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Reviewed, UniProtKB/Swiss-Prot Q9ZFM2 (XYNB_BACST)

Last modified January 19, 2010. Version 48. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein namesRecommended 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
OrganismBacillus stearothermophilus (Geobacillus stearothermophilus)
Taxonomic identifier1422 [NCBI]
Taxonomic lineageBacteria › Firmicutes › Bacillales › Bacillaceae › Geobacillus

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Protein attributes

Sequence length504 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level.

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General annotation (Comments)

Catalytic activity

Hydrolysis of (1->4)-beta-D-xylans, to remove successive D-xylose residues from the non-reducing termini.

Sequence similarities

Belongs to the glycosyl hydrolase 39 family.

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Ontologies

Keywords
   Biological processXylan degradation
   Molecular functionGlycosidase
Hydrolase
   Technical term3D-structure
Gene Ontology (GO)
   Biological processxylan catabolic process

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular functioncation binding

Inferred from electronic annotation. Source: InterPro

xylan 1,4-beta-xylosidase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 504504Beta-xylosidase
PRO_0000057687

Sites

Active site1601Proton donor Potential
Active site2801Nucleophile By similarity

Secondary structure

1 ......................................................................................... 504
Helix Strand Turn

Details...

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Sequences

Sequence LengthMass (Da)Tools
Q9ZFM2-1 [UniParc].

Last modified May 1, 1999. Version 1.
Checksum: 59518E75200A18B1

FASTA50458,119
        10         20         30         40         50         60 
MKVVNVPSNG REKFKKNWKF CVGTGRLGLA LQKEYLDHLK LVQEKIGFRY IRGHGLLSDD 

        70         80         90        100        110        120 
VGIYREVEID GEMKPFYNFT YIDRIVDSYL ALNIRPFIEF GFMPKALASG DQTVFYWKGN 

       130        140        150        160        170        180 
VTPPKDYNKW RDLIVAVVSH FIERYGIEEV RTWLFEVWNE PNLVNFWKDA NKQEYFKLYE 

       190        200        210        220        230        240 
VTARAVKSVD PHLQVGGPAI CGGSDEWITD FLHFCAERRV PVDFVSRHAY TSKAPHKKTF 

       250        260        270        280        290        300 
EYYYQELELE PPEDMLEQFK TVRALIRQSP FPHLPLHITE YNTSYSPINP VHDTALNAAY 

       310        320        330        340        350        360 
IARILSEGGD YVDSFSYWTF SDVFEEMDVP KALFHGGFGL VALHSIPKPT FHAFTFFNAL 

       370        380        390        400        410        420 
GDELLYRDGE MIVTRRKDGS IAAVLWNLVM EKGEGLTKEV QLVIPVSFSA VFIKRQIVNE 

       430        440        450        460        470        480 
QYGNAWRVWK QMGRPRFPSR QAVETLPSAQ PHVMTEQRRA TDGVIHLSIV LSKNEVTLIE 

       490        500 
IEQVRDETST YVGLDDGEIT SYSS

« Hide

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References

[1]"The glucuronic acid utilization gene cluster from Bacillus stearothermophilus T-6."
Shulami S., Gat O., Sonenshein A.L., Shoham Y.
J. Bacteriol. 181:3695-3704(1999) [PubMed: 10368143] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: T-6.
+Additional computationally mapped references.

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Cross-references

Sequence databases

EMBL
GenBank
DDBJ		DQ868502 Genomic DNA. Translation: ABI49941.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1W91X-ray2.20A/B/C/D/E/F/G/H1-504[»]
2BFGX-ray2.40A/B/C/D/E/F/G/H3-502[»]
2BS9X-ray2.20A/B/C/D/E/F/G/H3-502[»]
SMRQ9ZFM2. Positions 4-503.
ModBaseSearch...

Protein family/group databases

CAZyGH39. Glycoside Hydrolase Family 39.

Family and domain databases

InterProIPR000514. Glyco_hydro_39.
IPR017853. Glyco_hydro_catalytic_core.
IPR013781. Glyco_hydro_sg_catalytic.
[Graphical view]
Gene3DG3DSA:3.20.20.80. Glyco_hydro_cat. 1 hit.
PfamPF01229. Glyco_hydro_39. 1 hit.
[Graphical view]
PRINTSPR00745. GLHYDRLASE39.
PROSITEPS01027. GLYCOSYL_HYDROL_F39. 1 hit.
[Graphical view]
ProtoNetSearch...

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Entry information

Entry nameXYNB_BACST
AccessionPrimary (citable) accession number: Q9ZFM2
Secondary accession number(s): Q09LY4
Entry history
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: May 1, 1999
Last modified: January 19, 2010
This is version 48 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

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Relevant documents

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents