P07999 (DHGB_BACME) Reviewed, UniProtKB/Swiss-Prot
Last modified
December 14, 2011.
Version 78.
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: Glucose 1-dehydrogenase B EC=1.1.1.47 | ||
| Gene names |
| ||
| Organism | Bacillus megaterium | ||
| Taxonomic identifier | 1404 [NCBI] | ||
| Taxonomic lineage | Bacteria › Firmicutes › Bacillales › Bacillaceae › Bacillus |
Protein attributes
| Sequence length | 262 AA. |
| Sequence status | Complete. |
| Protein existence | Evidence at protein level |
General annotation (Comments)
| Catalytic activity | Beta-D-glucose + NAD(P)+ = D-glucono-1,5-lactone + NAD(P)H. |
| Subunit structure | Homotetramer. |
| Developmental stage | Expressed during sporulation. |
| Sequence similarities | Belongs to the short-chain dehydrogenases/reductases (SDR) family. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Sporulation |
| Ligand | NADP |
| Molecular function | Oxidoreductase |
| Technical term | Direct protein sequencing |
| Gene Ontology (GO) | |
| Biological process | sporulation resulting in formation of a cellular spore Inferred from electronic annotation. Source: UniProtKB-KW |
| Molecular function | glucose 1-dehydrogenase [NAD(P)] activity Inferred from electronic annotation. Source: EC nucleotide bindingInferred from electronic annotation. Source: InterPro |
| Complete GO annotation... | |
Sequence annotation (Features)
Sequences
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References
| [1] | "Complete amino acid sequence of glucose dehydrogenase from Bacillus megaterium." Jany K.-D., Ulmer W., Froschle M., Pfleiderer G. FEBS Lett. 165:6-10(1984) [PubMed: 6420184] [Abstract] Cited for: PROTEIN SEQUENCE. |
| [2] | "Identification and isolation of glucose dehydrogenase genes of Bacillus megaterium M1286 and their expression in Escherichia coli." Heilmann H.J., Maegert H.-J., Gassen H.G. Eur. J. Biochem. 174:485-490(1988) [PubMed: 3134196] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-52, SEQUENCE REVISION TO 207 AND 258. Strain: M1286. |
| [3] | "Evidence for an essential histidine residue in glucose dehydrogenase from Bacillus megaterium and sequence analysis of the peptides labeled with bromoacetyl pyridine." Ulmer W., Froschle M., Jany K.-D. Eur. J. Biochem. 136:183-194(1983) [PubMed: 6413208] [Abstract] Cited for: PROTEIN SEQUENCE OF 27-204. |
| [4] | "Tyrosine modification of glucose dehydrogenase from Bacillus megaterium. Effect of tetranitromethane on the enzyme in the tetrameric and monomeric state." Froschle M., Ulmer W., Jany K.-D. Eur. J. Biochem. 142:533-540(1984) [PubMed: 6432532] [Abstract] Cited for: PROTEIN SEQUENCE OF 218-262. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |
|---|---|
| PIR | A23260. S01227. S02299. |
3D structure databases | |
| ProteinModelPortal | P07999. |
| SMR | P07999. Positions 1-262. |
| ModBase | Search... |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Family and domain databases | |
| InterPro | IPR002198. DH_sc/Rdtase_SDR. IPR002347. Glc/ribitol_DH. IPR016040. NAD(P)-bd_dom. IPR020904. Sc_DH/Rdtase_CS. [Graphical view] |
| Gene3D | G3DSA:3.40.50.720. NAD(P)-bd. 1 hit. |
| Pfam | PF00106. adh_short. 1 hit. [Graphical view] |
| PRINTS | PR00081. GDHRDH. PR00080. SDRFAMILY. |
| PROSITE | PS00061. ADH_SHORT. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | DHGB_BACME | ||||||||
| Accession | Primary (citable) accession number: P07999 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Prokaryotic Protein Annotation Program | ||||||||
Relevant documents
| SIMILARITY comments Index of protein domains and families |

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