XYNB_GIBZE
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 25-MAY-2022, entry version 52.
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 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 SUBCELLULAR LOCATION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES,
RP 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 against
RT 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 genes
RT 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 blight
RT fungus Fusarium graminearum.";
RL Curr. Genet. 52:213-220(2007).
RN [7]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND ACTIVITY
RP 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 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 head
RT blight of wheat and seedling rot of soybean, but differing in their impact
RT on disease severity.";
RL Phytopathology 104:1201-1207(2014).
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. Induces cell death and hydrogen peroxide
CC accumulation in infected wheat leaves. {ECO:0000269|PubMed:22313372,
CC ECO:0000269|PubMed:23337356, ECO:0000269|PubMed:24779355,
CC ECO:0000269|Ref.7}.
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: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). {ECO:0000269|PubMed:15629130,
CC ECO:0000269|PubMed:22313372, 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 XYR1
CC 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 xylanase
CC activity when grown in culture with xylan as carbon source.
CC {ECO:0000269|PubMed:23337356, ECO:0000269|PubMed:24779355}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 11 (cellulase G) family.
CC {ECO:0000305}.
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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 AlphaFoldDB; I1RII8; -.
DR SMR; I1RII8; -.
DR STRING; 5518.FGSG_03624P0; -.
DR PRIDE; I1RII8; -.
DR EnsemblFungi; ESU09578; ESU09578; FGSG_03624.
DR GeneID; 23550922; -.
DR KEGG; fgr:FGSG_03624; -.
DR VEuPathDB; FungiDB:FGRAMPH1_01G13319; -.
DR eggNOG; ENOG502RXA7; Eukaryota.
DR HOGENOM; CLU_052631_0_0_1; -.
DR InParanoid; I1RII8; -.
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: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; Glycosidase; Hydrolase;
KW Polysaccharide degradation; Reference proteome; Secreted; Signal;
KW Virulence; Xylan degradation.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT CHAIN 20..228
FT /note="Endo-1,4-beta-xylanase B"
FT /id="PRO_0000429610"
FT DOMAIN 37..227
FT /note="GH11"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01097"
FT ACT_SITE 122
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10062"
FT ACT_SITE 214
FT /note="Proton donor"
FT /evidence="ECO:0000255|PROSITE-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
