BUT81_GIBZE
ID BUT81_GIBZE Reviewed; 332 AA.
AC I1RV21;
DT 12-AUG-2020, integrated into UniProtKB/Swiss-Prot.
DT 13-JUN-2012, sequence version 1.
DT 03-AUG-2022, entry version 57.
DE RecName: Full=2-oxoglutarate-dependent dioxygenase FG08081 {ECO:0000303|PubMed:17175185};
DE EC=1.14.-.- {ECO:0000305|PubMed:17175185};
DE AltName: Full=Butenolide biosynthesis cluster protein FG08081 {ECO:0000303|PubMed:17175185};
GN ORFNames=FG08081, FGRAMPH1_01T09071;
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: 2-oxoglutarate-dependent dioxygenase; 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=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU00805};
CC Note=Binds 1 Fe(2+) ion per subunit. {ECO:0000255|PROSITE-
CC ProRule:PRU00805};
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 iron/ascorbate-dependent oxidoreductase
CC family. {ECO:0000305}.
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DR EMBL; HG970333; CEF76338.1; -; Genomic_DNA.
DR RefSeq; XP_011320741.1; XM_011322439.1.
DR AlphaFoldDB; I1RV21; -.
DR SMR; I1RV21; -.
DR STRING; 5518.FGSG_08081P0; -.
DR GeneID; 23555115; -.
DR KEGG; fgr:FGSG_08081; -.
DR VEuPathDB; FungiDB:FGRAMPH1_01G09071; -.
DR eggNOG; KOG0143; Eukaryota.
DR HOGENOM; CLU_010119_4_0_1; -.
DR InParanoid; I1RV21; -.
DR Proteomes; UP000070720; Chromosome 2.
DR GO; GO:0051213; F:dioxygenase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR Gene3D; 2.60.120.330; -; 1.
DR InterPro; IPR044861; IPNS-like_FE2OG_OXY.
DR InterPro; IPR027443; IPNS-like_sf.
DR InterPro; IPR005123; Oxoglu/Fe-dep_dioxygenase.
DR Pfam; PF03171; 2OG-FeII_Oxy; 1.
DR PROSITE; PS51471; FE2OG_OXY; 1.
PE 2: Evidence at transcript level;
KW Dioxygenase; Iron; Metal-binding; Oxidoreductase; Reference proteome.
FT CHAIN 1..332
FT /note="2-oxoglutarate-dependent dioxygenase FG08081"
FT /id="PRO_0000450726"
FT DOMAIN 176..280
FT /note="Fe2OG dioxygenase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT BINDING 201
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT BINDING 203
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT BINDING 258
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT BINDING 271
FT /ligand="2-oxoglutarate"
FT /ligand_id="ChEBI:CHEBI:16810"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
SQ SEQUENCE 332 AA; 37686 MW; 821149E7CED7763A CRC64;
MTASSRPAEY RDVRTANLNT ITFDNLFDKD EAELKRLIES CEKDGFFYLD LKSAASQKFW
NDLYTIDSTT KDWFKQPIEK KLQTPTVSLA HGFKAVGNQS GSIESKKDGF EALKIGKSEL
DGRWALPDVV SDNLPLFDQF ASSCHFISKL LLDCLSDGLN LKGDARFETH HRDDCRSKST
LYFLHYPPGA QDPNKVGQNM HTDIGTLTIL YAPQWGLQVF SPADGAWEYV EPRPNQIIVN
VGDTLRFLSG KRFKSALHRV LPLGGIQIED RYSISYFLRA SDSTEFKDSD EDESNAKQWY
TKKYAMYEMP HVIQKQQTTL SGGMAQELQA TF
