XYNC_GIBZE
ID XYNC_GIBZE Reviewed; 327 AA.
AC I1S3T9; A0A098E530; A0A0E0SR14;
DT 09-JUL-2014, integrated into UniProtKB/Swiss-Prot.
DT 13-JUN-2012, sequence version 1.
DT 25-MAY-2022, entry version 50.
DE RecName: Full=Endo-1,4-beta-xylanase C;
DE Short=Xylanase B;
DE EC=3.2.1.8;
DE AltName: Full=1,4-beta-D-xylan xylanohydrolase C;
DE Flags: Precursor;
GN Name=XYLC; ORFNames=FGRRES_11487, FGSG_11487;
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, 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|Ref.6};
CC -!- ACTIVITY REGULATION: Weakly inhibited by the wheat xylanase inhibiting
CC protein I (XIP-I). {ECO:0000269|Ref.6}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=3.6 mg/ml for wheat flour arabinoxylan {ECO:0000269|Ref.6};
CC KM=3.5 mg/ml for soluble oat spelt xylan {ECO:0000269|Ref.6};
CC KM=6.3 mg/ml for soluble birchwood xylan {ECO:0000269|Ref.6};
CC pH dependence:
CC Optimum pH is 5.0-7.0. {ECO:0000269|Ref.6};
CC Temperature dependence:
CC Optimum temperature is 40 degrees Celsius. {ECO:0000269|Ref.6};
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; AY575965; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; DS231671; ESU18104.1; -; Genomic_DNA.
DR EMBL; HG970334; CEF88877.1; -; Genomic_DNA.
DR RefSeq; XP_011325726.1; XM_011327424.1.
DR AlphaFoldDB; I1S3T9; -.
DR SMR; I1S3T9; -.
DR STRING; 5518.FGSG_11487P0; -.
DR CLAE; XYN10C_GIBZE; -.
DR EnsemblFungi; ESU18104; ESU18104; FGSG_11487.
DR GeneID; 23558319; -.
DR KEGG; fgr:FGSG_11487; -.
DR VEuPathDB; FungiDB:FGRAMPH1_01G22187; -.
DR eggNOG; ENOG502QSCW; Eukaryota.
DR HOGENOM; CLU_020161_2_1_1; -.
DR InParanoid; I1S3T9; -.
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 InterPro; IPR044846; GH10.
DR InterPro; IPR001000; GH10_dom.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR PANTHER; PTHR31490; PTHR31490; 1.
DR Pfam; PF00331; Glyco_hydro_10; 1.
DR PRINTS; PR00134; GLHYDRLASE10.
DR SMART; SM00633; Glyco_10; 1.
DR SUPFAM; SSF51445; SSF51445; 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..15
FT /evidence="ECO:0000255"
FT CHAIN 16..327
FT /note="Endo-1,4-beta-xylanase C"
FT /id="PRO_0000429611"
FT DOMAIN 43..325
FT /note="GH10"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01096"
FT ACT_SITE 154
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT ACT_SITE 262
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT DISULFID 280..286
FT /evidence="ECO:0000250"
SQ SEQUENCE 327 AA; 35739 MW; 5552A6A73E487C4E CRC64;
MKFSSLLFTA SLVAAMPASI EPRQAQESIN KLIKAKGKLY YGTITDPNLL QSQQNNAVIK
ADFGQVTPEN SMKWDATEPQ QGKFNFGGGD QVVNFAAQNG LKVRGHALVW HSQLPQWVHN
IKDKTQMKNA IENHIKNVAG HFKGKVYAWD VLNEIFDWDG SLRKDSPFTQ VLGEEFVGIA
FRAARAADPN AKLYINDYSI DDPNAAKLKA GMVAHVKKWV SQGIPIDGIG SQTHLDPGAA
NGVQAALQQM ASTGVKEVAI TELDIRSAPA ADYATVTKAC LNVPKCVGIT VWGVSDKDSW
RKEKDSLLFN AQYQAKPAYT AVVNALR
