Reviewed, UniProtKB/Swiss-Prot P07129 (XYNB_BACPU)

Names and origin

Protein names

Recommended name:
    Beta-xylosidase
    EC=3.2.1.37
Alternative name(s):
    1,4-beta-D-xylan xylohydrolase
    Xylan 1,4-beta-xylosidase

Gene names

Name:

xynB

Organism

Bacillus pumilus (Bacillus mesentericus)

Taxonomic identifier

1408 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Bacillales › Bacillaceae › Bacillus

Protein attributes

Sequence length	535 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Beta-xylosidase is an intracellular xylan-degrading enzyme.
Catalytic activity	Hydrolysis of (1->4)-beta-D-xylans, to remove successive D-xylose residues from the non-reducing termini.
Subunit structure	Oligomer; homotetramer or homotrimer.
Sequence similarities	Belongs to the glycosyl hydrolase 43 family.
Sequence caution	The sequence CAA29235.1 differs from that shown. Reason: Miscellaneous discrepancy.

Ontologies

Keywords
Biological process	Xylan degradation
Molecular function	Glycosidase Hydrolase
Technical term	Direct protein sequencing
Gene Ontology (GO)
Biological process	xylan catabolic process Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	xylan 1,4-beta-xylosidase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 535	535	Beta-xylosidase		PRO_0000057692

Sequences

	Sequence		Length	Mass (Da)
	P07129-1 [UniParc]. Last modified February 1, 1994. Version 2. Checksum: 5D8CA8F9D85592D8	FASTA	535	61,190
	10 20 30 40 50 60 MKITNPVLKG FNPDPSICRA GEDYYMAVST FEWFPGVQIY HSKDLIHWRL AARPLQKTSQ 70 80 90 100 110 120 LDMKGNPDSG GVWAPCLSYA DGQFWLIYSD IKVVDGPFKD GHNYLVTADA VDGEWSDPVR 130 140 150 160 170 180 LNSSGFDPSL FHDPSGKKYV LNMLWDHREK HHSFAGIALQ EYSVSEKKLV GERKVIFKGT 190 200 210 220 230 240 PIKLTEAPHL YYINDVYYLL TAEGGTRYEH AATIARSSRI DGPYEVHPDN PILTAFHAPS 250 260 270 280 290 300 HPLQKCGHAS IVQTHTNEWY LAHLTGRPIH SSKESIFQQR GWCPLGRETA IQKLEWKDGW 310 320 330 340 350 360 PYVVGGKEGL LEVEAPAMSV KEFSPTYHIV DEFKDSSLNR HFQTLRIPFT DQIGSVTENP 370 380 390 400 410 420 HHLRLYGQES LTSKFTQAFV ARRWQSFYFE AETAVSFFPK NFQQAAGLVN YYNTENWTAL 430 440 450 460 470 480 QVTYDDALGR ILELSVCENL AFSQPLIKKI IIPDEIPYVY LKVTVQRETY TYSYSFDQQE 490 500 510 520 530 WEKIDVPLES THLSDDFIRG GGFFTGAFVG MQCQDTSGER LPADFKYFRY EETTE

References

[1]	"Structure and expression of genes coding for xylan-degrading enzymes of Bacillus pumilus." Moriyama H., Fukusaki E., Cabrera-Crespo J., Shinmoy A., Okada H. Eur. J. Biochem. 166:539-545(1987) [PubMed: 2440680] [Abstract] Cited for: PRELIMINARY NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: IPO.
[2]	"Sequence and properties of beta-xylosidase from Bacillus pumilus IPO. Contradiction of the previous nucleotide sequence." Xu W.-Z., Shima Y., Negoro S., Urabe I. Eur. J. Biochem. 202:1197-1203(1991) [PubMed: 1765080] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-5. Strain: IPO.

Cross-references

Sequence databases
EMBLGenBankDDBJ	X05793 Genomic DNA. Translation: CAA29235.1. Sequence problems.
PIR	S00067. S19729.
3D structure databases
ModBase	Search...
Protein family/group databases
CAZy	GH43. Glycoside Hydrolase Family 43.
Enzyme and pathway databases
BRENDA	3.2.1.37. 1189.
Family and domain databases
InterPro	IPR013320. ConA-like_subgrp. IPR006710. Glyco_hydro_43. [Graphical view]
Gene3D	G3DSA:2.60.120.200. ConA_like_subgrp. 1 hit.
PANTHER	PTHR22925. Glyco_hydro_43. 1 hit.
Pfam	PF04616. Glyco_hydro_43. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

XYNB_BACPU

Accession

Primary (citable) accession number: P07129

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 1, 1988
Last sequence update:	February 1, 1994
Last modified:	June 16, 2009
This is version 53 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)