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Q7SID8 (Q7SID8_BACSU) Unreviewed, UniProtKB/TrEMBL

Last modified April 5, 2011. Version 48. Feed History...

Clusters with 100%, 90%, 50% identity | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Endo-1,4-beta-xylanase RuleBase RU004392
EC=3.2.1.8 RuleBase RU004392
OrganismBacillus subtilis PDB 1IGO
Taxonomic identifier1423 [NCBI]
Taxonomic lineageBacteria › Firmicutes › Bacillales › Bacillaceae › Bacillus

Protein attributes

Sequence length205 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Catalytic activity

Endohydrolysis of (1->4)-beta-D-xylosidic linkages in xylans. RuleBase RU004392

Pathway

Glycan degradation; xylan degradation. RuleBase RU004392

Sequence similarities

Belongs to the glycosyl hydrolase 11 (cellulase G) family. RuleBase RU003433

Ontologies

Keywords
   Biological processXylan degradation RuleBase RU003433
   Molecular functionGlycosidase RuleBase RU003433
Hydrolase
   Technical term3D-structure PDB 1IGO
Gene Ontology (GO)
   Biological processxylan catabolic process

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular functionendo-1,4-beta-xylanase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequences

Sequence LengthMass (Da)Tools
Q7SID8 [UniParc].

Last modified December 15, 2003. Version 1.
Checksum: 35F4E6BC657BBC74

FASTA20522,562
        10         20         30         40         50         60 
ATTITSNQTG THDGYDYELW KDSGNTSMTL NSGGAFSAQW SNIGNALFRK GKKFDSTKTH 

        70         80         90        100        110        120 
SQLGNISINY NATFNPGGNS YLCVYGWTKD PLTEYYIVDN WGTYRPTGTP KGTFTVDGGT 

       130        140        150        160        170        180 
YDIYETTRIN QPSIIGIATF KQYWSVRQTK RTSGTVSVSE HFKKWESLGM PMGKMYETAL 

       190        200 
TVEGYQSNGS ANVTANVLTI GGKPL

« Hide

References

[1]"Characterization of a family 11 xylanase from Bacillus subtillis B230 used for paper bleaching."
Oakley A.J., Heinrich T., Thompson C.A., Wilce M.C.
Acta Crystallogr. D Biol. Crystallogr. 59:627-636(2003) [PubMed: 12657781] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS).
+Additional computationally mapped references.

Cross-references

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1IGOX-ray2.20A/B1-205[»]
ProteinModelPortalQ7SID8.
SMRQ7SID8. Positions 1-205.
ModBaseSearch...

Protein family/group databases

CAZyGH11. Glycoside Hydrolase Family 11.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

InterProIPR008985. ConA-like_lec_gl.
IPR001137. Glyco_hydro_11.
IPR013319. Glyco_hydro_11/12_cat.
IPR018208. Glyco_hydro_11_AS.
[Graphical view]
Gene3DG3DSA:2.60.120.180. Glyco_hydro_11/12_cat. 1 hit.
PfamPF00457. Glyco_hydro_11. 1 hit.
[Graphical view]
PRINTSPR00911. GLHYDRLASE11.
SUPFAMSSF49899. ConA_like_lec_gl. 1 hit.
PROSITEPS00776. GLYCOSYL_HYDROL_F11_1. 1 hit.
PS00777. GLYCOSYL_HYDROL_F11_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameQ7SID8_BACSU
AccessionPrimary (citable) accession number: Q7SID8
Entry history
Integrated into UniProtKB/TrEMBL: December 15, 2003
Last sequence update: December 15, 2003
Last modified: April 5, 2011
This is version 48 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)
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