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Q9L7Q9 (Q9L7Q9_BACPU) Unreviewed, UniProtKB/TrEMBL

Last modified March 8, 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 pumilus (Bacillus mesentericus) EMBL AAF32359.1
Taxonomic identifier1408 [NCBI]
Taxonomic lineageBacteria › Firmicutes › Bacillales › Bacillaceae › Bacillus

Protein attributes

Sequence length227 AA.
Sequence statusComplete.
Protein existenceInferred from homology

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 EMBL AAF32359.1
   Molecular functionGlycosidase RuleBase RU003433
Hydrolase
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
Q9L7Q9 [UniParc].

Last modified October 1, 2000. Version 1.
Checksum: 1D26819FA4BB5966

FASTA22725,563
        10         20         30         40         50         60 
MNLKRLRLLF VMCIGFVLTL TAVPAHAETI YDNRIGTHSG YDFELWKDYG NTSMTLNNGG 

        70         80         90        100        110        120 
AFSASWNNIG NALFRKGKKF DSTKTHHQLG NISINYNAAF NPGGNSYLCV YGWTQSPLAE 

       130        140        150        160        170        180 
YYIVESWGTY RPTGTYKGSF YADGGTYDIY ETLRVNQPSI IGDATFKQYW SVRQTKRTSG 

       190        200        210        220 
TASVSEHFKK WESLGMPMGK MYETALTVEG YRSNGSANVM TNQLMIR

« Hide

References

[1]"Cloning and expression of the Bacillus pumilus endo-beta-xylanase encoding gene xynA in Saccharomyces cerevisiae."
Nuyens F., Iserentant D., Van Zyl W.H., Michiels C.
Submitted (JAN-2000) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AF220528 Genomic DNA. Translation: AAF32359.1.

3D structure databases

HSSPHSSP built from PDB template 1F5J based on UniProtKB P77853.
ProteinModelPortalQ9L7Q9.
SMRQ9L7Q9. Positions 27-226.
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 nameQ9L7Q9_BACPU
AccessionPrimary (citable) accession number: Q9L7Q9
Entry history
Integrated into UniProtKB/TrEMBL: October 1, 2000
Last sequence update: October 1, 2000
Last modified: March 8, 2011
This is version 48 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)
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