XYLA_THEST
ID XYLA_THEST Reviewed; 473 AA.
AC P48790;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 1.
DT 25-MAY-2022, entry version 68.
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=xylA;
OS Thermoclostridium stercorarium (Clostridium stercorarium).
OC Bacteria; Firmicutes; Clostridia; Eubacteriales; Oscillospiraceae;
OC Thermoclostridium.
OX NCBI_TaxID=1510;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PARTIAL PROTEIN SEQUENCE.
RX PubMed=7763495; DOI=10.1271/bbb.57.268;
RA Sakka K., Yoshikawa K., Kojima Y., Karita S., Ohmiya K., Shimada K.;
RT "Nucleotide sequence of the Clostridium stercorarium xylA gene encoding a
RT bifunctional protein with beta-D-xylosidase and alpha-L-arabinofuranosidase
RT activities, and properties of the translated product.";
RL Biosci. Biotechnol. Biochem. 57:268-272(1993).
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 -!- SUBUNIT: Homotetramer.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 43 family. {ECO:0000305}.
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DR EMBL; D13268; BAA02527.1; -; Genomic_DNA.
DR PIR; JQ1936; JQ1936.
DR AlphaFoldDB; P48790; -.
DR SMR; P48790; -.
DR CAZy; GH43; Glycoside Hydrolase Family 43.
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 1: Evidence at protein level;
KW Carbohydrate metabolism; Direct protein sequencing; Glycosidase; Hydrolase;
KW Multifunctional enzyme; Polysaccharide degradation; Xylan degradation.
FT CHAIN 1..473
FT /note="Xylosidase/arabinosidase"
FT /id="PRO_0000057695"
FT ACT_SITE 18
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:Q45071"
FT ACT_SITE 209
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:Q45071"
FT SITE 144
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 473 AA; 53341 MW; CDA34CE9DEBB2399 CRC64;
MRKQRFNPYL PSWEYIPDAE PYVFNGRVYI YGSHDRFNGH AFCLNDYVCW SAPVDDLSEW
RYEGVIYRKT DDPLNPDGRM CLYAPDVTLG PDGRYYLYYV LDKVPVVSVA VCDTPAGKYE
FYGYVRYADG TRLGEREGDW PQFDPAVLTE GERTYLYTGF CPKGDKSRKG AMATVLGPDM
LTVVEEPVII VPSEPYSRGS GFEGHEFFEA PSIRKKGDTY YFIYSSVVMH ELCYATSKHP
TKGFKYGGVI VSNCDLHIDS YKPAEKPMYY GGNNHGSIVE INGEWYIFYH RHTNGTSFSR
QGCMEKIKIL EDGSIPQVEM TSCGSADEPL PGRGEYPAYI ACNLFCGEES VYTDLTGAWM
NNQFPKITQD GKDGDEEPGY IANMKDSATA GFKYFDCKGI KSVKIKVRGY CRGVFEVKTS
WNGEVLGKIP VEFSNIWTEF SASIPIPDGI HALYFTYRGS GSASLKSFTL CTD
