XYND_GIBZE
ID XYND_GIBZE Reviewed; 381 AA.
AC I1S3C6; A0A0E0SJD3;
DT 09-JUL-2014, integrated into UniProtKB/Swiss-Prot.
DT 13-JUN-2012, sequence version 1.
DT 25-MAY-2022, entry version 53.
DE RecName: Full=Endo-1,4-beta-xylanase D;
DE Short=Xylanase D;
DE EC=3.2.1.8;
DE AltName: Full=1,4-beta-D-xylan xylanohydrolase D;
DE Flags: Precursor;
GN Name=XYLD; ORFNames=FGRRES_11304, FGSG_11304;
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 FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=18707875; DOI=10.1016/j.biortech.2008.07.006;
RA Carapito R., Carapito C., Jeltsch J.M., Phalip V.;
RT "Efficient hydrolysis of hemicellulose by a Fusarium graminearum xylanase
RT blend produced at high levels in Escherichia coli.";
RL Bioresour. Technol. 100:845-850(2009).
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 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:18707875,
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:18707875,
CC ECO:0000269|Ref.7};
CC -!- ACTIVITY REGULATION: Inhibited by the wheat xylanase inhibiting protein
CC I (XIP-I). {ECO:0000269|Ref.7}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 6.0. {ECO:0000269|PubMed:18707875, ECO:0000269|Ref.7};
CC Temperature dependence:
CC Optimum temperature is 50 degrees Celsius.
CC {ECO:0000269|PubMed:18707875, ECO:0000269|Ref.7};
CC -!- PATHWAY: Glycan degradation; xylan degradation.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC -!- INDUCTION: Expression is under the control of transcription factor XYR1
CC and highly induced by xylan, carboxymethylcellulose (CMC), and hop cell
CC wall. {ECO:0000269|PubMed:16707104, ECO:0000269|PubMed:17924109,
CC ECO:0000269|PubMed:23337356}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 10 (cellulase F) family.
CC {ECO:0000305}.
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DR EMBL; AY575964; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; DS231671; ESU18318.1; -; Genomic_DNA.
DR EMBL; HG970334; CEF86546.1; -; Genomic_DNA.
DR RefSeq; XP_011325940.1; XM_011327638.1.
DR AlphaFoldDB; I1S3C6; -.
DR SMR; I1S3C6; -.
DR STRING; 5518.FGSG_11304P0; -.
DR EnsemblFungi; ESU18318; ESU18318; FGSG_11304.
DR GeneID; 23558155; -.
DR KEGG; fgr:FGSG_11304; -.
DR VEuPathDB; FungiDB:FGRAMPH1_01G21737; -.
DR eggNOG; ENOG502QSCW; Eukaryota.
DR HOGENOM; CLU_020161_2_1_1; -.
DR InParanoid; I1S3C6; -.
DR UniPathway; UPA00114; -.
DR PHI-base; PHI:4246; -.
DR Proteomes; UP000070720; Chromosome 3.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0030248; F:cellulose binding; IEA:InterPro.
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; IPR035971; CBD_sf.
DR InterPro; IPR000254; Cellulose-bd_dom_fun.
DR InterPro; IPR044846; GH10.
DR InterPro; IPR001000; GH10_dom.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR PANTHER; PTHR31490; PTHR31490; 1.
DR Pfam; PF00734; CBM_1; 1.
DR Pfam; PF00331; Glyco_hydro_10; 1.
DR PRINTS; PR00134; GLHYDRLASE10.
DR SMART; SM00236; fCBD; 1.
DR SMART; SM00633; Glyco_10; 1.
DR SUPFAM; SSF51445; SSF51445; 1.
DR SUPFAM; SSF57180; SSF57180; 1.
DR PROSITE; PS00562; CBM1_1; 1.
DR PROSITE; PS51164; CBM1_2; 1.
DR PROSITE; PS51760; GH10_2; 1.
PE 1: Evidence at protein level;
KW Carbohydrate metabolism; Disulfide bond; Glycosidase; Hydrolase;
KW Polysaccharide degradation; Reference proteome; Secreted; Signal;
KW Virulence; Xylan degradation.
FT SIGNAL 1..18
FT /evidence="ECO:0000255"
FT CHAIN 19..381
FT /note="Endo-1,4-beta-xylanase D"
FT /id="PRO_0000429612"
FT DOMAIN 19..52
FT /note="CBM1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00597"
FT DOMAIN 74..379
FT /note="GH10"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01096"
FT REGION 58..78
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 58..74
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 205
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT ACT_SITE 316
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT DISULFID 334..340
FT /evidence="ECO:0000250"
SQ SEQUENCE 381 AA; 41327 MW; B57FB580B66AF72E CRC64;
MHFLGLVVAF APAALAQSAI WGQCGGTGWS GSTTCQSGLK CEKINDFYYQ CIPGSDNGGG
TTPDPGTPSP GNGNADATGL DAKIRAKGKI YFGTEIDHYH LSNNPLINIV KKDFGQVTNE
NSMKWDAIEP SRGQFTFSNA DKVVDFAQAN GKKIRGHTLL WYSQLPQWVK NIRDRATMTS
VIENHVKTVV TRYKGKILHW DVVNEIFAED GNMRNSEFYQ VLGEDFVGIA FRAARAADPA
AKLYINDYNL DIANYAKVTR GMVDHVNKWV SQGIPIDGIG SQAHLAKPGG WNPASGFPAA
LKVLAGANVK EVAITELDID GAAANDYVTV VNSCLTTPKC VGITVWGVSD KDSWRSESNP
LLFDRNYQPK AAYTAVSNAL N
