Reviewed, UniProtKB/Swiss-Prot P45702 (XYLA1_BACST)

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:

xylA

Organism

Bacillus stearothermophilus (Geobacillus stearothermophilus)

Taxonomic identifier

1422 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Bacillales › Bacillaceae › Geobacillus

Protein attributes

Sequence length	705 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

General annotation (Comments)

Catalytic activity	Hydrolysis of (1->4)-beta-D-xylans, to remove successive D-xylose residues from the non-reducing termini.
Pathway	Glycan degradation; xylan degradation.
Subcellular location	Secreted.
Induction	By xylan and xylose.
Sequence similarities	Belongs to the glycosyl hydrolase 52 family.

Ontologies

Keywords
Biological process	Xylan degradation
Cellular component	Secreted
Domain	Signal
Molecular function	Glycosidase Hydrolase
Technical term	Direct protein sequencing
Gene Ontology (GO)
Biological process	xylan catabolic process Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	extracellular region Inferred from electronic annotation. Source: UniProtKB-SubCell
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
	Signal peptide	1 – 18	18	Potential
	Chain	19 – 705	687	Beta-xylosidase		PRO_0000012218

Sequences

	Sequence		Length	Mass (Da)
	P45702-1 [UniParc]. Last modified November 1, 1995. Version 1. Checksum: AE3BFF272C08CFB2	FASTA	705	79,835
	10 20 30 40 50 60 MPTNLFFNAH HSPVGAFASF TLGFPGKSGG LDLELARPPR QNVLIGVESL HESGLYHVLP 70 80 90 100 110 120 FLETAEEDES KRYDIENPDP NPQKPNILIP FAKEEIQREF HVATDTWKAG DLTFTIYSPV 130 140 150 160 170 180 KAVPNPETAD EEELKLALVP AVIVEMTIDN TNGTRARRAF FGFEGTDPYT SMRRIDDTCP 190 200 210 220 230 240 QLRGVGQGRI LSIVSKDEGV RSALHFSMED ILTAQLEENW TFGLGKVGAL IVDVPAGEKK 250 260 270 280 290 300 TYQFAVCFYR GGYVTAGMDA SYFYTRFFQN IEEVGLYALE QAEVLKEQSF RSNKLIEKEW 310 320 330 340 350 360 LSDDQTFMMA HAIRSYYGNT QLLEHEGKPI WVVNEGEYRM MNTFDLTVDQ LFFELKLNPW 370 380 390 400 410 420 TVKNVLDLYV ERYSYEDRVR FPGEETEYPS GISFTHDMGV ANTFSRPHYS SYELYGISGC 430 440 450 460 470 480 FSHMTHEQLV NWVLCAAVYI EQTKDWAWRD KRLAILEQCL ESMVRRDHPD PEQRNGVMGL 490 500 510 520 530 540 DSTRTMGGAE ITTYDSLDVS LGQARNNLYL AGKCWAAYVA LEKLFRDVGK EELAALAGEQ 550 560 570 580 590 600 AEKCAATIVS HVTDDGYIPA IMGEGNDSKI IPAIEGLVFP YFTNCHEALD ENGRFGAYIQ 610 620 630 640 650 660 ALRNHLQYVL REGICLFPDG GWKISSTSNN SWLSKIYLCQ FIARHILGWE WDEQGKRADA 670 680 690 700 AHVAWLTHPT LSIWSWSDQI IAGEITGSKY YPRGVTSILW LEEGE

References

[1]

"Identification and characterization of clustered genes for thermostable xylan-degrading enzymes, beta-xylosidase and xylanase, of Bacillus stearothermophilus 21." Baba T., Shinke R., Nanmori T. Appl. Environ. Microbiol. 60:2252-2258(1994) [PubMed: 8074507] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 2-7. Strain: No. 21.

Cross-references

Sequence databases
EMBLGenBankDDBJ	D28121 Genomic DNA. Translation: BAA05667.1.
PIR	I39759.
3D structure databases
ModBase	Search...
Protein family/group databases
CAZy	GH52. Glycoside Hydrolase Family 52.
Enzyme and pathway databases
BRENDA	3.2.1.37. 266715.
Family and domain databases
InterPro	IPR000852. Glyco_hydro_52. [Graphical view]
Pfam	PF03512. Glyco_hydro_52. 1 hit. [Graphical view]
PRINTS	PR00845. GLHYDRLASE52.
ProtoNet	Search...

Entry information

Entry name

XYLA1_BACST

Accession

Primary (citable) accession number: P45702

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1995
Last sequence update:	November 1, 1995
Last modified:	June 16, 2009
This is version 49 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

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