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BUT78_GIBZE
ID   BUT78_GIBZE             Reviewed;         546 AA.
AC   I1RV18;
DT   12-AUG-2020, integrated into UniProtKB/Swiss-Prot.
DT   13-JUN-2012, sequence version 1.
DT   25-MAY-2022, entry version 56.
DE   RecName: Full=Amidase FG08078 {ECO:0000303|PubMed:17175185};
DE            EC=3.5.1.- {ECO:0000305|PubMed:17175185};
DE   AltName: Full=Butenolide biosynthesis cluster protein FG08078 {ECO:0000303|PubMed:17175185};
GN   ORFNames=FG08078, FGRAMPH1_01T09065;
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: Amidase; part of the gene cluster that mediates the
CC       biosynthesis of butenolide, a mycotoxin that shows antibiotic activity
CC       but does not seem to play a major role in the spread of head blight in
CC       wheat (PubMed:17175185). Butenolide is derived from glutamic acid via a
CC       4-acetamido-2-butenoic acid intermediate (Probable). The predicted
CC       function of the NADH:flavin oxidoreductase FG08077, the cytochrome P450
CC       monooxygenase FG08079, the decarboxylase FG08083, and the putative
CC       acetyltransferase FG08082 are consistent with this pathway, however,
CC       the respective activities of the butelonide biosynthesis cluster
CC       enzymes have still to be experimentally determined (Probable).
CC       {ECO:0000269|PubMed:17175185, ECO:0000305|PubMed:17175185}.
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 amidase family. {ECO:0000305}.
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DR   EMBL; HG970333; CEF76335.1; -; Genomic_DNA.
DR   RefSeq; XP_011320744.1; XM_011322442.1.
DR   AlphaFoldDB; I1RV18; -.
DR   SMR; I1RV18; -.
DR   STRING; 5518.FGSG_08078P0; -.
DR   GeneID; 23555112; -.
DR   KEGG; fgr:FGSG_08078; -.
DR   VEuPathDB; FungiDB:FGRAMPH1_01G09065; -.
DR   eggNOG; KOG1212; Eukaryota.
DR   HOGENOM; CLU_009600_9_2_1; -.
DR   InParanoid; I1RV18; -.
DR   Proteomes; UP000070720; Chromosome 2.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR   Gene3D; 3.90.1300.10; -; 1.
DR   InterPro; IPR023631; Amidase_dom.
DR   InterPro; IPR036928; AS_sf.
DR   Pfam; PF01425; Amidase; 1.
DR   SUPFAM; SSF75304; SSF75304; 1.
PE   2: Evidence at transcript level;
KW   Hydrolase; Reference proteome.
FT   CHAIN           1..546
FT                   /note="Amidase FG08078"
FT                   /id="PRO_0000450723"
FT   ACT_SITE        129
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250|UniProtKB:P97612"
FT   ACT_SITE        204
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250|UniProtKB:P97612"
FT   ACT_SITE        228
FT                   /note="Acyl-ester intermediate"
FT                   /evidence="ECO:0000250|UniProtKB:P97612"
SQ   SEQUENCE   546 AA;  60107 MW;  13AF46F3119DEE4A CRC64;
     MSWKAIAKAA QAEVLDAIPT KWKLDPAKYR TLTDVTSVPR ECGILSDAQL SITDLTALEV
     VKRIESRELT AVQALEAFGA RTAIAHQLVN CLMDWFYEDG LRQAEELDKS FKATGKLKGP
     LHGVPVALKD FHFVAGRPTT TGYVSRRDFR PEHDSALVKT LRDAGAVFYC KTTMPQSGMA
     IETVSNLWGR TLNPYNTALS AGGSSGGDAV LVALKGTPIT PSTDLGGSIR VPAAFNGLYA
     IRPTSDRIPK GGMDNINSGQ ISIKLSCGPI CHSMEDLESF TKLINAYPEN QNDPTSVPVP
     WKTVKPIEGK LTIGLMKWDK VVMPHPPVIR ALEHTKRTLE KAGHEVVEFD VPFDCWDAIQ
     TTFDTYYQSG HSGTLSTLEA TGEPLIPAFE DLIKVFGSKE ISAAESQQLN VKARIFREKF
     RDAWDATTKL TSTGRPVDAL ICPTAPAVGY PHDFNVYWGY TSLFNLLDYP SVILPVANFK
     VNPQDDPVAS NYKPLETNPY DKPNHELYKP ELFSSQPSTI QVVGRPFQDE ELIKVSSVMD
     DLLRAM
 
 
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