BUT83_GIBZE
ID BUT83_GIBZE Reviewed; 520 AA.
AC I1RV23;
DT 12-AUG-2020, integrated into UniProtKB/Swiss-Prot.
DT 13-JUN-2012, sequence version 1.
DT 03-AUG-2022, entry version 61.
DE RecName: Full=Glutamate decarboxylase-like protein FG08083 {ECO:0000303|PubMed:17175185};
DE EC=4.1.1.- {ECO:0000305|PubMed:17175185};
DE AltName: Full=Butenolide biosynthesis cluster protein FG08083 {ECO:0000303|PubMed:17175185};
GN ORFNames=FG08083, FGRAMPH1_01T09075;
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: Glutamate decarboxylase-like protein; 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=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000250|UniProtKB:Q99259};
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 group II decarboxylase family.
CC {ECO:0000305}.
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DR EMBL; HG970333; CEF76340.1; -; Genomic_DNA.
DR RefSeq; XP_011320739.1; XM_011322437.1.
DR AlphaFoldDB; I1RV23; -.
DR SMR; I1RV23; -.
DR STRING; 5518.FGSG_08083P0; -.
DR GeneID; 23555117; -.
DR KEGG; fgr:FGSG_08083; -.
DR VEuPathDB; FungiDB:FGRAMPH1_01G09075; -.
DR eggNOG; KOG0629; Eukaryota.
DR HOGENOM; CLU_011856_0_0_1; -.
DR InParanoid; I1RV23; -.
DR Proteomes; UP000070720; Chromosome 2.
DR GO; GO:0016831; F:carboxy-lyase activity; IEA:UniProtKB-KW.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0019752; P:carboxylic acid metabolic process; IEA:InterPro.
DR Gene3D; 3.40.640.10; -; 1.
DR InterPro; IPR002129; PyrdxlP-dep_de-COase.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR Pfam; PF00282; Pyridoxal_deC; 2.
DR SUPFAM; SSF53383; SSF53383; 1.
PE 2: Evidence at transcript level;
KW Decarboxylase; Lyase; Pyridoxal phosphate; Reference proteome.
FT CHAIN 1..520
FT /note="Glutamate decarboxylase-like protein FG08083"
FT /id="PRO_0000450728"
FT REGION 338..357
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 86..88
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q99259"
FT BINDING 492
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q99259"
FT MOD_RES 300
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000250|UniProtKB:Q99259"
SQ SEQUENCE 520 AA; 56206 MW; 50FE334DBD9845E0 CRC64;
MDNGLSRRHE ISELLQLVDS TTTRAFHTSN GSPKSDCRND SKPLKRYEEL FGSFPAEGLG
TSGFKDAIDL ISRNSVDNAS PGFLGKLVSA PSAPGIASDL FLSILNNNGH VQRAGPALTA
IEKHTSLELA RLFDLQGPHA GGVTVPGGAA GNLMAMLVAR NIVAPESKQR GLTPGEYAIF
VSDAAHYSVS NSANVIGLGN DSIIRVPALD DGTMDADALQ RAVDQAGKDG KKPLLIAATS
GSTVNGAFDP LDKIGEIAHR VGAWFHVDAC WGGGVVFSDK LKHLMKGSHL ADSIAFNPHK
LLGVPLVCAF LLVNDLRTLW LANKLNAGYL FHDDAPKKNG VSSEQSANTN GSEKESWRHS
KLLDTAPDVM KINDLASLTI QCSRRHDATK MFLHWLYYGT AGIAREVEQA VDSAKHLACL
VRDHPRFELI WDPEQVFAQV CFYWKSASTP EKSGETLAEI NSRNTRALFQ GIEEMGWKVD
FAPGKAKGEF LRIACNRLTT RQTVEKIVSE LVELGESLGL
