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P17877 (GUN1_CLOJO) Reviewed, UniProtKB/Swiss-Prot

Last modified October 16, 2013. Version 39. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | 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 1

EC=3.2.1.4
Alternative name(s):
Cellulase 1
Endo-1,4-beta-glucanase 1
OrganismClostridium josui
Taxonomic identifier1499 [NCBI]
Taxonomic lineageBacteriaFirmicutesClostridiaClostridialesClostridiaceaeClostridium

Protein attributes

Sequence length25 AA.
Sequence statusFragment.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

This enzyme hydrolyzes cellotetraose, cellopentaose, and cellohexaose to cellobiose and cellotriose but does not hydrolyze cellobiose or cellotriose.

Catalytic activity

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

Biophysicochemical properties

pH dependence:

Optimum pH is 6.8 with carboxymethyl cellulose (CmC) as substrate.

Temperature dependence:

Optimum temperature is 60 degrees Celsius with carboxymethyl cellulose (CmC) as substrate.

Ontologies

Keywords
   Biological processCarbohydrate metabolism
Cellulose degradation
Polysaccharide degradation
   Molecular functionGlycosidase
Hydrolase
   Technical termDirect 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 – ›25›25Endoglucanase 1
PRO_0000184077

Experimental info

Non-terminal residue251

Sequences

Sequence LengthMass (Da)Tools
P17877 [UniParc].

Last modified August 1, 1990. Version 1.
Checksum: F68D1B4D3BD9DFCB

FASTA252,808
        10         20 
YDASLKPNLQ IPQKNIPNND AVNIK 

« Hide

References

[1]"Purification and properties of an endo-1,4-beta-glucanase from Clostridium josui."
Fujino T., Sukhumavasi J., Sasaki T., Ohmiya K., Shimizu S.
J. Bacteriol. 171:4076-4079(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE.

Cross-references

Sequence databases

PIRA45920.

3D structure databases

ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

ProtoNetSearch...

Entry information

Entry nameGUN1_CLOJO
AccessionPrimary (citable) accession number: P17877
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1990
Last sequence update: August 1, 1990
Last modified: October 16, 2013
This is version 39 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries