P46320 (LICH_BACSU) Reviewed, UniProtKB/Swiss-Prot
Last modified
May 1, 2013.
Version 97.
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: Probable 6-phospho-beta-glucosidase EC=3.2.1.86 | ||||||
| Gene names |
| ||||||
| Organism | Bacillus subtilis (strain 168) [Reference proteome] [HAMAP] | ||||||
| Taxonomic identifier | 224308 [NCBI] | ||||||
| Taxonomic lineage | Bacteria › Firmicutes › Bacilli › Bacillales › Bacillaceae › Bacillus › ![]() |
Protein attributes
| Sequence length | 442 AA. |
| Sequence status | Complete. |
| 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 Reference 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 metal ion bindingInferred from electronic annotation. Source: UniProtKB-KW nucleotide bindingInferred from electronic annotation. Source: InterPro oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptorInferred from electronic annotation. Source: InterPro |
| 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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-305. Strain: 168 / BGSC1A1. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | Z49992 Genomic DNA. Translation: CAA90288.1. AL009126 Genomic DNA. Translation: CAB15882.1. D83026 Genomic DNA. Translation: BAA11746.1. |
| PIR | S57762. |
| RefSeq | NP_391735.1. NC_000964.3. |
3D structure databases | |
| ProteinModelPortal | P46320. |
| SMR | P46320. Positions 5-439. |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | 224308.BSU38560. |
Protein family/group databases | |
| CAZy | GH4. Glycoside Hydrolase Family 4. |
Proteomic databases | |
| PaxDb | P46320. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| EnsemblBacteria | CAB15882; CAB15882; BSU38560. |
| GeneID | 937373. |
| KEGG | bsu:BSU38560. |
| PATRIC | 18979760. VBIBacSub10457_4042. |
Organism-specific databases | |
| GenoList | BSU38560. [Micado] |
Phylogenomic databases | |
| eggNOG | COG1486. |
| HOGENOM | HOG000239811. |
| KO | K01222. |
| OMA | AKDERIP. |
| ProtClustDB | CLSK2752558. |
Enzyme and pathway databases | |
| BioCyc | BSUB:BSU38560-MONOMER. |
Family and domain databases | |
| Gene3D | 3.40.50.720. 1 hit. 3.90.110.10. 1 hit. |
| InterPro | IPR019802. GlycHydrolase_4_CS. IPR001088. Glyco_hydro_4. IPR022616. Glyco_hydro_4_C. IPR015955. Lactate_DH/Glyco_Ohase_4_C. IPR016040. NAD(P)-bd_dom. [Graphical view] |
| Pfam | PF02056. Glyco_hydro_4. 1 hit. PF11975. Glyco_hydro_4C. 1 hit. [Graphical view] |
| PRINTS | PR00732. GLHYDRLASE4. |
| SUPFAM | SSF56327. Lactate_DH/Glyco_hydro_4_C. 1 hit. |
| 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 program | Prokaryotic Protein Annotation Program | ||||||||
Relevant documents
| Glycosyl hydrolases Classification of glycosyl hydrolase families and list of entries |
| Bacillus subtilis Bacillus subtilis (strain 168): entries, gene names and cross-references to SubtiList |
| SIMILARITY comments Index of protein domains and families |

Clusters with
