Reviewed,
UniProtKB/Swiss-Prot P46320 (LICH_BACSU)
Last modified
June 16, 2009.
Version 69.
History...
Clusters with 100%,
90%,
50% identity |
Documents (3) |
Third-party data |
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Names and origin
| Protein names | Recommended name: Probable 6-phospho-beta-glucosidase EC=3.2.1.86 | ||||||
| Gene names |
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| Organism | Bacillus subtilis [Complete proteome] [HAMAP] | ||||||
| Taxonomic identifier | 1423 [NCBI] | ||||||
| Taxonomic lineage | Bacteria › Firmicutes › Bacillales › Bacillaceae › Bacillus |
Protein attributes
| Sequence length | 442 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is not processed. |
| Protein existence | Evidence at transcript level. |
General annotation (Comments)
| Function | Hydrolyzes phospho-beta-glucosides Probable. |
| Catalytic activity | 6-phospho-beta-D-glucosyl-(1,4)-D-glucose + H2O = D-glucose + D-glucose 6-phosphate. |
| Cofactor | NAD By similarity. Divalent metal ion By similarity. |
| Induction | Induced by lichenan, lichenan hydrolysate and cellobiose. Subject to carbon catabolite repression. |
| Sequence similarities | Belongs to the glycosyl hydrolase 4 family. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Carbohydrate metabolism |
| Ligand | Manganese Metal-binding NAD |
| Molecular function | Glycosidase Hydrolase |
| Technical term | Complete proteome |
| Gene Ontology (GO) | |
| Biological process | carbohydrate metabolic process Inferred from electronic annotation. Source: UniProtKB-KW |
| Molecular function | 6-phospho-beta-glucosidase activity Inferred from electronic annotation. Source: EC manganese ion bindingInferred from electronic annotation. Source: UniProtKB-KW |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 442 | 442 | Probable 6-phospho-beta-glucosidase | PRO_0000169861 | |||||
Regions | |||||||||
| Nucleotide binding | 5 – 73 | 69 | NAD By similarity | ||||||
Sites | |||||||||
| Active site | 256 | 1 | Proton acceptor By similarity | ||||||
| Metal binding | 172 | 1 | Manganese By similarity | ||||||
| Metal binding | 202 | 1 | Manganese By similarity | ||||||
| Binding site | 96 | 1 | Substrate By similarity | ||||||
| Binding site | 150 | 1 | Substrate By similarity | ||||||
| Site | 112 | 1 | Increases basicity of active site Tyr By similarity | ||||||
Sequences
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References
| « Hide 'large scale' references | |
| [1] | "Identification and characterization of a new beta-glucoside utilization system in Bacillus subtilis." Tobisch S., Glaser P., Krueger S., Hecker M. J. Bacteriol. 179:496-506(1997) [PubMed: 8990303] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: 168. |
| [2] | "The complete genome sequence of the Gram-positive bacterium Bacillus subtilis." Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V., Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R., Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S., Bruschi C.V. Danchin A.Nature 390:249-256(1997) [PubMed: 9384377] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 168. |
| [3] | "Sequencing of a 65 kb region of the Bacillus subtilis genome containing the lic and cel loci, and creation of a 177 kb contig covering the gnt-sacXY region." Yoshida K., Shindo K., Sano H., Seki S., Fujimura M., Yanai N., Miwa Y., Fujita Y. Microbiology 142:3113-3123(1996) [PubMed: 8969509] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-305. Strain: 168 / BGSC1A1. |
Cross-references
Sequence databases | |
|---|---|
| Z49992 Genomic DNA. Translation: CAA90288.1. AL009126 Genomic DNA. Translation: CAB15882.1. D83026 Genomic DNA. Translation: BAA11746.1. | |
| PIR | S57762. |
| RefSeq | NP_391735.1. |
3D structure databases | |
| SMR | P46320. Positions 5-439. |
| ModBase | Search... |
Protein family/group databases | |
| CAZy | GH4. Glycoside Hydrolase Family 4. |
Genome annotation databases | |
| GeneID | 937373. |
| GenomeReviews | Gene locus BSU38560 in contig AL009126_GR. |
| KEGG | bsu:BSU38560. |
| NMPDR | fig|224308.1.peg.3861. |
Organism-specific databases | |
| SubtiList | BG11350. licH. [Micado] |
| CMR | Search... |
Phylogenomic databases | |
| HOGENOM | P46320. |
| OMA | P46320. AKLDIIF. |
Enzyme and pathway databases | |
| BioCyc | BSUB224308:BSU3852-MON. |
| BRENDA | 3.2.1.86. 150. |
Family and domain databases | |
| InterPro | IPR019802. GlycHydrolase_4_CS. IPR001088. Glyco_hydro_4. IPR015955. Lactate_DH/Glyco_Ohase_4_C. [Graphical view] |
| Gene3D | G3DSA:3.90.110.10. lact_mal_DH. 1 hit. |
| Pfam | PF02056. Glyco_hydro_4. 1 hit. [Graphical view] |
| PRINTS | PR00732. GLHYDRLASE4. |
| ProDom | PD006892. Glyco_hydro_4. 1 hit. [Graphical view] [Entries sharing at least one domain] |
| PROSITE | PS01324. GLYCOSYL_HYDROL_F4. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | LICH_BACSU | ||||||||
| Accession | Primary (citable) accession number: P46320 | ||||||||
| 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
| Bacillus subtilis Bacillus subtilis (strain 168): entries, gene names and cross-references to SubtiList |
| Glycosyl hydrolases Classification of glycosyl hydrolase families and list of entries |
| SIMILARITY comments Index of protein domains and families |

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