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Database: UniProt
Entry: I1S2K3
LinkDB: I1S2K3
Original site: I1S2K3 
ID   XYNA_GIBZE              Reviewed;         231 AA.
AC   I1S2K3; A0A0E0SN32;
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 A;
DE            Short=Xylanase A;
DE            EC=3.2.1.8;
DE   AltName: Full=1,4-beta-D-xylan xylanohydrolase A;
DE   Flags: Precursor;
GN   Name=XYLA; ORFNames=FGRRES_10999, FGSG_10999;
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   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   [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
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.
CC       {ECO:0000269|Ref.6}.
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|Ref.6};
CC   -!- ACTIVITY REGULATION: Inhibited by the proteinaceous endoxylanase
CC       inhibitor I from T.aestivum (TAXI-I).
CC       {ECO:0000269|PubMed:15629130, ECO:0000269|Ref.6}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=3.5 mg/ml for wheat flour arabinoxylan
CC         {ECO:0000269|PubMed:15629130, ECO:0000269|Ref.6};
CC         KM=3.1 mg/ml for soluble oat spelt xylan
CC         {ECO:0000269|PubMed:15629130, ECO:0000269|Ref.6};
CC         KM=5.1 mg/ml for soluble birchwood xylan
CC         {ECO:0000269|PubMed:15629130, ECO:0000269|Ref.6};
CC       pH dependence:
CC         Optimum pH is 8.0. {ECO:0000269|PubMed:15629130,
CC         ECO:0000269|Ref.6};
CC       Temperature dependence:
CC         Optimum temperature is 40 degrees Celsius.
CC         {ECO:0000269|PubMed:15629130, ECO:0000269|Ref.6};
CC   -!- PATHWAY: Glycan degradation; xylan degradation.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:15629130}.
CC   -!- INDUCTION: Expression is highly induced by xylan.
CC       {ECO:0000269|PubMed:16707104, ECO:0000269|PubMed:23337356}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 11 (cellulase G)
CC       family. {ECO:0000305}.
DR   EMBL; AY289919; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AY648860; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; DS231670; ESU17749.1; -; Genomic_DNA.
DR   EMBL; HG970334; CEF87845.1; -; Genomic_DNA.
DR   RefSeq; XP_011325371.1; XM_011327069.1.
DR   ProteinModelPortal; I1S2K3; -.
DR   SMR; I1S2K3; -.
DR   STRING; 5518.FGSG_10999P0; -.
DR   EnsemblFungi; ESU17749; ESU17749; FGSG_10999.
DR   GeneID; 23557873; -.
DR   KEGG; fgr:FGSG_10999; -.
DR   EuPathDB; FungiDB:FGRAMPH1_01G20977; -.
DR   eggNOG; ENOG410IHTC; Eukaryota.
DR   eggNOG; ENOG410YH6C; LUCA.
DR   InParanoid; I1S2K3; -.
DR   KO; K01181; -.
DR   UniPathway; UPA00114; -.
DR   Proteomes; UP000070720; Chromosome 3.
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; Glycoprotein; Glycosidase;
KW   Hydrolase; Polysaccharide degradation; Reference proteome; Secreted;
KW   Signal; Virulence; Xylan degradation.
FT   SIGNAL        1     19       {ECO:0000255}.
FT   CHAIN        20    231       Endo-1,4-beta-xylanase A.
FT                                /FTId=PRO_0000429609.
FT   DOMAIN       41    229       GH11. {ECO:0000255|PROSITE-
FT                                ProRule:PRU01097}.
FT   ACT_SITE    125    125       Nucleophile. {ECO:0000255|PROSITE-
FT                                ProRule:PRU10062}.
FT   ACT_SITE    216    216       Proton donor. {ECO:0000255|PROSITE-
FT                                ProRule:PRU10063}.
FT   CARBOHYD     32     32       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
SQ   SEQUENCE   231 AA;  25845 MW;  63FF356561AF8B02 CRC64;
     MVSFKSLLVA VSALTGALAR PFDFLDERDD GNATSVLEAR QVTGNSEGYH NGYFYSWWSD
     GGGYAQYRMG EGSHYQVDWR NTGNFVGGKG WNPGTGRTIN YGGSFNPQGN GYLCVYGWTR
     GPLVEYYVIE SYGSYNPGSQ AQHRGTVYTD GDTYDLYMST RYQQPSIDGV QTFNQYWSIR
     RNKRTSGSVN MQNHFNAWRS AGMNLGNHYY QILATEGYQS SGSSSIYVQT S
//
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