Reviewed,
UniProtKB/Swiss-Prot P37699 (GUNC_CLOCE)
Last modified
June 16, 2009.
Version 64.
History...
Clusters with 100%,
90%,
50% identity |
Documents (3) |
Third-party data |
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Names and origin
| Protein names | Recommended name: Endoglucanase C EC=3.2.1.4 Alternative name(s): Endo-1,4-beta-glucanase C Cellulase C EGCCC | ||||
| Gene names |
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| Organism | Clostridium cellulolyticum (strain ATCC 35319 / DSM 5812 / JCM 6584 / H10) | ||||
| Taxonomic identifier | 394503 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Firmicutes › Clostridia › Clostridiales › Clostridiaceae › Clostridium |
Protein attributes
| Sequence length | 460 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is further processed into a mature form. |
| Protein existence | Evidence 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 | |
| Subunit structure | Monomer. |
| Domain | A 24 residues 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 process | Carbohydrate metabolism Cellulose degradation Polysaccharide degradation |
| Domain | Repeat Signal |
| Molecular function | Glycosidase Hydrolase |
| Technical term | Direct protein sequencing |
| Gene Ontology (GO) | |
| Biological process | cellulose catabolic process Inferred from electronic annotation. Source: UniProtKB-KW |
| Molecular function | cellulase activity Inferred from electronic annotation. Source: EC |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Signal peptide | 1 – 32 | 32 | Ref.3 | ||||||
| Chain | 33 – 460 | 428 | Endoglucanase C | PRO_0000007936 | |||||
Regions | |||||||||
| Repeat | 406 – 429 | 24 | 1 | ||||||
| Repeat | 439 – 460 | 22 | 2 | ||||||
| Region | 406 – 460 | 55 | 2 X 24 AA approximate repeats | ||||||
Sites | |||||||||
| Active site | 99 | 1 | Proton donor By similarity | ||||||
| Active site | 155 | 1 | Nucleophile Potential | ||||||
Experimental info | |||||||||
| Sequence conflict | 91 | 1 | S → T in AAA73867. Ref.1 | ||||||
Sequences
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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: 1398087] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. |
| [2] | "Complete sequence of Clostridium cellulolyticum H10." 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. Richardson P.Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. |
| [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: 8223599] [Abstract] Cited for: PROTEIN SEQUENCE OF 33-37, CHARACTERIZATION. Strain: JM83. |
Cross-references
Sequence databases | |
|---|---|
| M87018 Genomic DNA. Translation: AAA73867.1. CP001348 Genomic DNA. Translation: ACL75109.1. | |
| PIR | JC1299. |
3D structure databases | |
| HSSP | HSSP built from PDB template 1IS9 based on UniProtKB P04955. |
| ModBase | Search... |
Protein family/group databases | |
| CAZy | GH8. Glycoside Hydrolase Family 8. |
Enzyme and pathway databases | |
| BRENDA | 3.2.1.4. 97402. |
Family and domain databases | |
| PROSITE | PS00448. CLOS_CELLULOSOME_RPT. 1 hit. PS00018. EF_HAND_1. 2 hits. Uncertain. PS00812. GLYCOSYL_HYDROL_F8. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | GUNC_CLOCE | ||||||||
| Accession | Primary (citable) accession number: P37699 Secondary accession number(s): B8I7V2 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes) | ||||||||
Relevant documents
| Glycosyl hydrolases Classification of glycosyl hydrolase families and list of entries |
| PATHWAY comments Index of metabolic and biosynthesis pathways |
| SIMILARITY comments Index of protein domains and families |

Clusters with


