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XYN1_GIBZE
ID   XYN1_GIBZE              Reviewed;         354 AA.
AC   I1RQU5; A0A098DQN2; A0A0E0SB56;
DT   09-JUL-2014, integrated into UniProtKB/Swiss-Prot.
DT   13-JUN-2012, sequence version 1.
DT   25-MAY-2022, entry version 46.
DE   RecName: Full=Endo-1,4-beta-xylanase 1;
DE            Short=Xylanase 1;
DE            EC=3.2.1.8;
DE   AltName: Full=1,4-beta-D-xylan xylanohydrolase 1;
DE   Flags: Precursor;
GN   Name=XYL1; ORFNames=FGRRES_06445, FGSG_06445;
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   INDUCTION.
RX   PubMed=16707104; DOI=10.1016/j.bbrc.2006.04.171;
RA   Hatsch D., Phalip V., Petkovski E., Jeltsch J.M.;
RT   "Fusarium graminearum on plant cell wall: no fewer than 30 xylanase genes
RT   transcribed.";
RL   Biochem. Biophys. Res. Commun. 345:959-966(2006).
RN   [5]
RP   INDUCTION.
RX   PubMed=17924109; DOI=10.1007/s00294-007-0154-x;
RA   Brunner K., Lichtenauer A.M., Kratochwill K., Delic M., Mach R.L.;
RT   "Xyr1 regulates xylanase but not cellulase formation in the head blight
RT   fungus Fusarium graminearum.";
RL   Curr. Genet. 52:213-220(2007).
RN   [6]
RP   SUBCELLULAR LOCATION, IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION,
RP   CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX   PubMed=22313372; DOI=10.1021/jf203407p;
RA   Dong X., Meinhardt S.W., Schwarz P.B.;
RT   "Isolation and characterization of two endoxylanases from Fusarium
RT   graminearum.";
RL   J. Agric. Food Chem. 60:2538-2545(2012).
RN   [7]
RP   INDUCTION.
RX   PubMed=23337356; DOI=10.1016/j.plaphy.2012.12.008;
RA   Sella L., Gazzetti K., Faoro F., Odorizzi S., D'Ovidio R., Schafer W.,
RA   Favaron F.;
RT   "A Fusarium graminearum xylanase expressed during wheat infection is a
RT   necrotizing factor but is not essential for virulence.";
RL   Plant Physiol. Biochem. 64:1-10(2013).
CC   -!- FUNCTION: Endo-1,4-beta-xylanase involved in the hydrolysis of xylan, a
CC       major structural heterogeneous polysaccharide found in plant biomass
CC       representing the second most abundant polysaccharide in the biosphere,
CC       after cellulose. Plays an important role in causing fusarium head
CC       blight (FHB) on cereal crops. {ECO:0000269|PubMed:22313372}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Endohydrolysis of (1->4)-beta-D-xylosidic linkages in xylans.;
CC         EC=3.2.1.8; Evidence={ECO:0000269|PubMed:22313372};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=0.86 mg/ml for xylan {ECO:0000269|PubMed:22313372};
CC         KM=1.7 mg/ml for arabinoxylan {ECO:0000269|PubMed:22313372};
CC         Vmax=15.9 umol/min/mg enzyme toward xylan
CC         {ECO:0000269|PubMed:22313372};
CC         Vmax=12.4 umol/min/mg enzyme toward arabinoxylan
CC         {ECO:0000269|PubMed:22313372};
CC       pH dependence:
CC         Optimum pH is 6.0. {ECO:0000269|PubMed:22313372};
CC       Temperature dependence:
CC         Optimum temperature is 40 degrees Celsius.
CC         {ECO:0000269|PubMed:22313372};
CC   -!- PATHWAY: Glycan degradation; xylan degradation.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:22313372}.
CC   -!- INDUCTION: Expression is under the control of transcription factor XYR1
CC       and highly induced by xylan. {ECO:0000269|PubMed:16707104,
CC       ECO:0000269|PubMed:17924109, ECO:0000269|PubMed:23337356}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 10 (cellulase F) family.
CC       {ECO:0000305}.
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DR   EMBL; AY730561; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; DS231666; ESU12536.1; -; Genomic_DNA.
DR   EMBL; HG970335; CEF83669.1; -; Genomic_DNA.
DR   RefSeq; XP_011326043.1; XM_011327741.1.
DR   AlphaFoldDB; I1RQU5; -.
DR   SMR; I1RQU5; -.
DR   STRING; 5518.FGSG_06445P0; -.
DR   EnsemblFungi; ESU12536; ESU12536; FGSG_06445.
DR   GeneID; 23553577; -.
DR   KEGG; fgr:FGSG_06445; -.
DR   VEuPathDB; FungiDB:FGRAMPH1_01G22295; -.
DR   eggNOG; ENOG502SHCI; Eukaryota.
DR   HOGENOM; CLU_020161_1_0_1; -.
DR   InParanoid; I1RQU5; -.
DR   UniPathway; UPA00114; -.
DR   Proteomes; UP000070720; Chromosome 4.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0031176; F:endo-1,4-beta-xylanase activity; IEA:UniProtKB-EC.
DR   GO; GO:0045493; P:xylan catabolic process; IEA:UniProtKB-UniPathway.
DR   InterPro; IPR044846; GH10.
DR   InterPro; IPR001000; GH10_dom.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   PANTHER; PTHR31490; PTHR31490; 1.
DR   Pfam; PF00331; Glyco_hydro_10; 1.
DR   PRINTS; PR00134; GLHYDRLASE10.
DR   SMART; SM00633; Glyco_10; 1.
DR   SUPFAM; SSF51445; SSF51445; 1.
DR   PROSITE; PS51760; GH10_2; 1.
PE   1: Evidence at protein level;
KW   Carbohydrate metabolism; Disulfide bond; Glycoprotein; Glycosidase;
KW   Hydrolase; Polysaccharide degradation; Reference proteome; Secreted;
KW   Signal; Virulence; Xylan degradation.
FT   SIGNAL          1..?
FT                   /evidence="ECO:0000255"
FT   CHAIN           ?..354
FT                   /note="Endo-1,4-beta-xylanase 1"
FT                   /id="PRO_0000429613"
FT   DOMAIN          19..339
FT                   /note="GH10"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01096"
FT   ACT_SITE        147
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        261
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        117
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        289..295
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   354 AA;  39336 MW;  A593D4861805182C CRC64;
     MAWLQPTLCR KELESRQTSG LDAAMKAAGK KYFGTALTVR NDAGETNVLN TKGEFGSITP
     ENAMKWEAIQ PNRGQFNWGP ADQHANAATQ RGMELRCHTL VWHSQLPSWV ANGNWNNQTL
     QQVMKDHINA VMGRYKGKCT HWDVVNEALN EDGTYRDSVF YRVIGEAFIP IAFRMVLAAD
     PTTKLYYNDY NLEYGGAKTA GAIRITKLIQ SYGLRIDGVG LQAHMTSEST PTQSTVTPSR
     ANLASVLNSF TKLNVDVAYT ELDIRMNTPA NQQKLQANAA AYARMVGSCM DVKRCVGVTV
     WGISDKYSWV PGTFPGEGSA LLWDDNFNKK PSYTSSLNTI RACWKCHRLL VSIS
 
 
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