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P37699 (GUNC_CLOCE) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 95. 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 C

EC=3.2.1.4
Alternative name(s):
Cellulase C
EGCCC
Endo-1,4-beta-glucanase C
Gene names
Name:celCCC
Ordered Locus Names:Ccel_0730
OrganismClostridium cellulolyticum (strain ATCC 35319 / DSM 5812 / JCM 6584 / H10) [Complete proteome] [HAMAP]
Taxonomic identifier394503 [NCBI]
Taxonomic lineageBacteriaFirmicutesClostridiaClostridialesClostridiaceaeClostridium

Protein attributes

Sequence length460 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

The biological conversion of cellulose to glucose generally requires three types of hydrolytic enzymes: (1) Endoglucanases which cut internal beta-1,4-glucosidic bonds; (2) Exocellobiohydrolases that cut the dissaccharide cellobiose from the non-reducing end of the cellulose polymer chain; (3) Beta-1,4-glucosidases which hydrolyze the cellobiose and other short cello-oligosaccharides to glucose.

Catalytic activity

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

Pathway

Glycan metabolism; cellulose degradation.

Subunit structure

Monomer.

Domain

A 24 residue domain is repeated twice in this enzyme as well as in other C.thermocellum cellulosome enzymes. This domain may function as the binding ligand for the SL component.

Post-translational modification

There are two forms of the cellulase. The shorter form lacks probably the C-terminal reiterated domains.

Sequence similarities

Belongs to the glycosyl hydrolase 8 (cellulase D) family.

Ontologies

Keywords
   Biological processCarbohydrate metabolism
Cellulose degradation
Polysaccharide degradation
   DomainRepeat
Signal
   Molecular functionGlycosidase
Hydrolase
   Technical termComplete proteome
Direct protein sequencing
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

Signal peptide1 – 3232 Ref.3
Chain33 – 460428Endoglucanase C
PRO_0000007936

Regions

Repeat406 – 429241
Repeat439 – 460222
Region406 – 460552 X 24 AA approximate repeats

Sites

Active site991Proton donor By similarity
Active site1551Nucleophile Potential

Experimental info

Sequence conflict911S → T in AAA73867. Ref.1

Sequences

Sequence LengthMass (Da)Tools
P37699 [UniParc].

Last modified May 26, 2009. Version 2.
Checksum: 2F31E1F6CB41504F

FASTA46050,483
        10         20         30         40         50         60 
MIKGSSLKRF KSLVMAAIFS VSIISTAIAS SAADQIPFPY DAKYPNGAYS CLADSQSIGN 

        70         80         90        100        110        120 
NLVRSEWEQW KSAHITSNGA RGYKRVQRDA STNYDTVSEG LGYGLLLSVY FGEQQLFDDL 

       130        140        150        160        170        180 
YRYVKVFLNS NGLMSWRIDS SGNIMGKDSI GAATDADEDI AVSLVFAHKK WGTSGGFNYQ 

       190        200        210        220        230        240 
TEAKNYINNI YNKMVEPGTY VIKAGDTWGG SNVTNPSYFA PAWYRIFADF TGNSGWINVA 

       250        260        270        280        290        300 
NKCYEIADKA RNSNTGLVPD WCTANGTPAS GQGFDFYYDA IRYQWRAAID YSWYGTAKAK 

       310        320        330        340        350        360 
THCDAISNFF KNIGYANIKD GYTISGSQIS SNHTATFVSC AAAAAMTGTD TTYAKNIYNE 

       370        380        390        400        410        420 
CVKVKDSGNY TYFGNTLRMM VLLYTTGNFP NLYTYNSQPK PDLKGDVNND GAIDALDIAA 

       430        440        450        460 
LKKAILTQTT SNISLTNADM NNDGNIDAID FAQLKVKLLN 

« Hide

References

« Hide 'large scale' references
[1]"Sequence analysis of a gene cluster encoding cellulases from Clostridium cellulolyticum."
Bagnara-Tardif C., Gaudin C., Belaich A., Hoest P., Citard T., Belaich J.-P.
Gene 119:17-28(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC 35319 / DSM 5812 / JCM 6584 / H10.
[2]"Complete sequence of Clostridium cellulolyticum H10."
US DOE Joint Genome Institute
Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H., Bruce D., Goodwin L., Pitluck S., Chertkov O., Saunders E., Brettin T., Detter J.C., Han C., Larimer F., Land M., Hauser L., Kyrpides N. expand/collapse author list , Ivanova N., Zhou J., Richardson P.
Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 35319 / DSM 5812 / JCM 6584 / H10.
[3]"Purification and characterization of endoglucanase C from Clostridium cellulolyticum. Catalytic comparison with endoglucanase A."
Fierobe H.-P., Bagnara-Tardif C., Gaudin C., Guerlesquin F., Sauve P., Belaich A., Belaich J.-P.
Eur. J. Biochem. 217:557-565(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 33-37, CHARACTERIZATION.
Strain: ATCC 35319 / DSM 5812 / JCM 6584 / H10.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M87018 Genomic DNA. Translation: AAA73867.1.
CP001348 Genomic DNA. Translation: ACL75109.1.
PIRJC1299.
RefSeqYP_002505089.1. NC_011898.1.

3D structure databases

ProteinModelPortalP37699.
SMRP37699. Positions 39-391.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING394503.Ccel_0730.

Protein family/group databases

CAZyGH8. Glycoside Hydrolase Family 8.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACL75109; ACL75109; Ccel_0730.
GeneID7309584.
KEGGcce:Ccel_0730.
PATRIC19432257. VBICloCel57783_0755.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG3405.
HOGENOMHOG000069581.
OMAGNFPNLY.
OrthoDBEOG67Q9BX.

Enzyme and pathway databases

BioCycCCEL394503:GJET-751-MONOMER.
UniPathwayUPA00696.

Family and domain databases

Gene3D1.10.1330.10. 1 hit.
1.50.10.10. 1 hit.
InterProIPR008928. 6-hairpin_glycosidase-like.
IPR012341. 6hp_glycosidase.
IPR016134. Cellulos_enz_dockerin_1.
IPR002105. Cellulos_enz_dockerin_1_Ca-bd.
IPR018242. Dockerin_1.
IPR018247. EF_Hand_1_Ca_BS.
IPR002037. Glyco_hydro_8.
IPR019834. Glyco_hydro_8_CS.
[Graphical view]
PfamPF00404. Dockerin_1. 2 hits.
PF01270. Glyco_hydro_8. 1 hit.
[Graphical view]
PRINTSPR00735. GLHYDRLASE8.
SUPFAMSSF48208. SSF48208. 1 hit.
SSF63446. SSF63446. 1 hit.
PROSITEPS00448. CLOS_CELLULOSOME_RPT. 1 hit.
PS00018. EF_HAND_1. 2 hits.
PS00812. GLYCOSYL_HYDROL_F8. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameGUNC_CLOCE
AccessionPrimary (citable) accession number: P37699
Secondary accession number(s): B8I7V2
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1994
Last sequence update: May 26, 2009
Last modified: May 14, 2014
This is version 95 of the entry and version 2 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

PATHWAY comments

Index of metabolic and biosynthesis pathways

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries