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Q7SIE3 (Q7SIE3_BACAG) Unreviewed, UniProtKB/TrEMBL

Last modified June 11, 2014. Version 63. Feed History...

Clusters with 100%, 90%, 50% identity | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry infoCustomize order

Names and origin

Protein namesRecommended name:
Endo-1,4-beta-xylanase RuleBase RU004392

EC=3.2.1.8 RuleBase RU004392
OrganismBacillus agaradhaerens (Bacillus agaradherans) PDB 1H4G
Taxonomic identifier76935 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus

Protein attributes

Sequence length207 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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Sites

Active site941Nucleophile PDB 1H4G
Active site1841Proton donor/acceptor PDB 1H4G
Binding site1531Sulfate PDB 1H4G

Amino acid modifications

Modified residue11Pyrrolidone carboxylic acid PDB 1QH7 PDB 1QH6

Sequences

Sequence LengthMass (Da)Tools
Q7SIE3 [UniParc].

Last modified December 15, 2003. Version 1.
Checksum: C498EF0D0A085D0B

FASTA20723,152
        10         20         30         40         50         60 
QIVTDNSIGN HDGYDYEFWK DSGGSGTMIL NHGGTFSAQW NNVNNILFRK GKKFNETQTH 

        70         80         90        100        110        120 
QQVGNMSINY GANFQPNGNA YLCVYGWTVD PLVEYYIVDS WGNWRPPGAT PKGTITVDGG 

       130        140        150        160        170        180 
TYDIYETLRV NQPSIKGIAT FKQYWSVRRS KRTSGTISVS NHFRAWENLG MNMGKMYEVA 

       190        200 
LTVEGYQSSG SANVYSNTLR INGNPLS 

« Hide

References

[1]"Catalysis and specificity in enzymatic glycoside hydrolysis: a 2,5B conformation for the glycosyl-enzyme intermediate revealed by the structure of the Bacillus agaradhaerens family 11 xylanase."
Sabini E., Sulzenbacher G., Dauter M., Dauter Z., Jorgensen P.L., Schulein M., Dupont C., Davies G.J., Wilson K.S.
Chem. Biol. 6:483-492(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.10 ANGSTROMS) OF 2-207 IN COMPLEX WITH SULFATE, ACTIVE SITE, AND CARBOXYLATION AT GLN-1.
[2]"Structural and active site modification studies implicate Glu, Trp and Arg in the activity of xylanase from alkalophilic Bacillus sp. (NCL 87-6-10)."
Balakrishnan H., Satyanarayana L., Gaikward S., Suresh C.G.
Submitted (NOV-2005) to the PDB data bank
Cited for: X-RAY CRYSTALLOGRAPHY (2.80 ANGSTROMS) OF 2-206.
[3]"Crystal structure of alkaline thermophlic xylanase from Bacillus sp. (NCL 86-6-10) with complex xylotriose: Xylotriose cleaved to xylobiose and xylose."
Satyanarayana L., Gaikwad S.M., Balakrishnan H., Suresh C.G.
Submitted (NOV-2006) to the PDB data bank
Cited for: X-RAY CRYSTALLOGRAPHY (2.40 ANGSTROMS) OF 2-206.

Cross-references

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1H4GX-ray1.10A/B2-207[»]
1QH6X-ray2.00A/B1-207[»]
1QH7X-ray1.78A/B1-207[»]
2F6BX-ray2.80A/B2-206[»]
2NQYX-ray2.40A/B2-206[»]
ProteinModelPortalQ7SIE3.
SMRQ7SIE3. Positions 1-207.
ModBaseSearch...
MobiDBSearch...

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. SSF49899. 1 hit.
PROSITEPS00776. GLYCOSYL_HYDROL_F11_1. 1 hit.
PS00777. GLYCOSYL_HYDROL_F11_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceQ7SIE3.

Entry information

Entry nameQ7SIE3_BACAG
AccessionPrimary (citable) accession number: Q7SIE3
Entry history
Integrated into UniProtKB/TrEMBL: December 15, 2003
Last sequence update: December 15, 2003
Last modified: June 11, 2014
This is version 63 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)