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P82186 (GUN_MYTED) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 63. 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

EC=3.2.1.4
Alternative name(s):
CMCase
Cellulase
Endo-1,4-beta-glucanase
OrganismMytilus edulis (Blue mussel)
Taxonomic identifier6550 [NCBI]
Taxonomic lineageEukaryotaMetazoaLophotrochozoaMolluscaBivalviaPteriomorphiaMytiloidaMytiloideaMytilidaeMytilinaeMytilus

Protein attributes

Sequence length181 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Active towards the soluble carboxymethylcellulose (CMC). Possesses expansin activity too. Ref.1

Catalytic activity

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

Tissue specificity

Digestive gland.

Sequence similarities

Belongs to the glycosyl hydrolase 45 (cellulase K) family.

Biophysicochemical properties

pH dependence:

Optimum pH is 4.6.

Temperature dependence:

Optimum temperature is 30-50 degrees Celsius.

Mass spectrometry

Molecular mass is 19702 Da from positions 1 - 181. Determined by MALDI. Ref.1

Ontologies

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

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular_functioncellulase activity

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 181181Endoglucanase
PRO_0000184075

Sites

Active site241Nucleophile By similarity
Active site1321Proton donor By similarity

Amino acid modifications

Disulfide bond4 ↔ 16
Disulfide bond30 ↔ 69
Disulfide bond32 ↔ 176
Disulfide bond65 ↔ 178
Disulfide bond72 ↔ 157
Disulfide bond103 ↔ 113

Secondary structure

...................................... 181
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P82186 [UniParc].

Last modified January 11, 2001. Version 1.
Checksum: E00A8C57203823F6

FASTA18119,711
        10         20         30         40         50         60 
NQKCSGNPRR YNGKSCASTT NYHDSHKGAC GCGPASGDAQ FGWNAGSFVA AASQMYFDSG 

        70         80         90        100        110        120 
NKGWCGQHCG QCIKLTTTGG YVPGQGGPVR EGLSKTFMIT NLCPNIYPNQ DWCNQGSQYG 

       130        140        150        160        170        180 
GHNKYGYELH LDLENGRSQV TGMGWNNPET TWEVVNCDSE HNHDHRTPSN SMYGQCQCAH 


Q 

« Hide

References

[1]"Purification, characterization and amino-acid sequence analysis of a thermostable, low molecular mass endo-beta-1,4-glucanase from blue mussel, Mytilus edulis."
Xu B., Hellman U., Ersson B., Janson J.-C.
Eur. J. Biochem. 267:4970-4977(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE, FUNCTION, MASS SPECTROMETRY.
Tissue: Digestive gland.

Cross-references

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1WC2X-ray1.20A1-181[»]
ProteinModelPortalP82186.
SMRP82186. Positions 1-180.
ModBaseSearch...
MobiDBSearch...

Protein family/group databases

CAZyGH45. Glycoside Hydrolase Family 45.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

InterProIPR009009. RlpA-like_DPBB.
[Graphical view]
SUPFAMSSF50685. SSF50685. 1 hit.
ProtoNetSearch...

Other

EvolutionaryTraceP82186.

Entry information

Entry nameGUN_MYTED
AccessionPrimary (citable) accession number: P82186
Entry history
Integrated into UniProtKB/Swiss-Prot: January 11, 2001
Last sequence update: January 11, 2001
Last modified: February 19, 2014
This is version 63 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)

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