XYNB_BACPU
ID XYNB_BACPU Reviewed; 535 AA.
AC P07129;
DT 01-APR-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1994, sequence version 2.
DT 25-MAY-2022, entry version 87.
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=xynB;
OS Bacillus pumilus (Bacillus mesentericus).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=1408;
RN [1]
RP PRELIMINARY NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=IPO;
RX PubMed=2440680; DOI=10.1111/j.1432-1033.1987.tb13547.x;
RA Moriyama H., Fukusaki E., Cabrera-Crespo J., Shinmoy A., Okada H.;
RT "Structure and expression of genes coding for xylan-degrading enzymes of
RT Bacillus pumilus.";
RL Eur. J. Biochem. 166:539-545(1987).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 1-5.
RC STRAIN=IPO;
RX PubMed=1765080; DOI=10.1111/j.1432-1033.1991.tb16490.x;
RA Xu W.-Z., Shima Y., Negoro S., Urabe I.;
RT "Sequence and properties of beta-xylosidase from Bacillus pumilus IPO.
RT Contradiction of the previous nucleotide sequence.";
RL Eur. J. Biochem. 202:1197-1203(1991).
CC -!- FUNCTION: Beta-xylosidase is an intracellular xylan-degrading enzyme.
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 -!- SUBUNIT: Oligomer; homotetramer or homotrimer.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 43 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA29235.1; Type=Miscellaneous discrepancy; Evidence={ECO:0000305};
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DR EMBL; X05793; CAA29235.1; ALT_SEQ; Genomic_DNA.
DR PIR; S00067; S00067.
DR PIR; S19729; S19729.
DR PDB; 5ZQJ; X-ray; 1.73 A; A/B=1-535.
DR PDB; 5ZQS; X-ray; 1.78 A; A/B=1-535.
DR PDB; 5ZQX; X-ray; 2.00 A; A/B/C/D=1-535.
DR PDBsum; 5ZQJ; -.
DR PDBsum; 5ZQS; -.
DR PDBsum; 5ZQX; -.
DR AlphaFoldDB; P07129; -.
DR SMR; P07129; -.
DR CAZy; GH43; Glycoside Hydrolase Family 43.
DR BRENDA; 3.2.1.37; 673.
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 1: Evidence at protein level;
KW 3D-structure; Carbohydrate metabolism; Direct protein sequencing;
KW Glycosidase; Hydrolase; Polysaccharide degradation; Xylan degradation.
FT CHAIN 1..535
FT /note="Beta-xylosidase"
FT /id="PRO_0000057692"
FT ACT_SITE 14
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:A7LXU0"
FT ACT_SITE 186
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:A7LXU0"
FT SITE 127
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"
FT STRAND 3..5
FT /evidence="ECO:0007829|PDB:5ZQJ"
FT STRAND 16..20
FT /evidence="ECO:0007829|PDB:5ZQJ"
FT STRAND 23..28
FT /evidence="ECO:0007829|PDB:5ZQJ"
FT STRAND 33..36
FT /evidence="ECO:0007829|PDB:5ZQJ"
FT STRAND 38..46
FT /evidence="ECO:0007829|PDB:5ZQJ"
FT STRAND 49..52
FT /evidence="ECO:0007829|PDB:5ZQJ"
FT TURN 58..60
FT /evidence="ECO:0007829|PDB:5ZQJ"
FT STRAND 76..80
FT /evidence="ECO:0007829|PDB:5ZQJ"
FT STRAND 83..91
FT /evidence="ECO:0007829|PDB:5ZQJ"
FT STRAND 95..97
FT /evidence="ECO:0007829|PDB:5ZQJ"
FT STRAND 101..110
FT /evidence="ECO:0007829|PDB:5ZQJ"
FT STRAND 129..132
FT /evidence="ECO:0007829|PDB:5ZQJ"
FT STRAND 138..145
FT /evidence="ECO:0007829|PDB:5ZQJ"
FT STRAND 153..163
FT /evidence="ECO:0007829|PDB:5ZQJ"
FT TURN 164..167
FT /evidence="ECO:0007829|PDB:5ZQJ"
FT STRAND 174..177
FT /evidence="ECO:0007829|PDB:5ZQJ"
FT STRAND 186..193
FT /evidence="ECO:0007829|PDB:5ZQJ"
FT STRAND 196..204
FT /evidence="ECO:0007829|PDB:5ZQJ"
FT STRAND 211..219
FT /evidence="ECO:0007829|PDB:5ZQJ"
FT STRAND 232..234
FT /evidence="ECO:0007829|PDB:5ZQJ"
FT STRAND 242..253
FT /evidence="ECO:0007829|PDB:5ZQJ"
FT STRAND 259..266
FT /evidence="ECO:0007829|PDB:5ZQJ"
FT TURN 276..278
FT /evidence="ECO:0007829|PDB:5ZQJ"
FT STRAND 287..297
FT /evidence="ECO:0007829|PDB:5ZQJ"
FT STRAND 300..303
FT /evidence="ECO:0007829|PDB:5ZQJ"
FT STRAND 311..313
FT /evidence="ECO:0007829|PDB:5ZQJ"
FT STRAND 329..331
FT /evidence="ECO:0007829|PDB:5ZQJ"
FT STRAND 335..337
FT /evidence="ECO:0007829|PDB:5ZQJ"
FT STRAND 343..347
FT /evidence="ECO:0007829|PDB:5ZQJ"
FT TURN 351..353
FT /evidence="ECO:0007829|PDB:5ZQJ"
FT STRAND 354..356
FT /evidence="ECO:0007829|PDB:5ZQJ"
FT TURN 357..361
FT /evidence="ECO:0007829|PDB:5ZQJ"
FT STRAND 362..366
FT /evidence="ECO:0007829|PDB:5ZQJ"
FT STRAND 378..383
FT /evidence="ECO:0007829|PDB:5ZQJ"
FT STRAND 386..396
FT /evidence="ECO:0007829|PDB:5ZQJ"
FT STRAND 404..413
FT /evidence="ECO:0007829|PDB:5ZQJ"
FT STRAND 416..425
FT /evidence="ECO:0007829|PDB:5ZQJ"
FT TURN 426..428
FT /evidence="ECO:0007829|PDB:5ZQJ"
FT STRAND 429..438
FT /evidence="ECO:0007829|PDB:5ZQJ"
FT STRAND 441..443
FT /evidence="ECO:0007829|PDB:5ZQJ"
FT STRAND 459..466
FT /evidence="ECO:0007829|PDB:5ZQJ"
FT STRAND 469..480
FT /evidence="ECO:0007829|PDB:5ZQJ"
FT HELIX 490..493
FT /evidence="ECO:0007829|PDB:5ZQJ"
FT TURN 495..497
FT /evidence="ECO:0007829|PDB:5ZQJ"
FT STRAND 508..519
FT /evidence="ECO:0007829|PDB:5ZQJ"
FT STRAND 522..532
FT /evidence="ECO:0007829|PDB:5ZQJ"
SQ SEQUENCE 535 AA; 61190 MW; 5D8CA8F9D85592D8 CRC64;
MKITNPVLKG FNPDPSICRA GEDYYMAVST FEWFPGVQIY HSKDLIHWRL AARPLQKTSQ
LDMKGNPDSG GVWAPCLSYA DGQFWLIYSD IKVVDGPFKD GHNYLVTADA VDGEWSDPVR
LNSSGFDPSL FHDPSGKKYV LNMLWDHREK HHSFAGIALQ EYSVSEKKLV GERKVIFKGT
PIKLTEAPHL YYINDVYYLL TAEGGTRYEH AATIARSSRI DGPYEVHPDN PILTAFHAPS
HPLQKCGHAS IVQTHTNEWY LAHLTGRPIH SSKESIFQQR GWCPLGRETA IQKLEWKDGW
PYVVGGKEGL LEVEAPAMSV KEFSPTYHIV DEFKDSSLNR HFQTLRIPFT DQIGSVTENP
HHLRLYGQES LTSKFTQAFV ARRWQSFYFE AETAVSFFPK NFQQAAGLVN YYNTENWTAL
QVTYDDALGR ILELSVCENL AFSQPLIKKI IIPDEIPYVY LKVTVQRETY TYSYSFDQQE
WEKIDVPLES THLSDDFIRG GGFFTGAFVG MQCQDTSGER LPADFKYFRY EETTE
