaprio D., Gale L.R., Gnerre S., Goswami R.S.,
RA Hammond-Kosack K., Harris L.J., Hilburn K., Kennell J.C., Kroken S.,
RA Magnuson J.K., Mannhaupt G., Mauceli E.W., Mewes H.-W., Mitterbauer R.,
RA Muehlbauer G., Muensterkoetter M., Nelson D., O'Donnell K., Ouellet T.,
RA Qi W., Quesneville H., Roncero M.I.G., Seong K.-Y., Tetko I.V., Urban M.,
RA Waalwijk C., Ward T.J., Yao J., Birren B.W., Kistler H.C.;
RT "The Fusarium graminearum genome reveals a link between localized
RT polymorphism and pathogen specialization.";
RL Science 317:1400-1402(2007).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=ATCC MYA-4620 / CBS 123657 / FGSC 9075 / NRRL 31084 / PH-1;
RX PubMed=20237561; DOI=10.1038/nature08850;
RA Ma L.-J., van der Does H.C., Borkovich K.A., Coleman J.J., Daboussi M.-J.,
RA Di Pietro A., Dufresne M., Freitag M., Grabherr M., Henrissat B.,
RA Houterman P.M., Kang S., Shim W.-B., Woloshuk C., Xie X., Xu J.-R.,
RA Antoniw J., Baker S.E., Bluhm B.H., Breakspear A., Brown D.W.,
RA Butchko R.A.E., Chapman S., Coulson R., Coutinho P.M., Danchin E.G.J.,
RA Diener A., Gale L.R., Gardiner D.M., Goff S., Hammond-Kosack K.E.,
RA Hilburn K., Hua-Van A., Jonkers W., Kazan K., Kodira C.D., Koehrsen M.,
RA Kumar L., Lee Y.-H., Li L., Manners J.M., Miranda-Saavedra D.,
RA Mukherjee M., Park G., Park J., Park S.-Y., Proctor R.H., Regev A.,
RA Ruiz-Roldan M.C., Sain D., Sakthikumar S., Sykes S., Schwartz D.C.,
RA Turgeon B.G., Wapinski I., Yoder O., Young S., Zeng Q., Zhou S.,
RA Galagan J., Cuomo C.A., Kistler H.C., Rep M.;
RT "Comparative genomics reveals mobile pathogenicity chromosomes in
RT Fusarium.";
RL Nature 464:367-373(2010).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4620 / CBS 123657 / FGSC 9075 / NRRL 31084 / PH-1;
RX PubMed=26198851; DOI=10.1186/s12864-015-1756-1;
RA King R., Urban M., Hammond-Kosack M.C.U., Hassani-Pak K.,
RA Hammond-Kosack K.E.;
RT "The completed genome sequence of the pathogenic ascomycete fungus Fusarium
RT graminearum.";
RL BMC Genomics 16:544-544(2015).
RN [4]
RP FUNCTION, INDUCTION, DISRUPTION PHENOTYPE, AND PATHWAY.
RX PubMed=17175185; DOI=10.1016/j.fgb.2006.11.001;
RA Harris L.J., Alexander N.J., Saparno A., Blackwell B., McCormick S.P.,
RA Desjardins A.E., Robert L.S., Tinker N., Hattori J., Piche C.,
RA Schernthaner J.P., Watson R., Ouellet T.;
RT "A novel gene cluster in Fusarium graminearum contains a gene that
RT contributes to butenolide synthesis.";
RL Fungal Genet. Biol. 44:293-306(2007).
CC -!- FUNCTION: Cytochrome P450 monooxygenase FG08079; part of the gene
CC cluster that mediates the biosynthesis of butenolide, a mycotoxin that
CC shows antibiotic activity but does not seem to play a major role in the
CC spread of head blight in wheat (PubMed:17175185). Butenolide is derived
CC from glutamic acid via a 4-acetamido-2-butenoic acid intermediate
CC (Probable). The predicted function of the NADH:flavin oxidoreductase
CC FG08077, the cytochrome P450 monooxygenase FG08079, the decarboxylase
CC FG08083, and the putative acetyltransferase FG08082 are consistent with
CC this pathway, however, the respective activities of the butelonide
CC biosynthesis cluster enzymes have still to be experimentally determined
CC (Probable). {ECO:0000269|PubMed:17175185, ECO:0000305|PubMed:17175185}.
CC -!- COFACTOR:
CC Name=heme; Xref=ChEBI:CHEBI:30413;
CC Evidence={ECO:0000250|UniProtKB:P04798};
CC -!- PATHWAY: Mycotoxin biosynthesis. {ECO:0000269|PubMed:17175185}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Single-pass membrane
CC protein {ECO:0000255}.
CC -!- INDUCTION: Highly expressed under trichothecene-producing conditions.
CC {ECO:0000269|PubMed:17175185}.
CC -!- DISRUPTION PHENOTYPE: Results in the loss of butelonide production.
CC {ECO:0000269|PubMed:17175185}.
CC -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
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DR EMBL; HG970333; CEF76336.1; -; Genomic_DNA.
DR RefSeq; XP_011320743.1; XM_011322441.1.
DR AlphaFoldDB; I1RV19; -.
DR SMR; I1RV19; -.
DR STRING; 229533.I1RV19; -.
DR GeneID; 23555113; -.
DR KEGG; fgr:FGSG_08079; -.
DR VEuPathDB; FungiDB:FGRAMPH1_01G09067; -.
DR eggNOG; KOG0158; Eukaryota.
DR HOGENOM; CLU_001570_14_0_1; -.
DR InParanoid; I1RV19; -.
DR Proteomes; UP000070720; Chromosome 2.
DR GO; GO:0016021; C:integral component of 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 Gene3D; 1.10.630.10; -; 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 Pfam; PF00067; p450; 1.
DR PRINTS; PR00463; EP450I.
DR PRINTS; PR00385; P450.
DR SUPFAM; SSF48264; SSF48264; 1.
DR PROSITE; PS00086; CYTOCHROME_P450; 1.
PE 2: Evidence at transcript level;
KW Heme; Iron; Membrane; Metal-binding; Monooxygenase; Oxidoreductase;
KW Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..509
FT /note="Cytochrome P450 monooxygenase FG08079"
FT /id="PRO_0000450724"
FT TRANSMEM 6..26
FT /note="Helical"
FT /evidence="ECO:0000255"
FT BINDING 458
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000250|UniProtKB:P04798"
SQ SEQUENCE 509 AA; 57604 MW; 439F9D9CA2B6D43E CRC64;
MAMFTVLPLI WLAPLGLISL FFYYIIPYFW NYRHLRSIPG PLFARLSNWW LVYACREKSR
WKYVNDAHTR YGPVVRIQPN HVSIANEEVI NAIYGHGNGM LKSSFYDASV ITTYSIFTSR
DRAEHSRKRK VVSHSFAPQS MRNFEPFIQQ HLNVFLQKWD AMAANEAKFD GYADVESRVW
LNYLVLDIIG DLAFGAPFGV LAKGSEVVDF ETEKGPSSLP VITSLSTRSE IAATVGALPE
LKPYLKWSPD PFFRTGFNGM INLRTLGTSR ITDRLNNPPG DEREKDLLER VREGRDHKGQ
PFGKGELIAE ALTVLIAGTD TTSSTMAALL YHVVRTPGVL KKLQAELDEA IPADVSIPSF
EMVKNLKYLG FVVNEALRHH STISLGLPRL VPENGNGVTI AGYHFAPGTV LSIPIYTVHH
LKEVWGPDAD EFKPERWEDV TQRQKQAFIP FSHGPRACLG RNLAEMELKV ITATWARRYD
LIMRDDTMEI LEGLARKPEA VNVGIRRRM
