ID   XYLB_BACOV              Reviewed;         325 AA.
AC   P49943;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   27-MAR-2024, entry version 79.
DE   RecName: Full=Xylosidase/arabinosidase;
DE   Includes:
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;
DE   Includes:
DE     RecName: Full=Alpha-L-arabinofuranosidase;
DE              Short=Arabinosidase;
DE              EC=3.2.1.55;
GN   Name=xsa;
OS   Bacteroides ovatus.
OC   Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC   Bacteroides.
OX   NCBI_TaxID=28116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=V975;
RX   PubMed=7766665; DOI=10.1016/0304-4165(95)00051-c;
RA   Whitehead T.R.;
RT   "Nucleotide sequences of xylan-inducible xylanase and
RT   xylosidase/arabinosidase genes from Bacteroides ovatus V975.";
RL   Biochim. Biophys. Acta 1244:239-241(1995).
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   -!- CATALYTIC ACTIVITY:
CC       Reaction=Hydrolysis of terminal non-reducing alpha-L-arabinofuranoside
CC         residues in alpha-L-arabinosides.; EC=3.2.1.55;
CC   -!- INDUCTION: By xylan.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 43 family. {ECO:0000305}.
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DR   EMBL; U04957; AAB08024.1; -; Genomic_DNA.
DR   PIR; S55893; S55893.
DR   RefSeq; WP_004300838.1; NZ_WTXO01000021.1.
DR   AlphaFoldDB; P49943; -.
DR   SMR; P49943; -.
DR   STRING; 28116.Bovatus_01724; -.
DR   CAZy; GH43; Glycoside Hydrolase Family 43.
DR   GeneID; 29454815; -.
DR   GO; GO:0046556; F:alpha-L-arabinofuranosidase activity; IEA:UniProtKB-EC.
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   CDD; cd18619; GH43_CoXyl43_like; 1.
DR   InterPro; IPR006710; Glyco_hydro_43.
DR   InterPro; IPR023296; Glyco_hydro_beta-prop_sf.
DR   PANTHER; PTHR43772:SF2; BETA-1,4-XYLOSIDASE (EUROFUNG); 1.
DR   PANTHER; PTHR43772; ENDO-1,4-BETA-XYLANASE; 1.
DR   Pfam; PF04616; Glyco_hydro_43; 1.
DR   SUPFAM; SSF75005; Arabinanase/levansucrase/invertase; 1.
PE   2: Evidence at transcript level;
KW   Carbohydrate metabolism; Glycosidase; Hydrolase; Multifunctional enzyme;
KW   Polysaccharide degradation; Xylan degradation.
FT   CHAIN           1..325
FT                   /note="Xylosidase/arabinosidase"
FT                   /id="PRO_0000057693"
FT   ACT_SITE        16
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:Q45071"
FT   ACT_SITE        224
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250|UniProtKB:Q45071"
FT   SITE            137
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   325 AA;  37246 MW;  D54AEB7B62EAB2BE CRC64;
     MKTEKRYLVP GDYMADPAVH VFDGKLYIYP SHDWESGIAE NDNGDHFNMK DYHVYSMDDV
     MNGEIKDHGV VLSTEDIPWA GRQLWDCDVV CKDGKYYMYF PLKDQNDIFR IGVAVSDKPY
     GPFIPEANPM KGSYSIDPAV WDDGDGNYYI YFGGLWGGQL QRYRNNKALE SAILPEGEEE
     AIPSRVARLS EDMMEFAEEP RAVVILDEDG KPLTAGDTER RFFEASWMHK YNGKYYFSYS
     TGDTHLLCYA TGDNPYGPFT YQGVILTPVV GWTTHHAIVE FKGKWYLFHH DCVPSEGKTW
     LRSLKVCELQ YDADGRIITI EGKDE
//