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Q9RQB8 (Q9RQB8_9MICO) Unreviewed, UniProtKB/TrEMBL

Last modified January 25, 2012. Version 47. 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:xyn11A EMBL AAD54767.1
OrganismXylanimicrobium pachnodae EMBL AAD54767.1
Taxonomic identifier101489 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesMicrococcineaePromicromonosporaceaeXylanimicrobium

Protein attributes

Sequence length335 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

Sequences

Sequence LengthMass (Da)Tools
Q9RQB8 [UniParc].

Last modified May 1, 2000. Version 1.
Checksum: 64EFDB808C25542D

FASTA33534,383
        10         20         30         40         50         60 
MTRTISRAAH RPPAGGRIAR ALAAAGATVA MVIAGVAAAQ PAAAVDSNST GSSGGYFYSF 

        70         80         90        100        110        120 
WTDAPGTVSM NLGSGGNYST SWSNTGNFVA GKGWSTGSAR TISYSGTFNP SGNAYLAVYG 

       130        140        150        160        170        180 
WSHDPLVEYY IVDSWGTYRP TGTFMGTVNS DGGTYDIYKT TRTNAPSIEG TATFTQYWSV 

       190        200        210        220        230        240 
RQSKRVGGTI TTANHFNAWA SHGMNLGRHD YQILATEGYQ SSGSSNITIG STSGGGGSGG 

       250        260        270        280        290        300 
GTTTPPTNNG CTVQVTKGDE WGDRFNVSFT VSGSSSWKVA IALSGGQSLQ NSWSANVTGS 

       310        320        330 
TGTLTATPNG SGNSFGITVY KNGSSTLPTA TCSTT 

« Hide

References

[1]"Molecular and biochemical characterization of two xylanase-encoding genes from Cellulomonas pachnodae."
Cazemier A.E., Verdoes J.C., van Ooyen A.J., Op den Camp H.J.
Appl. Environ. Microbiol. 65:4099-4107(1999) [PubMed: 10473422] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF120156 Genomic DNA. Translation: AAD54767.1.

3D structure databases

HSSPHSSP built from PDB template 1M4W based on UniProtKB Q8GMV7.
ProteinModelPortalQ9RQB8.
SMRQ9RQB8. Positions 45-220, 250-333.
ModBaseSearch...

Protein family/group databases

CAZyCBM2. Carbohydrate-Binding Module Family 2.
GH11. Glycoside Hydrolase Family 11.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

InterProIPR008965. Carb-bd_dom.
IPR012291. CBD_carb-bd_dom.
IPR001919. Cellulose-bd_dom_fam2_bac.
IPR008985. ConA-like_lec_gl.
IPR001137. Glyco_hydro_11.
IPR013319. Glyco_hydro_11/12_cat.
IPR018208. Glyco_hydro_11_AS.
[Graphical view]
Gene3DG3DSA:2.60.40.290. CBD_carb_bd. 1 hit.
G3DSA:2.60.120.180. Glyco_hydro_11/12_cat. 1 hit.
PfamPF00553. CBM_2. 1 hit.
PF00457. Glyco_hydro_11. 1 hit.
[Graphical view]
PRINTSPR00911. GLHYDRLASE11.
SMARTSM00637. CBD_II. 1 hit.
[Graphical view]
SUPFAMSSF49384. Cellul_bind. 1 hit.
SSF49899. ConA_like_lec_gl. 1 hit.
PROSITEPS51173. CBM2. 1 hit.
PS00776. GLYCOSYL_HYDROL_F11_1. 1 hit.
PS00777. GLYCOSYL_HYDROL_F11_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameQ9RQB8_9MICO
AccessionPrimary (citable) accession number: Q9RQB8
Entry history
Integrated into UniProtKB/TrEMBL: May 1, 2000
Last sequence update: May 1, 2000
Last modified: January 25, 2012
This is version 47 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)