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O85465 (GUN5_BACAG) Reviewed, UniProtKB/Swiss-Prot

Last modified October 16, 2013. Version 79. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Endoglucanase 5A

EC=3.2.1.4
Alternative name(s):
Alkaline cellulase
Endo-1,4-beta-glucanase 5A
Gene names
Name:cel5A
OrganismBacillus agaradhaerens (Bacillus agaradherans)
Taxonomic identifier76935 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus

Protein attributes

Sequence length400 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Catalytic activity

Endohydrolysis of (1->4)-beta-D-glucosidic linkages in cellulose, lichenin and cereal beta-D-glucans.

Subunit structure

Monomer.

Sequence similarities

Belongs to the glycosyl hydrolase 5 (cellulase A) family.

Ontologies

Keywords
   Biological processCarbohydrate metabolism
Cellulose degradation
Polysaccharide degradation
   Molecular functionGlycosidase
Hydrolase
   Technical term3D-structure
Gene Ontology (GO)
   Biological_processcellulose catabolic process

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentextracellular region

Inferred from electronic annotation. Source: InterPro

   Molecular_functioncarbohydrate binding

Inferred from electronic annotation. Source: InterPro

cellulase activity

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 400400Endoglucanase 5A
PRO_0000184043

Sites

Active site1651Proton donor
Active site2541Nucleophile

Secondary structure

......................................................... 400
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
O85465 [UniParc].

Last modified November 1, 1998. Version 1.
Checksum: 3F9C66FB9BC36FFF

FASTA40044,702
        10         20         30         40         50         60 
MKKITTIFVV LLMTVALFSI GNTTAADNDS VVEEHGQLSI SNGELVNERG EQVQLKGMSS 

        70         80         90        100        110        120 
HGLQWYGQFV NYESMKWLRD DWGINVFRAA MYTSSGGYID DPSVKEKVKE AVEAAIDLDI 

       130        140        150        160        170        180 
YVIIDWHILS DNDPNIYKEE AKDFFDEMSE LYGDYPNVIY EIANEPNGSD VTWGNQIKPY 

       190        200        210        220        230        240 
AEEVIPIIRN NDPNNIIIVG TGTWSQDVHH AADNQLADPN VMYAFHFYAG THGQNLRDQV 

       250        260        270        280        290        300 
DYALDQGAAI FVSEWGTSAA TGDGGVFLDE AQVWIDFMDE RNLSWANWSL THKDESSAAL 

       310        320        330        340        350        360 
MPGANPTGGW TEAELSPSGT FVREKIRESA SIPPSDPTPP SDPGEPDPTP PSDPGEYPAW 

       370        380        390        400 
DPNQIYTNEI VYHNGQLWQA KWWTQNQEPG DPYGPWEPLN 

« Hide

References

[1]Bjornvad M.E.
Submitted (MAY-1998) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC 700163 / DSM 8721 / LMG 17948 / NCIMB 40482.
[2]"Structure of the Bacillus agaradherans family 5 endoglucanase at 1.6-A and its cellobiose complex at 2.0-A resolution."
Davies G.J., Dauter M., Brzozowski A.M., Bjoernvad M.E., Andersen K.V., Schuelein M.
Biochemistry 37:1926-1932(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.57 ANGSTROMS) OF 30-329.
Strain: ATCC 700163 / DSM 8721 / LMG 17948 / NCIMB 40482.
[3]"Snapshots along an enzymatic reaction coordinate: analysis of a retaining beta-glycoside hydrolase."
Davies G.J., MacKenzie L.F., Varrot A., Dauter M., Brzozowski A.M., Schuelein M., Withers S.G.
Biochemistry 37:11707-11713(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.64 ANGSTROMS) OF 30-329.
Strain: ATCC 700163 / DSM 8721 / LMG 17948 / NCIMB 40482.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF067428 Genomic DNA. Translation: AAC19169.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1A3HX-ray1.57A30-329[»]
1E5JX-ray1.85A27-331[»]
1H11X-ray1.08A27-329[»]
1H2JX-ray1.15A27-329[»]
1H5VX-ray1.10A30-330[»]
1HF6X-ray1.15A27-329[»]
1OCQX-ray1.08A27-329[»]
1QHZX-ray1.95A27-331[»]
1QI0X-ray2.10A27-331[»]
1QI2X-ray1.75A27-331[»]
1W3KX-ray1.20A27-329[»]
1W3LX-ray1.04A27-329[»]
2A3HX-ray2.00A30-329[»]
2V38X-ray1.50A27-331[»]
3A3HX-ray1.64A30-329[»]
4A3HX-ray1.65A27-329[»]
5A3HX-ray1.82A27-329[»]
6A3HX-ray1.68A27-329[»]
7A3HX-ray0.95A27-329[»]
8A3HX-ray0.97A27-329[»]
ProteinModelPortalO85465.
SMRO85465. Positions 30-331.
ModBaseSearch...
MobiDBSearch...

Protein family/group databases

CAZyCBM5. Carbohydrate-Binding Module Family 5.
GH5. Glycoside Hydrolase Family 5.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

Gene3D2.10.10.20. 1 hit.
3.20.20.80. 1 hit.
InterProIPR003610. CBM_fam5/12.
IPR001547. Glyco_hydro_5.
IPR018087. Glyco_hydro_5_CS.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]
PfamPF02839. CBM_5_12. 1 hit.
PF00150. Cellulase. 1 hit.
[Graphical view]
SMARTSM00495. ChtBD3. 1 hit.
[Graphical view]
SUPFAMSSF51055. SSF51055. 1 hit.
SSF51445. SSF51445. 1 hit.
PROSITEPS00659. GLYCOSYL_HYDROL_F5. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceO85465.

Entry information

Entry nameGUN5_BACAG
AccessionPrimary (citable) accession number: O85465
Entry history
Integrated into UniProtKB/Swiss-Prot: July 15, 1999
Last sequence update: November 1, 1998
Last modified: October 16, 2013
This is version 79 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries