O05508 (GMUD_BACSU) Reviewed, UniProtKB/Swiss-Prot
Last modified
May 1, 2013.
Version 80.
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: 6-phospho-beta-glucosidase GmuD EC=3.2.1.86 Alternative name(s): Aryl-phospho-beta-D-glucosidase BglD Glucomannan utilization protein D | ||||||
| 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 | 465 AA. |
| Sequence status | Complete. |
| Protein existence | Evidence at protein level |
General annotation (Comments)
| Function | Phospho-beta-D-glucosidase that seems to be involved in the degradation of glucomannan. Is also capable of hydrolyzing aryl-phospho-beta-D-glucosides, although very weakly, and plays only a minor role, if any, in the degradation of these substrates in vivo. Ref.3 Ref.4 |
| Catalytic activity | 6-phospho-beta-D-glucosyl-(1,4)-D-glucose + H2O = D-glucose + D-glucose 6-phosphate. |
| Developmental stage | Expressed at only a very low level in exponential-phase cells and germinating spores, but is expressed at a higher levels upon entry into the stationary phase of growth. Ref.3 |
| Induction | Up-regulated by konjac glucomannan and by cellobiose and mannobiose, the possible degradation products of glucomannan. Repressed by glucose via the carbon catabolite repression system. Also repressed by GmuR. Is not induced by aryl-beta-D-glucosides such as arbutin or salicin. Ref.3 Ref.4 |
| Sequence similarities | Belongs to the glycosyl hydrolase 1 family. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Carbohydrate metabolism Polysaccharide degradation |
| Molecular function | Glycosidase Hydrolase |
| Technical term | Complete proteome Reference proteome |
| Gene Ontology (GO) | |
| Biological_process | polysaccharide catabolic process Inferred from electronic annotation. Source: UniProtKB-KW |
| Molecular_function | 6-phospho-beta-glucosidase activity Inferred from electronic annotation. Source: EC |
| Complete GO annotation... | |
Sequence annotation (Features)
Sequences
| ||||||||||||||||||
References
| « Hide 'large scale' references | |
| [1] | "Nucleotide sequence and analysis of the phoB-rrnE-groESL region of the Bacillus subtilis chromosome." Sadaie Y., Yata K., Fujita M., Sagai H., Itaya M., Kasahara Y., Ogasawara N. Microbiology 143:1861-1866(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: 168 / JH642. |
| [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] | "Identification of aryl-phospho-beta-D-glucosidases in Bacillus subtilis." Setlow B., Cabrera-Hernandez A., Cabrera-Martinez R.M., Setlow P. Arch. Microbiol. 181:60-67(2004) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION AS AN ARYL-PHOSPHO-BETA-D-GLUCOSIDASE, DEVELOPMENTAL STAGE, INDUCTION. Strain: 168 / PS832. |
| [4] | "Glucomannan utilization operon of Bacillus subtilis." Sadaie Y., Nakadate H., Fukui R., Yee L.M., Asai K. FEMS Microbiol. Lett. 279:103-109(2008) [PubMed] [Europe PMC] [Abstract] Cited for: INDUCTION BY GLUCOMANNAN, FUNCTION IN GLUCOMANNAN UTILIZATION. Strain: 168. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | D88802 Genomic DNA. Translation: BAA19708.1. AL009126 Genomic DNA. Translation: CAB12403.1. |
| PIR | D69785. |
| RefSeq | NP_388465.1. NC_000964.3. |
3D structure databases | |
| HSSP | HSSP built from PDB template 1PBG based on UniProtKB P11546. |
| ProteinModelPortal | O05508. |
| SMR | O05508. Positions 6-465. |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | 224308.BSU05840. |
Protein family/group databases | |
| CAZy | GH1. Glycoside Hydrolase Family 1. |
Proteomic databases | |
| PaxDb | O05508. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| EnsemblBacteria | CAB12403; CAB12403; BSU05840. |
| GeneID | 939872. |
| KEGG | bsu:BSU05840. |
| PATRIC | 18972784. VBIBacSub10457_0613. |
Organism-specific databases | |
| GenoList | BSU05840. [Micado] |
Phylogenomic databases | |
| eggNOG | COG2723. |
| HOGENOM | HOG000088632. |
| KO | K01223. |
| OMA | HRISIVL. |
| ProtClustDB | CLSK873751. |
Enzyme and pathway databases | |
| BioCyc | BSUB:BSU05840-MONOMER. |
Family and domain databases | |
| Gene3D | 3.20.20.80. 1 hit. |
| InterPro | IPR001360. Glyco_hydro_1. IPR018120. Glyco_hydro_1_AS. IPR013781. Glyco_hydro_catalytic_dom. IPR017853. Glycoside_hydrolase_SF. [Graphical view] |
| PANTHER | PTHR10353. PTHR10353. 1 hit. |
| Pfam | PF00232. Glyco_hydro_1. 1 hit. [Graphical view] |
| PRINTS | PR00131. GLHYDRLASE1. |
| SUPFAM | SSF51445. Glyco_hydro_cat. 1 hit. |
| PROSITE | PS00572. GLYCOSYL_HYDROL_F1_1. 1 hit. PS00653. GLYCOSYL_HYDROL_F1_2. False negative. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | GMUD_BACSU | ||||||||
| Accession | Primary (citable) accession number: O05508 Secondary accession number(s): Q797D9 | ||||||||
| Entry history |
| ||||||||
| 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
