P06564 (GUN_BACS1) Reviewed, UniProtKB/Swiss-Prot
Last modified
May 31, 2011.
Version 84.
History...
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames and origin
| Protein names | Recommended name: Endoglucanase EC=3.2.1.4 Alternative name(s): Alkaline cellulase Endo-1,4-beta-glucanase |
| Organism | Bacillus sp. (strain 1139) |
| Taxonomic identifier | 1411 [NCBI] |
| Taxonomic lineage | Bacteria › Firmicutes › Bacillales › Bacillaceae › Bacillus |
Protein attributes
| Sequence length | 800 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)
| Catalytic activity | Endohydrolysis of (1->4)-beta-D-glucosidic linkages in cellulose, lichenin and cereal beta-D-glucans. |
| Miscellaneous | Alkalophilic Bacillus sp strain 1139 is not a true cellulolytic micro-organism because the enzyme is unable to hydrolyze native cellulose. |
| Sequence similarities | Belongs to the glycosyl hydrolase 5 (cellulase A) family. |
| Biophysicochemical properties | pH dependence: Optimum pH is 9.0. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Carbohydrate metabolism Cellulose degradation Polysaccharide degradation |
| Domain | Signal |
| Molecular function | Glycosidase Hydrolase |
| Technical term | 3D-structure |
| Gene Ontology (GO) | |
| Biological process | cellulose catabolic process Inferred from electronic annotation. Source: UniProtKB-KW |
| Molecular function | cation binding Inferred from electronic annotation. Source: InterPro cellulase activityInferred 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 – 30 | 30 | Potential | ||||||||||||||||||||||||||||||
| Chain | 31 – 800 | 770 | Endoglucanase | PRO_0000007837 | |||||||||||||||||||||||||||||
Sites | |||||||||||||||||||||||||||||||||
| Active site | 190 | 1 | Proton donor By similarity | ||||||||||||||||||||||||||||||
| Active site | 305 | 1 | Nucleophile By similarity | ||||||||||||||||||||||||||||||
Secondary structure | |||||||||||||||||||||||||||||||||
Helix Strand Turn | |||||||||||||||||||||||||||||||||
| Beta strand | 588 – 590 | 3 | |||||||||||||||||||||||||||||||
| Beta strand | 613 – 616 | 4 | |||||||||||||||||||||||||||||||
| Beta strand | 621 – 625 | 5 | |||||||||||||||||||||||||||||||
| Turn | 637 – 640 | 4 | |||||||||||||||||||||||||||||||
| Beta strand | 643 – 647 | 5 | |||||||||||||||||||||||||||||||
| Beta strand | 658 – 669 | 12 | |||||||||||||||||||||||||||||||
| Beta strand | 675 – 681 | 7 | |||||||||||||||||||||||||||||||
| Beta strand | 696 – 698 | 3 | |||||||||||||||||||||||||||||||
| Helix | 700 – 705 | 6 | |||||||||||||||||||||||||||||||
| Beta strand | 713 – 720 | 8 | |||||||||||||||||||||||||||||||
| Beta strand | 735 – 744 | 10 | |||||||||||||||||||||||||||||||
| Beta strand | 750 – 759 | 10 | |||||||||||||||||||||||||||||||
Sequences
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References
| [1] | "Molecular cloning and nucleotide sequence of the alkaline cellulase gene from the alkalophilic Bacillus sp. strain 1139." Fukumori F., Kudo T., Narahashi Y., Horikoshi K. J. Gen. Microbiol. 132:2329-2335(1986) [PubMed: 3098909] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| EMBL GenBank DDBJ | M15743 Genomic DNA. Translation: AAA22305.1. D00066 Genomic DNA. Translation: BAA00045.1. | ||||||||||||
| PIR | A29003. | ||||||||||||
3D structure databases | |||||||||||||
| PDBe RCSB PDB PDBj |
| ||||||||||||
| ProteinModelPortal | P06564. | ||||||||||||
| SMR | P06564. Positions 44-570, 578-761. | ||||||||||||
| ModBase | Search... | ||||||||||||
Protein family/group databases | |||||||||||||
| CAZy | CBM17. Carbohydrate-Binding Module Family 17. CBM28. Carbohydrate-Binding Module Family 28. GH5. Glycoside Hydrolase Family 5. | ||||||||||||
Protocols and materials databases | |||||||||||||
| StructuralBiologyKnowledgebase | Search... | ||||||||||||
Family and domain databases | |||||||||||||
| InterPro | IPR005086. CBM_fam_17/28. IPR008979. Galactose-bd-like. IPR001547. Glyco_hydro_5. IPR018087. Glyco_hydro_5_CS. IPR013781. Glyco_hydro_subgr_catalytic. IPR017853. Glycoside_hydrolase_SF. [Graphical view] | ||||||||||||
| Gene3D | G3DSA:3.20.20.80. Glyco_hydro_cat. 1 hit. | ||||||||||||
| Pfam | PF03424. CBM_17_28. 2 hits. PF00150. Cellulase. 1 hit. [Graphical view] | ||||||||||||
| SUPFAM | SSF49785. Gal_bind_like. 2 hits. SSF51445. Glyco_hydro_cat. 1 hit. | ||||||||||||
| PROSITE | PS00659. GLYCOSYL_HYDROL_F5. 1 hit. [Graphical view] | ||||||||||||
| ProtoNet | Search... | ||||||||||||
Entry information
| Entry name | GUN_BACS1 | ||||||||
| Accession | Primary (citable) accession number: P06564 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Prokaryotic Protein Annotation Program | ||||||||
Relevant documents
| Glycosyl hydrolases Classification of glycosyl hydrolase families and list of entries |
| PDB cross-references Index of Protein Data Bank (PDB) cross-references |
| SIMILARITY comments Index of protein domains and families |

Clusters with