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Database: UniProt
Entry: M4U3F7_9XANT
LinkDB: M4U3F7_9XANT
Original site: M4U3F7_9XANT 
ID   M4U3F7_9XANT            Unreviewed;       319 AA.
AC   M4U3F7;
DT   29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   29-MAY-2013, sequence version 1.
DT   27-MAR-2024, entry version 33.
DE   RecName: Full=Beta-xylanase {ECO:0000256|RuleBase:RU361174};
DE            EC=3.2.1.8 {ECO:0000256|RuleBase:RU361174};
GN   ORFNames=XAC29_21460 {ECO:0000313|EMBL:AGH79677.1};
OS   Xanthomonas axonopodis Xac29-1.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC   Xanthomonadaceae; Xanthomonas.
OX   NCBI_TaxID=1304892 {ECO:0000313|EMBL:AGH79677.1, ECO:0000313|Proteomes:UP000011979};
RN   [1] {ECO:0000313|EMBL:AGH79677.1, ECO:0000313|Proteomes:UP000011979}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Xac29-1 {ECO:0000313|EMBL:AGH79677.1,
RC   ECO:0000313|Proteomes:UP000011979};
RA   Chen G., Zou H., Ye G., Song X., Ji Z., Ma W.;
RT   "Completed genome of Xanthomonas axonopodis sp. Xac29-1.";
RL   Submitted (MAR-2013) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Endohydrolysis of (1->4)-beta-D-xylosidic linkages in xylans.;
CC         EC=3.2.1.8; Evidence={ECO:0000256|RuleBase:RU361174};
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 10 (cellulase F) family.
CC       {ECO:0000256|RuleBase:RU361174}.
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DR   EMBL; CP004399; AGH79677.1; -; Genomic_DNA.
DR   AlphaFoldDB; M4U3F7; -.
DR   KEGG; xao:XAC29_21460; -.
DR   PATRIC; fig|1304892.4.peg.4486; -.
DR   HOGENOM; CLU_041139_0_0_6; -.
DR   Proteomes; UP000011979; Chromosome.
DR   GO; GO:0031176; F:endo-1,4-beta-xylanase activity; IEA:UniProtKB-EC.
DR   GO; GO:0045493; P:xylan catabolic process; IEA:UniProtKB-KW.
DR   Gene3D; 3.20.20.80; Glycosidases; 1.
DR   InterPro; IPR044846; GH10.
DR   InterPro; IPR001000; GH10_dom.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   PANTHER; PTHR31490:SF1; ENDO-1,4-BETA-XYLANASE 1; 1.
DR   PANTHER; PTHR31490; GLYCOSYL HYDROLASE; 1.
DR   Pfam; PF00331; Glyco_hydro_10; 1.
DR   PRINTS; PR00134; GLHYDRLASE10.
DR   SMART; SM00633; Glyco_10; 1.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR   PROSITE; PS51760; GH10_2; 1.
PE   3: Inferred from homology;
KW   Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023277,
KW   ECO:0000256|RuleBase:RU361174};
KW   Glycosidase {ECO:0000256|RuleBase:RU361174, ECO:0000313|EMBL:AGH79677.1};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU361174};
KW   Polysaccharide degradation {ECO:0000256|ARBA:ARBA00023326,
KW   ECO:0000256|RuleBase:RU361174};
KW   Xylan degradation {ECO:0000313|EMBL:AGH79677.1}.
FT   DOMAIN          11..309
FT                   /note="GH10"
FT                   /evidence="ECO:0000259|PROSITE:PS51760"
SQ   SEQUENCE   319 AA;  35596 MW;  61ADF59D82A9142E CRC64;
     MAAGMAAPVH AAPLAATASK FLGCAYGAQQ APGFAQYWNK LTPENGGKWG SVEAVRDQMD
     WSTLDAAYRF AQANQMPFQM HVMVWGNQQP EWIKTLRPAE QRREIEQWFA AVAQRYPDIA
     LLEVVNEPLN DPPSKADTGG GNYLQALGGN GDSGWEWVLQ SFRLARRHFP HTKLMINDYS
     ITSSAQATQK YLQIVRLLQR ENLVDAIGVQ EHAFETTPEV AVSVHRDNLD ALAATGLPIY
     ITEFDLDGPT DAQQLADYKR VFPVFWEHPA VHGITLWGFR PGLWRDKEAA YLIRADGTER
     PALTWLRDYV AAHPGTPAP
//
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