ID   XYNB_CELJU              Reviewed;         599 AA.
AC   P23030; B3PEH8;
DT   01-NOV-1991, integrated into UniProtKB/Swiss-Prot.
DT   20-APR-2010, sequence version 2.
DT   25-MAY-2022, entry version 133.
DE   RecName: Full=Endo-1,4-beta-xylanase B;
DE            Short=Xylanase B;
DE            EC=3.2.1.8;
DE   AltName: Full=1,4-beta-D-xylan xylanohydrolase B;
DE   Flags: Precursor;
GN   Name=xynB; Synonyms=xyn10B; OrderedLocusNames=CJA_3280;
OS   Cellvibrio japonicus (strain Ueda107) (Pseudomonas fluorescens subsp.
OS   cellulosa).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Cellvibrionales;
OC   Cellvibrionaceae; Cellvibrio.
OX   NCBI_TaxID=498211;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 38-46.
RX   PubMed=2125205; DOI=10.1042/bj2720369;
RA   Kellett L.E., Poole D.M., Ferreira L.M.A., Durrant A.J., Hazlewood G.P.,
RA   Gilbert H.J.;
RT   "Xylanase B and an arabinofuranosidase from Pseudomonas fluorescens subsp.
RT   cellulosa contain identical cellulose-binding domains and are encoded by
RT   adjacent genes.";
RL   Biochem. J. 272:369-376(1990).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Ueda107;
RX   PubMed=18556790; DOI=10.1128/jb.01701-07;
RA   DeBoy R.T., Mongodin E.F., Fouts D.E., Tailford L.E., Khouri H.,
RA   Emerson J.B., Mohamoud Y., Watkins K., Henrissat B., Gilbert H.J.,
RA   Nelson K.E.;
RT   "Insights into plant cell wall degradation from the genome sequence of the
RT   soil bacterium Cellvibrio japonicus.";
RL   J. Bacteriol. 190:5455-5463(2008).
CC   -!- FUNCTION: Xylanase B contributes to hydrolyze hemicellulose, the major
CC       component of plant cell-walls.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Endohydrolysis of (1->4)-beta-D-xylosidic linkages in xylans.;
CC         EC=3.2.1.8;
CC   -!- PATHWAY: Glycan metabolism; hemicellulose degradation.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 10 (cellulase F) family.
CC       {ECO:0000305}.
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DR   EMBL; X54523; CAA38389.1; -; Genomic_DNA.
DR   EMBL; CP000934; ACE84499.1; -; Genomic_DNA.
DR   RefSeq; WP_012488856.1; NC_010995.1.
DR   AlphaFoldDB; P23030; -.
DR   SMR; P23030; -.
DR   STRING; 498211.CJA_3280; -.
DR   CAZy; CBM2; Carbohydrate-Binding Module Family 2.
DR   CAZy; CBM35; Carbohydrate-Binding Module Family 35.
DR   CAZy; GH10; Glycoside Hydrolase Family 10.
DR   PRIDE; P23030; -.
DR   EnsemblBacteria; ACE84499; ACE84499; CJA_3280.
DR   KEGG; cja:CJA_3280; -.
DR   eggNOG; COG3693; Bacteria.
DR   HOGENOM; CLU_029617_0_0_6; -.
DR   OrthoDB; 593041at2; -.
DR   UniPathway; UPA00697; -.
DR   Proteomes; UP000001036; Chromosome.
DR   GO; GO:0031176; F:endo-1,4-beta-xylanase activity; IEA:UniProtKB-EC.
DR   GO; GO:0030247; F:polysaccharide binding; IEA:InterPro.
DR   GO; GO:0030245; P:cellulose catabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0045493; P:xylan catabolic process; IEA:UniProtKB-KW.
DR   Gene3D; 2.60.40.290; -; 1.
DR   InterPro; IPR001919; CBD2.
DR   InterPro; IPR008965; CBM2/CBM3_carb-bd_dom_sf.
DR   InterPro; IPR012291; CBM2_carb-bd_dom_sf.
DR   InterPro; IPR018366; CBM2_CS.
DR   InterPro; IPR005084; CMB_fam6.
DR   InterPro; IPR008979; Galactose-bd-like_sf.
DR   InterPro; IPR044846; GH10.
DR   InterPro; IPR031158; GH10_AS.
DR   InterPro; IPR001000; GH10_dom.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   PANTHER; PTHR31490; PTHR31490; 1.
DR   Pfam; PF00553; CBM_2; 1.
DR   Pfam; PF03422; CBM_6; 1.
DR   Pfam; PF00331; Glyco_hydro_10; 1.
DR   PRINTS; PR00134; GLHYDRLASE10.
DR   SMART; SM00637; CBD_II; 1.
DR   SMART; SM00633; Glyco_10; 1.
DR   SUPFAM; SSF49384; SSF49384; 1.
DR   SUPFAM; SSF49785; SSF49785; 1.
DR   SUPFAM; SSF51445; SSF51445; 1.
DR   PROSITE; PS51173; CBM2; 1.
DR   PROSITE; PS00561; CBM2_A; 1.
DR   PROSITE; PS51175; CBM6; 1.
DR   PROSITE; PS00591; GH10_1; 1.
DR   PROSITE; PS51760; GH10_2; 1.
PE   1: Evidence at protein level;
KW   Carbohydrate metabolism; Cellulose degradation; Direct protein sequencing;
KW   Disulfide bond; Glycosidase; Hydrolase; Polysaccharide degradation;
KW   Reference proteome; Signal; Xylan degradation.
FT   SIGNAL          1..37
FT                   /evidence="ECO:0000269|PubMed:2125205"
FT   CHAIN           38..599
FT                   /note="Endo-1,4-beta-xylanase B"
FT                   /id="PRO_0000007978"
FT   DOMAIN          38..136
FT                   /note="CBM2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01135"
FT   DOMAIN          163..289
FT                   /note="CBM6"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00523"
FT   DOMAIN          315..595
FT                   /note="GH10"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01096"
FT   ACT_SITE        431
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        530
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10061"
FT   DISULFID        39..133
FT                   /evidence="ECO:0000250"
FT   CONFLICT        563..598
FT                   /note="LWGYVVGRTWIEGSGLIQDNGTPRPAMTWLINNYLN -> SGICGGQDLDRR
FT                   LRFDPGQWHTAPGNDVVD (in Ref. 1; CAA38389)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   599 AA;  64363 MW;  D2DE51E5FD4B33E5 CRC64;
     MTISASDYRH PGNFLKRTTA LLCVGTALTA LAFNASAACT YTIDSEWSTG FTANITLKND
     TGAAINNWNV NWQYSSNRMT SGWNANFSGT NPYNATNMSW NGSIAPGQSI SFGLQGEKNG
     STAERPTVTG AACNSATTSS VASSSSTPTT SSSSASSVAS ALLLQEAQAG FCRVDGTIDN
     NHTGFTGSGF ANTNNAQGAA VVWAIDATSS GRRTLTIRYA NGGTANRNGS LVINGGSNGN
     YTVSLPTTGA WTTWQTATID VDLVQGNNIV QLSATTAEGL PNIDSLSVVG GTVRAGNCGS
     VSSSSSVQSS SSSSSSSAAS AKKFIGNITT SGAVRSDFTR YWNQITPENE SKWGSVEGTR
     NVYNWAPLDR IYAYARQNNI PVKAHTFVWG AQSPSWLNNL SGPEVAVEIE QWIRDYCARY
     PDTAMIDVVN EAVPGHQPAG YAQRAFGNNW IQRVFQLARQ YCPNSILILN DYNNIRWQHN
     EFIALAKAQG NYIDAVGLQA HELKGMTAAQ VKTAIDNIWN QVGKPIYISE YDIGDTNDQV
     QLQNFQAHFP VFYNHPHVHG ITLWGYVVGR TWIEGSGLIQ DNGTPRPAMT WLINNYLNQ