Reviewed,
UniProtKB/Swiss-Prot P15329 (GUNX_CLOTM)
Last modified
May 5, 2009.
Version 56.
History...
Clusters with 100%,
90%,
50% identity |
Documents (2) |
Third-party data |
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Names and origin
| Protein names | Recommended name: Putative endoglucanase X Short name=EGX EC=3.2.1.4 Alternative name(s): Endo-1,4-beta-glucanase Cellulase | ||
| Gene names |
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| Organism | Clostridium thermocellum | ||
| Taxonomic identifier | 1515 [NCBI] | ||
| Taxonomic lineage | Bacteria › Firmicutes › Clostridia › Clostridiales › Clostridiaceae › Clostridium |
Protein attributes
| Sequence length | 224 AA. |
| Sequence status | Fragment. |
| Sequence processing | The displayed sequence is not processed. |
| Protein existence | Evidence 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. |
| 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. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Carbohydrate metabolism Cellulose degradation Polysaccharide degradation |
| Domain | Repeat |
| Molecular function | Glycosidase Hydrolase |
| Technical term | 3D-structure |
| Gene Ontology (GO) | |
| Biological process | cellulose catabolic process Inferred from electronic annotation. Source: UniProtKB-KW lipid metabolic processInferred from electronic annotation. Source: InterPro |
| Molecular function | cellulase activity Inferred from electronic annotation. Source: EC hydrolase activity, acting on ester bondsInferred from electronic annotation. Source: InterPro |
| Complete GO annotation... | |
Sequence annotation (Features)
Sequences
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References
| [1] | "Conserved reiterated domains in Clostridium thermocellum endoglucanases are not essential for catalytic activity." Hall J., Hazlewood G.P., Barker P.J., Gilbert H.J. Gene 69:29-38(1988) [PubMed: 3066698] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| M22759 Genomic DNA. Translation: AAA23223.1. | |||||||||||||
| PIR | A30476. | ||||||||||||
3D structure databases | |||||||||||||
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| ModBase | Search... | ||||||||||||
Enzyme and pathway databases | |||||||||||||
| BRENDA | 3.2.1.4. 97464. | ||||||||||||
Family and domain databases | |||||||||||||
| InterPro | IPR016134. Cellulos_enz_dockerin_1. IPR002105. Cellulos_enz_dockerin_1_Ca-bd. IPR018242. Dockerin_1. IPR018247. EF_HAND_1. IPR013831. Esterase_SGNH_hydro-type_subgr. IPR001087. Lipase_GDSL. [Graphical view] | ||||||||||||
| Gene3D | G3DSA:1.10.1330.10. Cellulos_enz_dockerin_1. 1 hit. G3DSA:3.40.50.1110. Esterase_SGNH_hydro-type_subgr. 1 hit. | ||||||||||||
| Pfam | PF00404. Dockerin_1. 2 hits. PF00657. Lipase_GDSL. 1 hit. [Graphical view] | ||||||||||||
| PROSITE | PS00448. CLOS_CELLULOSOME_RPT. 2 hits. PS00018. EF_HAND_1. 1 hit. Uncertain. [Graphical view] | ||||||||||||
| ProtoNet | Search... | ||||||||||||
Entry information
| Entry name | GUNX_CLOTM | ||||||||
| Accession | Primary (citable) accession number: P15329 | ||||||||
| 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 |
| PDB cross-references Index of Protein Data Bank (PDB) cross-references |

Clusters with


