XYNA_GIBZE
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 25-MAY-2022, entry version 51.
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 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 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 [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|Ref.6}.
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|Ref.6};
CC -!- ACTIVITY REGULATION: Inhibited by the proteinaceous endoxylanase
CC inhibitor I from T.aestivum (TAXI-I). {ECO:0000269|PubMed:15629130,
CC 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, 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) family.
CC {ECO:0000305}.
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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 AlphaFoldDB; I1S2K3; -.
DR SMR; I1S2K3; -.
DR STRING; 229533.I1S2K3; -.
DR EnsemblFungi; ESU17749; ESU17749; FGSG_10999.
DR GeneID; 23557873; -.
DR KEGG; fgr:FGSG_10999; -.
DR VEuPathDB; FungiDB:FGRAMPH1_01G20977; -.
DR eggNOG; ENOG502RXA7; Eukaryota.
DR HOGENOM; CLU_052631_0_0_1; -.
DR InParanoid; I1S2K3; -.
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: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; Glycoprotein; Glycosidase; Hydrolase;
KW Polysaccharide degradation; Reference proteome; Secreted; Signal;
KW Virulence; Xylan degradation.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT CHAIN 20..231
FT /note="Endo-1,4-beta-xylanase A"
FT /id="PRO_0000429609"
FT DOMAIN 41..229
FT /note="GH11"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01097"
FT ACT_SITE 125
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10062"
FT ACT_SITE 216
FT /note="Proton donor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10063"
FT CARBOHYD 32
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="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
