BUT77_GIBZE
ID BUT77_GIBZE Reviewed; 413 AA.
AC I1RV17; A0A098DBL4;
DT 12-AUG-2020, integrated into UniProtKB/Swiss-Prot.
DT 13-JUN-2012, sequence version 1.
DT 03-AUG-2022, entry version 51.
DE RecName: Full=NADH:flavin oxidoreductase FG08077 {ECO:0000303|PubMed:17175185};
DE EC=1.6.-.- {ECO:0000305|PubMed:17175185};
DE AltName: Full=Butenolide biosynthesis cluster protein FG08077 {ECO:0000303|PubMed:17175185};
GN ORFNames=FG08077, FGRAMPH1_01T09063;
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, 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: NADH:flavin oxidoreductase; part of the gene cluster that
CC mediates the biosynthesis of butenolide, a mycotoxin that shows
CC 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=FMN; Xref=ChEBI:CHEBI:58210;
CC Evidence={ECO:0000250|UniProtKB:P54550};
CC -!- PATHWAY: Mycotoxin biosynthesis. {ECO:0000305|PubMed:17175185}.
CC -!- INDUCTION: Highly expressed under trichothecene-producing conditions.
CC {ECO:0000269|PubMed:17175185}.
CC -!- SIMILARITY: Belongs to the NADH:flavin oxidoreductase/NADH oxidase
CC family. NamA subfamily. {ECO:0000305}.
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DR EMBL; HG970333; CEF76334.1; -; Genomic_DNA.
DR RefSeq; XP_011320745.1; XM_011322443.1.
DR AlphaFoldDB; I1RV17; -.
DR SMR; I1RV17; -.
DR GeneID; 23555111; -.
DR KEGG; fgr:FGSG_08077; -.
DR VEuPathDB; FungiDB:FGRAMPH1_01G09063; -.
DR eggNOG; KOG0134; Eukaryota.
DR HOGENOM; CLU_012153_2_1_1; -.
DR InParanoid; I1RV17; -.
DR Proteomes; UP000070720; Chromosome 2.
DR GO; GO:0010181; F:FMN binding; IEA:InterPro.
DR GO; GO:0050661; F:NADP binding; IEA:InterPro.
DR GO; GO:0003959; F:NADPH dehydrogenase activity; IEA:InterPro.
DR CDD; cd02932; OYE_YqiM_FMN; 1.
DR Gene3D; 3.20.20.70; -; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR001155; OxRdtase_FMN_N.
DR InterPro; IPR044152; YqjM-like.
DR PANTHER; PTHR43303; PTHR43303; 1.
DR Pfam; PF00724; Oxidored_FMN; 1.
PE 2: Evidence at transcript level;
KW Flavoprotein; FMN; NADP; Oxidoreductase; Reference proteome.
FT CHAIN 1..413
FT /note="NADH:flavin oxidoreductase FG08077"
FT /id="PRO_0000450722"
FT BINDING 53..56
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250|UniProtKB:P54550"
FT BINDING 58
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P54550"
FT BINDING 88
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250|UniProtKB:P54550"
FT BINDING 130
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250|UniProtKB:P54550"
FT BINDING 211..214
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P54550"
FT BINDING 264
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250|UniProtKB:P54550"
FT BINDING 370..371
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250|UniProtKB:P54550"
SQ SEQUENCE 413 AA; 44812 MW; 96CAAA7D7D1B0761 CRC64;
MAYEIIDNIA AEGAPYYTPA QDPPAGTQTS GSTKVFTPIT IRGVTFPNRL FLAPLCQYSA
KDGYATDWHL THLGGIIQRG PGLSMVEATA VQNHGRITPQ DVGLWEDGQI EPLKRITTFA
HSQSQKIGIQ LSHAGRKASC VSPWLSINAV AAKEVGGWPD NIVAPSAIAQ EAGVNPVPKA
FTKEDIEELK NDFLAAAKRA IRAGFDVIEI HAAHGYLLHQ FLSPVSNQRT DEYGGSFENR
IRVVLEIIDL IRGEIPETTP ILVRVSATDW FEYDAQFKDE FPESWTVEQT CKLAQILPKH
GVDLVDVSSG GIHPKSAIAI KAGPAYQVDL AKQVKKAVGD SVLVSAVGGI KTGHLAEEVL
QSGIDVVRAG RWFQQNPGLV RAFANELGVE VKMANQIDWS FKGRGKNGHK KSP
