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P0C2S3 (GUNC_CLOTM) Reviewed, UniProtKB/Swiss-Prot

Last modified October 16, 2013. Version 40. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | 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 C

EC=3.2.1.4
Alternative name(s):
Cellulase C
Endo-1,4-beta-glucanase C
Short name=EgC
Gene names
Name:celC
OrganismClostridium thermocellum
Taxonomic identifier1515 [NCBI]
Taxonomic lineageBacteriaFirmicutesClostridiaClostridialesClostridiaceaeClostridium

Protein attributes

Sequence length343 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

This enzyme catalyzes the endohydrolysis of 1,4-beta-glucosidic linkages in cellulose, lichenin and cereal beta-D-glucans.

Catalytic activity

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

Pathway

Glycan metabolism; cellulose degradation.

Miscellaneous

CelC has an unusual substrate range and displays features common to cellobiohydrolases by being able to cleave the agluconic bond of aryl-beta-glucosides.

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-UniPathway

   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 – 343343Endoglucanase C
PRO_0000184047

Sites

Active site1401Proton donor
Active site2801Nucleophile Ref.2

Secondary structure

............................................................ 343
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P0C2S3 [UniParc].

Last modified April 17, 2007. Version 1.
Checksum: BD24763F548C726E

FASTA34340,954
        10         20         30         40         50         60 
MVSFKAGINL GGWISQYQVF SKEHFDTFIT EKDIETIAEA GFDHVRLPFD YPIIESDDNV 

        70         80         90        100        110        120 
GEYKEDGLSY IDRCLEWCKK YNLGLVLDMH HAPGYRFQDF KTSTLFEDPN QQKRFVDIWR 

       130        140        150        160        170        180 
FLAKRYINER EHIAFELLNE VVEPDSTRWN KLMLEYIKAI REIDSTMWLY IGGNNYNSPD 

       190        200        210        220        230        240 
ELKNLADIDD DYIVYNFHFY NPFFFTHQKA HWSESAMAYN RTVKYPGQYE GIEEFVKNNP 

       250        260        270        280        290        300 
KYSFMMELNN LKLNKELLRK DLKPAIEFRE KKKCKLYCGE FGVIAIADLE SRIKWHEDYI 

       310        320        330        340 
SLLEEYDIGG AVWNYKKMDF EIYNEDRKPV SQELVNILAR RKT 

« Hide

References

[1]"Nucleotide sequence of the celC gene encoding endoglucanase C of Clostridium thermocellum."
Schwarz W.H., Schimming S., Ruecknagel K.P., Burgschwaiger S., Kreil G., Staudenbauer W.L.
Gene 63:23-30(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"Glu280 is the nucleophile in the active site of Clostridium thermocellum CelC, a family A endo-beta-1,4-glucanase."
Wang Q., Tull D., Meinke A., Gilkes N.R., Warren R.A., Aebersold R., Withers S.G.
J. Biol. Chem. 268:14096-14102(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: ACTIVE SITE GLU-280.
[3]"A common protein fold and similar active site in two distinct families of beta-glycanases."
Dominguez R., Souchon H., Spinelli S., Dauter Z., Wilson K.S., Chauvaux S., Beguin P., Alzari P.M.
Nat. Struct. Biol. 2:569-576(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.15 ANGSTROMS).
[4]"The crystal structure of a family 5 endoglucanase mutant in complexed and uncomplexed forms reveals an induced fit activation mechanism."
Dominguez R., Souchon H., Lascombe M.-B., Alzari P.M.
J. Mol. Biol. 257:1042-1051(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF MUTANT GLN-140.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M19422 Genomic DNA. Translation: AAA23220.1.
PIRJT0268.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1CECX-ray2.15A1-343[»]
1CENX-ray2.30A1-343[»]
1CEOX-ray1.90A1-343[»]
ProteinModelPortalP0C2S3.
SMRP0C2S3. Positions 1-340.
ModBaseSearch...
MobiDBSearch...

Protein family/group databases

CAZyGH5. Glycoside Hydrolase Family 5.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Enzyme and pathway databases

UniPathwayUPA00696.

Family and domain databases

Gene3D3.20.20.80. 1 hit.
InterProIPR001547. Glyco_hydro_5.
IPR018087. Glyco_hydro_5_CS.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]
PfamPF00150. Cellulase. 1 hit.
[Graphical view]
SUPFAMSSF51445. SSF51445. 2 hits.
PROSITEPS00659. GLYCOSYL_HYDROL_F5. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP0C2S3.

Entry information

Entry nameGUNC_CLOTM
AccessionPrimary (citable) accession number: P0C2S3
Secondary accession number(s): P07985
Entry history
Integrated into UniProtKB/Swiss-Prot: April 17, 2007
Last sequence update: April 17, 2007
Last modified: October 16, 2013
This is version 40 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

PATHWAY comments

Index of metabolic and biosynthesis pathways

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries