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E1AHZ6 (E1AHZ6_PAEPO) Unreviewed, UniProtKB/TrEMBL

Last modified March 6, 2013. Version 14. 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
Gene names
Name:xyn EMBL ADK47978.1
OrganismPaenibacillus polymyxa (Bacillus polymyxa) EMBL ADK47978.1
Taxonomic identifier1406 [NCBI]
Taxonomic lineageBacteria › Firmicutes › Bacilli › Bacillales › Paenibacillaceae › Paenibacillus

Protein attributes

Sequence length211 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.

Ontologies

Keywords
   Biological processXylan degradation RuleBase RU004392 EMBL ADK47978.1
   Molecular functionGlycosidase RuleBase RU004392 EMBL ADK47978.1
Hydrolase
Gene Ontology (GO)
   Biological_processxylan catabolic process

Inferred from electronic annotation. Source: UniProtKB-UniPathway

   Molecular_functionendo-1,4-beta-xylanase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequences

Sequence LengthMass (Da)Tools
E1AHZ6 [UniParc].

Last modified November 2, 2010. Version 1.
Checksum: F98287C31FEE94F3

FASTA21122,703
        10         20         30         40         50         60 
MFKLKKKVMT AVLAASMSIG LFAATANAAT DYWQNWTDGG GTVNAVNGSG GNYSVNWSNT 

        70         80         90        100        110        120 
GNFVVGKGWN TGSASRVINY NAGVWAPSGN GYLTLYGWTR NSLIEYYVVD SWGTYRPTGT 

       130        140        150        160        170        180 
YKGTVSSDGG TYDIYTAQRV NAPSIDGTAT FTQYWSVRQS KRATGSNVAI TFANHVNAWK 

       190        200        210 
SKGMNLGSSW SYQVLATEGY QSSGSSNVTV W

« Hide

References

[1]"Cell surface display of cellulase activity-free xylanase enzyme on Saccharomyces Cerevisiae EBY100."
Yeasmin S., Kim C.H., Park H.J., Sheikh M.I., Lee J.Y., Kim J.W., Back K.K., Kim S.H.
Appl. Biochem. Biotechnol. 164:294-304(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE.
Strain: PPL-3 EMBL ADK47978.1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		HM769760 Genomic DNA. Translation: ADK47978.1.

3D structure databases

ProteinModelPortalE1AHZ6.
SMRE1AHZ6. Positions 25-211.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Enzyme and pathway databases

UniPathwayUPA00114.

Family and domain databases

Gene3D2.60.120.180. 1 hit.
InterProIPR008985. ConA-like_lec_gl_sf.
IPR001137. Glyco_hydro_11.
IPR013319. Glyco_hydro_11/12.
IPR018208. Glyco_hydro_11_AS.
[Graphical view]
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 nameE1AHZ6_PAEPO
AccessionPrimary (citable) accession number: E1AHZ6
Entry history
Integrated into UniProtKB/TrEMBL: November 2, 2010
Last sequence update: November 2, 2010
Last modified: March 6, 2013
This is version 14 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)
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