ID   XYLA1_GEOSE             Reviewed;         705 AA.
AC   P45702;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   25-MAY-2022, entry version 70.
DE   RecName: Full=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;
GN   Name=xylA;
OS   Geobacillus stearothermophilus (Bacillus stearothermophilus).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Geobacillus.
OX   NCBI_TaxID=1422;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 2-7.
RC   STRAIN=No. 21;
RX   PubMed=8074507; DOI=10.1128/aem.60.7.2252-2258.1994;
RA   Baba T., Shinke R., Nanmori T.;
RT   "Identification and characterization of clustered genes for thermostable
RT   xylan-degrading enzymes, beta-xylosidase and xylanase, of Bacillus
RT   stearothermophilus 21.";
RL   Appl. Environ. Microbiol. 60:2252-2258(1994).
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   -!- PATHWAY: Glycan degradation; xylan degradation.
CC   -!- INDUCTION: By xylan and xylose.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 52 family. {ECO:0000305}.
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DR   EMBL; D28121; BAA05667.1; -; Genomic_DNA.
DR   PIR; I39759; I39759.
DR   AlphaFoldDB; P45702; -.
DR   SMR; P45702; -.
DR   CAZy; GH52; Glycoside Hydrolase Family 52.
DR   UniPathway; UPA00114; -.
DR   GO; GO:0009044; F:xylan 1,4-beta-xylosidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0045493; P:xylan catabolic process; IEA:UniProtKB-UniPathway.
DR   Gene3D; 1.50.10.10; -; 1.
DR   InterPro; IPR008928; 6-hairpin_glycosidase_sf.
DR   InterPro; IPR012341; 6hp_glycosidase-like_sf.
DR   InterPro; IPR000852; Glyco_hydro_52.
DR   Pfam; PF03512; Glyco_hydro_52; 1.
DR   PRINTS; PR00845; GLHYDRLASE52.
DR   SUPFAM; SSF48208; SSF48208; 1.
PE   1: Evidence at protein level;
KW   Carbohydrate metabolism; Direct protein sequencing; Glycosidase; Hydrolase;
KW   Polysaccharide degradation; Xylan degradation.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|PubMed:8074507"
FT   CHAIN           2..705
FT                   /note="Beta-xylosidase"
FT                   /id="PRO_0000012218"
SQ   SEQUENCE   705 AA;  79835 MW;  AE3BFF272C08CFB2 CRC64;
     MPTNLFFNAH HSPVGAFASF TLGFPGKSGG LDLELARPPR QNVLIGVESL HESGLYHVLP
     FLETAEEDES KRYDIENPDP NPQKPNILIP FAKEEIQREF HVATDTWKAG DLTFTIYSPV
     KAVPNPETAD EEELKLALVP AVIVEMTIDN TNGTRARRAF FGFEGTDPYT SMRRIDDTCP
     QLRGVGQGRI LSIVSKDEGV RSALHFSMED ILTAQLEENW TFGLGKVGAL IVDVPAGEKK
     TYQFAVCFYR GGYVTAGMDA SYFYTRFFQN IEEVGLYALE QAEVLKEQSF RSNKLIEKEW
     LSDDQTFMMA HAIRSYYGNT QLLEHEGKPI WVVNEGEYRM MNTFDLTVDQ LFFELKLNPW
     TVKNVLDLYV ERYSYEDRVR FPGEETEYPS GISFTHDMGV ANTFSRPHYS SYELYGISGC
     FSHMTHEQLV NWVLCAAVYI EQTKDWAWRD KRLAILEQCL ESMVRRDHPD PEQRNGVMGL
     DSTRTMGGAE ITTYDSLDVS LGQARNNLYL AGKCWAAYVA LEKLFRDVGK EELAALAGEQ
     AEKCAATIVS HVTDDGYIPA IMGEGNDSKI IPAIEGLVFP YFTNCHEALD ENGRFGAYIQ
     ALRNHLQYVL REGICLFPDG GWKISSTSNN SWLSKIYLCQ FIARHILGWE WDEQGKRADA
     AHVAWLTHPT LSIWSWSDQI IAGEITGSKY YPRGVTSILW LEEGE