ID   XYNB_PRERU              Reviewed;         319 AA.
AC   P48791;
DT   01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1996, sequence version 1.
DT   25-MAY-2022, entry version 57.
DE   RecName: Full=Beta-xylosidase;
DE            EC=3.2.1.37;
DE   AltName: Full=1,4-beta-D-xylan xylohydrolase;
DE   AltName: Full=Exo-beta-(1,4)-xylanase;
DE   AltName: Full=Xylan 1,4-beta-xylosidase;
GN   Name=xynB;
OS   Prevotella ruminicola (Bacteroides ruminicola).
OC   Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Prevotellaceae;
OC   Prevotella.
OX   NCBI_TaxID=839;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=B14;
RX   PubMed=7487028; DOI=10.1128/aem.61.8.2958-2964.1995;
RA   Gasparic A., Martin J., Daniel A.S., Flint H.J.;
RT   "A xylan hydrolase gene cluster in Prevotella ruminicola B(1)4: sequence
RT   relationships, synergistic interactions, and oxygen sensitivity of a novel
RT   enzyme with exoxylanase and beta-(1,4)-xylosidase activities.";
RL   Appl. Environ. Microbiol. 61:2958-2964(1995).
CC   -!- FUNCTION: Exoxylanase capable of acting on certain xylans and
CC       xylooligosaccharides.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Hydrolysis of (1->4)-beta-D-xylans, to remove successive D-
CC         xylose residues from the non-reducing termini.; EC=3.2.1.37;
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 43 family. {ECO:0000305}.
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DR   EMBL; Z49241; CAA89208.1; -; Genomic_DNA.
DR   AlphaFoldDB; P48791; -.
DR   SMR; P48791; -.
DR   CAZy; GH43; Glycoside Hydrolase Family 43.
DR   GO; GO:0009044; F:xylan 1,4-beta-xylosidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0045493; P:xylan catabolic process; IEA:UniProtKB-KW.
DR   Gene3D; 2.115.10.20; -; 1.
DR   InterPro; IPR006710; Glyco_hydro_43.
DR   InterPro; IPR023296; Glyco_hydro_beta-prop_sf.
DR   Pfam; PF04616; Glyco_hydro_43; 1.
DR   SUPFAM; SSF75005; SSF75005; 1.
PE   3: Inferred from homology;
KW   Carbohydrate metabolism; Glycosidase; Hydrolase; Multifunctional enzyme;
KW   Polysaccharide degradation; Xylan degradation.
FT   CHAIN           1..319
FT                   /note="Beta-xylosidase"
FT                   /id="PRO_0000057696"
FT   ACT_SITE        14
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:Q45071"
FT   ACT_SITE        222
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250|UniProtKB:Q45071"
FT   SITE            136
FT                   /note="Important for catalytic activity, responsible for
FT                   pKa modulation of the active site Glu and correct
FT                   orientation of both the proton donor and substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q45071"
SQ   SEQUENCE   319 AA;  36407 MW;  6C170659F2C81E92 CRC64;
     MKAKYVFPSD YMADPAANVF DGKLYIYPSH DYDSGECFDD DGGHFQMKDY HVLCIDGDPM
     EQDAKDCGKQ FGIEDIPWVE KQLWDNDCVE KDGKYYLIYS AKDYTGVFHL GVAVADKPEG
     PFVPEADPIR GSYSIDPCVF KDDDGEIYVY FGGIWGGQLQ WYKDNKMLKA EHLPEGKEDP
     LPSRVARMTG DVKQFAEAPR AVIIVDETGK PLPADDPHRF FEASWMHKYN GKYYFSYSTG
     DTHLLCYAVG DNPYGPFTYQ GVILEPVVGW TTHHSIVEYK GKWYLFHHDC VPSNDTTWLR
     SLKVAELEYD AEGHIKTVK