XYLB_BUTFI
ID XYLB_BUTFI Reviewed; 517 AA.
AC P45982;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 25-MAY-2022, entry version 74.
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=xylB;
OS Butyrivibrio fibrisolvens.
OC Bacteria; Firmicutes; Clostridia; Eubacteriales; Lachnospiraceae;
OC Butyrivibrio.
OX NCBI_TaxID=831;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1905520; DOI=10.1128/aem.57.4.1227-1234.1991;
RA Utt E.A., Eddy C.K., Keshav K.F., Ingram L.O.;
RT "Sequencing and expression of the Butyrivibrio fibrisolvens xylB gene
RT encoding a novel bifunctional protein with beta-D-xylosidase and alpha-L-
RT arabinofuranosidase activities.";
RL Appl. Environ. Microbiol. 57:1227-1234(1991).
CC -!- FUNCTION: Has a 1.6-fold higher activity as an arabinosidase than as a
CC beta-xylosidase when tested on the substrates nitrophenyl-beta-D-
CC xylopyranoside and P-nitrophenyl-alpha-L-arabinofuranoside.
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 -!- SIMILARITY: Belongs to the glycosyl hydrolase 43 family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; M55537; AAA63610.1; -; Genomic_DNA.
DR PIR; A49776; A49776.
DR AlphaFoldDB; P45982; -.
DR SMR; P45982; -.
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; 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; Multifunctional enzyme;
KW Polysaccharide degradation; Xylan degradation.
FT CHAIN 1..517
FT /note="Xylosidase/arabinosidase"
FT /id="PRO_0000057694"
FT ACT_SITE 15
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:A7LXU0"
FT ACT_SITE 185
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:A7LXU0"
FT SITE 123
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 517 AA; 58222 MW; F1B645F76F6FE0B5 CRC64;
MVIANNPILK GFYPDPSICR KGDDFYLVCS SFVYAPGVPI FHTKDLAHFE QIGNILDRES
QLPLSGDISR GIFAPTIREH NGIFYMITTN VSSGGNFIVT AKDPAGPWSE PYYLGEDEAP
GIDPSLFFDD DGKCYYVGTR PNPDGVRYNG DWEIWVQELD LEQMKLVGPS MAIWKGALKD
VIWPEGPHLY KKDGYYYLLH AEAGTSFEHA ISVARSKELF KWFEGCPRNP IFTHRNLGKD
YPVCNVGHAD LVDDINGNWY MVMLASRPCK GKCSLGRETF LAKVIWEDGW PVVNPGVGRL
TDEVEMDLPE YRFSKEITTK DKMTFEETVL DDRFVGIERR SEDFYSLTDN PGFLRLKLRP
EAIENTGNPS YLGIRQKTHS FRASCGLKFT PAKDNECAGM VLFQNNENHL ELLVVKKKDK
LQFKVGPVIK GTKIRLATFD ISSGDLEIIL EAANQLANIY IKKNNEKILV AECIDLSPYT
TEESGGFVGC TIGLYASSNG KTSDNYCDYS YFTVEEV
