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Database: UniProt
Entry: I1RII8
LinkDB: I1RII8
Original site: I1RII8 
ID   XYNB_GIBZE              Reviewed;         228 AA.
AC   I1RII8; A0A0E0S4N8;
DT   09-JUL-2014, integrated into UniProtKB/Swiss-Prot.
DT   13-JUN-2012, sequence version 1.
DT   10-APR-2019, entry version 42.
DE   RecName: Full=Endo-1,4-beta-xylanase B;
DE            Short=Xylanase B;
DE            EC=3.2.1.8;
DE   AltName: Full=1,4-beta-D-xylan xylanohydrolase B;
DE   AltName: Full=Xylanase 2;
DE   Flags: Precursor;
GN   Name=XYLB; Synonyms=XYL2; ORFNames=FGRRES_03624, FGSG_03624;
OS   Gibberella zeae (strain PH-1 / ATCC MYA-4620 / FGSC 9075 / NRRL 31084)
OS   (Wheat head blight fungus) (Fusarium graminearum).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina;
OC   Sordariomycetes; Hypocreomycetidae; Hypocreales; Nectriaceae;
OC   Fusarium.
OX   NCBI_TaxID=229533;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PH-1 / ATCC MYA-4620 / FGSC 9075 / NRRL 31084;
RX   PubMed=17823352; DOI=10.1126/science.1143708;
RA   Cuomo C.A., Gueldener U., Xu J.-R., Trail F., Turgeon B.G.,
RA   Di Pietro A., Walton J.D., Ma L.-J., Baker S.E., Rep M., Adam G.,
RA   Antoniw J., Baldwin T., Calvo S.E., Chang Y.-L., DeCaprio D.,
RA   Gale L.R., Gnerre S., Goswami R.S., Hammond-Kosack K., Harris L.J.,
RA   Hilburn K., Kennell J.C., Kroken S., Magnuson J.K., Mannhaupt G.,
RA   Mauceli E.W., Mewes H.-W., Mitterbauer R., Muehlbauer G.,
RA   Muensterkoetter M., Nelson D., O'Donnell K., Ouellet T., Qi W.,
RA   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=PH-1 / ATCC MYA-4620 / FGSC 9075 / NRRL 31084;
RX   PubMed=20237561; DOI=10.1038/nature08850;
RA   Ma L.-J., van der Does H.C., Borkovich K.A., Coleman J.J.,
RA   Daboussi M.-J., Di Pietro A., Dufresne M., Freitag M., Grabherr M.,
RA   Henrissat B., Houterman P.M., Kang S., Shim W.-B., Woloshuk C.,
RA   Xie X., Xu J.-R., Antoniw J., Baker S.E., Bluhm B.H., Breakspear A.,
RA   Brown D.W., Butchko R.A.E., Chapman S., Coulson R., Coutinho P.M.,
RA   Danchin E.G.J., Diener A., Gale L.R., Gardiner D.M., Goff S.,
RA   Hammond-Kosack K.E., Hilburn K., Hua-Van A., Jonkers W., Kazan K.,
RA   Kodira C.D., Koehrsen M., Kumar L., Lee Y.-H., Li L., Manners J.M.,
RA   Miranda-Saavedra D., Mukherjee M., Park G., Park J., Park S.-Y.,
RA   Proctor R.H., Regev A., Ruiz-Roldan M.C., Sain D., Sakthikumar S.,
RA   Sykes S., Schwartz D.C., Turgeon B.G., Wapinski I., Yoder O.,
RA   Young S., Zeng Q., Zhou S., Galagan J., Cuomo C.A., Kistler H.C.,
RA   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=PH-1 / ATCC MYA-4620 / FGSC 9075 / NRRL 31084;
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
RT   Fusarium graminearum.";
RL   BMC Genomics 16:544-544(2015).
RN   [4]
RP   SUBCELLULAR LOCATION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL
RP   PROPERTIES, AND ACTIVITY REGULATION.
RX   PubMed=15629130; DOI=10.1016/j.bbrc.2004.12.036;
RA   Belien T., Van Campenhout S., Van Acker M., Volckaert G.;
RT   "Cloning and characterization of two endoxylanases from the cereal
RT   phytopathogen Fusarium graminearum and their inhibition profile
RT   against endoxylanase inhibitors from wheat.";
RL   Biochem. Biophys. Res. Commun. 327:407-414(2005).
RN   [5]
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
RT   genes transcribed.";
RL   Biochem. Biophys. Res. Commun. 345:959-966(2006).
RN   [6]
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
RT   blight fungus Fusarium graminearum.";
RL   Curr. Genet. 52:213-220(2007).
RN   [7]
RP   FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND
RP   ACTIVITY REGULATION.
RX   DOI=10.1016/j.enzmictec.2008.12.005;
RA   Pollet A., Belien T., Fierens K., Delcour J.A., Courtin C.M.;
RT   "Fusarium graminearum xylanases show different functional stabilities,
RT   substrate specificities and inhibition sensitivities.";
RL   Enzyme Microb. Technol. 44:189-195(2009).
RN   [8]
RP   SUBCELLULAR LOCATION, IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION,
RP   CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND ACTIVITY
RP   REGULATION.
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   [9]
RP   INDUCTION, FUNCTION, AND DISRUPTION PHENOTYPE.
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).
RN   [10]
RP   FUNCTION, AND DISRUPTION PHENOTYPE.
RX   PubMed=24779355; DOI=10.1094/PHYTO-12-13-0355-R;
RA   Sella L., Gazzetti K.G., Castiglioni C., Schafer W., Favaron F.;
RT   "Fusarium graminearum possesses virulence factors common to Fusarium
RT   head blight of wheat and seedling rot of soybean, but differing in
RT   their impact on disease severity.";
RL   Phytopathology 104:1201-1207(2014).
CC   -!- FUNCTION: Endo-1,4-beta-xylanase involved in the hydrolysis of
CC       xylan, a major structural heterogeneous polysaccharide found in
CC       plant biomass representing the second most abundant polysaccharide
CC       in the biosphere, after cellulose. Plays a important role in
CC       causing fusarium head blight (FHB) on cereal crops. Induces cell
CC       death and hydrogen peroxide accumulation in infected wheat leaves.
CC       {ECO:0000269|PubMed:22313372, ECO:0000269|PubMed:23337356,
CC       ECO:0000269|PubMed:24779355, ECO:0000269|Ref.7}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Endohydrolysis of (1->4)-beta-D-xylosidic linkages in
CC         xylans.; EC=3.2.1.8; Evidence={ECO:0000269|PubMed:15629130,
CC         ECO:0000269|PubMed:22313372, ECO:0000269|Ref.7};
CC   -!- ACTIVITY REGULATION: Inhibited by the proteinaceous endoxylanase
CC       inhibitor I from T.aestivum (TAXI-I).
CC       {ECO:0000269|PubMed:15629130, ECO:0000269|PubMed:22313372,
CC       ECO:0000269|Ref.7}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=6.2 mg/ml for wheat flour arabinoxylan
CC         {ECO:0000269|PubMed:15629130, ECO:0000269|PubMed:22313372,
CC         ECO:0000269|Ref.7};
CC         KM=4.3 mg/ml for soluble oat spelt xylan
CC         {ECO:0000269|PubMed:15629130, ECO:0000269|PubMed:22313372,
CC         ECO:0000269|Ref.7};
CC         KM=11.9 mg/ml for soluble birchwood xylan
CC         {ECO:0000269|PubMed:15629130, ECO:0000269|PubMed:22313372,
CC         ECO:0000269|Ref.7};
CC         Vmax=18.4 umol/min/mg enzyme toward xylan
CC         {ECO:0000269|PubMed:15629130, ECO:0000269|PubMed:22313372,
CC         ECO:0000269|Ref.7};
CC         Vmax=61.7 umol/min/mg enzyme toward arabinoxylan
CC         {ECO:0000269|PubMed:15629130, ECO:0000269|PubMed:22313372,
CC         ECO:0000269|Ref.7};
CC       pH dependence:
CC         Optimum pH is 7.0. {ECO:0000269|PubMed:15629130,
CC         ECO:0000269|PubMed:22313372, ECO:0000269|Ref.7};
CC       Temperature dependence:
CC         Optimum temperature is 40 degrees Celsius.
CC         {ECO:0000269|PubMed:15629130, ECO:0000269|PubMed:22313372,
CC         ECO:0000269|Ref.7};
CC   -!- PATHWAY: Glycan degradation; xylan degradation.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:15629130,
CC       ECO:0000269|PubMed:22313372}.
CC   -!- INDUCTION: Expression is under the control of transcription factor
CC       XYR1 and highly induced during wheat infection and by xylan.
CC       {ECO:0000269|PubMed:16707104, ECO:0000269|PubMed:17924109,
CC       ECO:0000269|PubMed:23337356}.
CC   -!- DISRUPTION PHENOTYPE: Leads to about 40 percent reduction of
CC       xylanase activity when grown in culture with xylan as carbon
CC       source. {ECO:0000269|PubMed:23337356,
CC       ECO:0000269|PubMed:24779355}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 11 (cellulase G)
CC       family. {ECO:0000305}.
DR   EMBL; AJ863566; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AY575961; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; DS231664; ESU09578.1; -; Genomic_DNA.
DR   EMBL; HG970333; CEF78463.1; -; Genomic_DNA.
DR   RefSeq; XP_011322077.1; XM_011323775.1.
DR   ProteinModelPortal; I1RII8; -.
DR   SMR; I1RII8; -.
DR   STRING; 5518.FGSG_03624P0; -.
DR   EnsemblFungi; ESU09578; ESU09578; FGSG_03624.
DR   GeneID; 23550922; -.
DR   KEGG; fgr:FGSG_03624; -.
DR   EuPathDB; FungiDB:FGRAMPH1_01G13319; -.
DR   eggNOG; ENOG410YH6C; LUCA.
DR   InParanoid; I1RII8; -.
DR   KO; K01181; -.
DR   UniPathway; UPA00114; -.
DR   Proteomes; UP000070720; Chromosome 2.
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:0009405; P:pathogenesis; IEA:UniProtKB-KW.
DR   GO; GO:0045493; P:xylan catabolic process; IEA:UniProtKB-UniPathway.
DR   Gene3D; 2.60.120.180; -; 1.
DR   InterPro; IPR013320; ConA-like_dom_sf.
DR   InterPro; IPR013319; GH11/12.
DR   InterPro; IPR018208; GH11_AS_1.
DR   InterPro; IPR033119; GH11_AS_2.
DR   InterPro; IPR033123; GH11_dom.
DR   InterPro; IPR001137; Glyco_hydro_11.
DR   Pfam; PF00457; Glyco_hydro_11; 1.
DR   PRINTS; PR00911; GLHYDRLASE11.
DR   SUPFAM; SSF49899; SSF49899; 1.
DR   PROSITE; PS00776; GH11_1; 1.
DR   PROSITE; PS00777; GH11_2; 1.
DR   PROSITE; PS51761; GH11_3; 1.
PE   1: Evidence at protein level;
KW   Carbohydrate metabolism; Complete proteome; Glycosidase; Hydrolase;
KW   Polysaccharide degradation; Reference proteome; Secreted; Signal;
KW   Virulence; Xylan degradation.
FT   SIGNAL        1     19       {ECO:0000255}.
FT   CHAIN        20    228       Endo-1,4-beta-xylanase B.
FT                                /FTId=PRO_0000429610.
FT   DOMAIN       37    227       GH11. {ECO:0000255|PROSITE-
FT                                ProRule:PRU01097}.
FT   ACT_SITE    122    122       Nucleophile. {ECO:0000255|PROSITE-
FT                                ProRule:PRU10062}.
FT   ACT_SITE    214    214       Proton donor. {ECO:0000255|PROSITE-
FT                                ProRule:PRU10063}.
SQ   SEQUENCE   228 AA;  24544 MW;  F21FFE62EC3B0B80 CRC64;
     MVSFTYLLAA VSAVTGAVAA PNPTKVDAQP PSGLLEKRTS PTTGVNNGFY FSFWTDTPSA
     VTYTNGNGGQ FSMNWNGNRG NHVGGKGWNP GAARTIKYSG DYRPNGNSYL AVYGWTRNPL
     VEYYIVENFG TYNPSSGAQK KGEINIDGSI YDIAVSTRNC APSIEGDCKT FQQYWSVRRN
     KRSSGSVNTG AHFNAWAQAG LRLGSHDYQI LAVEGYQSSG QATMTVSG
//
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