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Q9AMB5 (Q9AMB5_BACPU) Unreviewed, UniProtKB/TrEMBL

Last modified March 8, 2011. Version 46. 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 AAG61087.1
Taxonomic identifier1408 [NCBI]
Taxonomic lineageBacteria › Firmicutes › Bacillales › Bacillaceae › Bacillus

Protein attributes

Sequence length228 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 AAG61087.1
   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
Q9AMB5 [UniParc].

Last modified June 1, 2001. Version 1.
Checksum: A47DF6DBE83DA5EA

FASTA22825,421
        10         20         30         40         50         60 
MNLRKLRLLF VMCIGLTLIL TAVPAHARTI TNNEMGNQSG YDYELWKDYG NTSMTLNNGG 

        70         80         90        100        110        120 
AFSSGWNNIG NALFRKGKKF DSTRTHHQLG NISINYNASF NPGGNSYLCV YVWTQSPLAE 

       130        140        150        160        170        180 
YYIVDSWGTY RPTGAYKGSF YADGGTYDIY ETTLVNQPSI IGIATFKQYL SVRQTKRTSG 

       190        200        210        220 
TVSVSAHFRK WESLGKPMGK MYETAFTVEG YQSSGSANVM TNQLFIGN

« Hide

References

[1]"Cloning and expression of endo-1,4-xylanase gene from Bacillus pumilus HB030."
Lixin M.
Submitted (DEC-2000) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AF326785 Genomic DNA. Translation: AAG61087.1.

3D structure databases

HSSPHSSP built from PDB template 1F5J based on UniProtKB P77853.
ProteinModelPortalQ9AMB5.
SMRQ9AMB5. Positions 27-227.
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 nameQ9AMB5_BACPU
AccessionPrimary (citable) accession number: Q9AMB5
Entry history
Integrated into UniProtKB/TrEMBL: June 1, 2001
Last sequence update: June 1, 2001
Last modified: March 8, 2011
This is version 46 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)
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