ID   XYLO_PRERU              Reviewed;         518 AA.
AC   Q9WXE8;
DT   23-MAR-2010, integrated into UniProtKB/Swiss-Prot.
DT   23-MAR-2010, sequence version 2.
DT   12-AUG-2020, entry version 52.
DE   RecName: Full=Putative beta-xylosidase;
DE            EC=3.2.1.37;
DE   AltName: Full=1,4-beta-D-xylan xylohydrolase;
DE   AltName: Full=Xylan 1,4-beta-xylosidase;
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=T31;
RA   Ogata K., Aminov R.I., Nagamine T., Matsui H., Tajima K., Nakamura M.,
RA   Benno Y.;
RT   "A Prevotella ruminicola T31 operon encoding xylosidase and
RT   galacturonase.";
RL   Submitted (JAN-1999) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   IDENTIFICATION OF FRAMESHIFTS.
RX   PubMed=11093261;
RX   DOI=10.1002/1097-0134(20010101)42:1<66::aid-prot70>3.0.co;2-4;
RA   Naumoff D.G.;
RT   "beta-fructosidase superfamily: homology with some alpha-L-arabinases and
RT   beta-D-xylosidases.";
RL   Proteins 42:66-76(2001).
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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAA78558.1; Type=Frameshift; Evidence={ECO:0000305};
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DR   EMBL; AB022865; BAA78558.1; ALT_FRAME; Genomic_DNA.
DR   CAZy; GH43; Glycoside Hydrolase Family 43.
DR   GO; GO:0009044; F:xylan 1,4-beta-xylosidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-KW.
DR   Gene3D; 2.115.10.20; -; 1.
DR   InterPro; IPR013320; ConA-like_dom_sf.
DR   InterPro; IPR041542; GH43_C2.
DR   InterPro; IPR006710; Glyco_hydro_43.
DR   InterPro; IPR023296; Glyco_hydro_beta-prop_sf.
DR   Pfam; PF17851; GH43_C2; 1.
DR   Pfam; PF04616; Glyco_hydro_43; 1.
DR   SUPFAM; SSF49899; SSF49899; 1.
DR   SUPFAM; SSF75005; SSF75005; 1.
PE   3: Inferred from homology;
KW   Carbohydrate metabolism; Glycosidase; Hydrolase.
FT   CHAIN           1..518
FT                   /note="Putative beta-xylosidase"
FT                   /id="PRO_0000393239"
FT   ACT_SITE        47
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:A7LXU0"
FT   ACT_SITE        203
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250|UniProtKB:A7LXU0"
FT   SITE            154
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:A7LXU0"
SQ   SEQUENCE   518 AA;  58322 MW;  97AF5900486A8E9E CRC64;
     MHHARNVQFS NIHVSTVDED VRPDFVEVDT KGWGDQGDGT YRNPXSDPDV IRVGNKXYMV
     ASDFHXMGMQ VLESDDMVXW RYISQIYRRF NEPGWDANLH YAGGSWAPSI RYHSGLFYVY
     FCTPDEGLYM STASNPAGPW APLHLVKRVA KWEDPCPFWD EDGQAYIGRS QHGAGPIIVH
     RMSADGKTLL DEGKTVYEGP IAEGTKFMKR NGWYYLIIPE GGVGTGWQTV LRARNIYGPY
     ERRIVLEQGS TGVNGPHQGA LVDAPDGSWW FYHFQETPVL GRVVHLQPAR WEADWPVIGV
     DYDKNGIGEP VATWKKPVSS VGTAGFQTCD DSNDALGLHW QWNHNPVDTH WNLTDRKGWL
     TLKAMPADSL KMVRNMLTQK VVGYQSESTT KVSIKGDSYA GLFCSGKLFC GVGLCKDGVF
     IEFGGQRKII DKGSYQEVWF KVTNDCEQNR HLFYYSIDGE HYQPAGSAFA MSGGYWKGIR
     VGCLTTFLQA KRLLRARHLR MLNSTISIKN SPNSLADC