XYLB_BACOV
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 25-MAY-2022, entry version 75.
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; Bacteroidetes; 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_UAQF01000004.1.
DR AlphaFoldDB; P49943; -.
DR SMR; P49943; -.
DR STRING; 28116.Bovatus_01724; -.
DR CAZy; GH43; Glycoside Hydrolase Family 43.
DR GeneID; 29454815; -.
DR OrthoDB; 386120at2; -.
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 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 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