Q73B03 (Q73B03_BACC1) Unreviewed, UniProtKB/TrEMBL
Last modified
January 25, 2012.
Version 53.
History...
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry infoCustomize order
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry infoCustomize orderNames and origin
| Protein names | Recommended name: Glutamate dehydrogenase PIRNR PIRNR000185 | ||||
| Gene names |
| ||||
| Organism | Bacillus cereus (strain ATCC 10987) [Complete proteome] [HAMAP] EMBL AAS40546.1 | ||||
| Taxonomic identifier | 222523 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Firmicutes › Bacillales › Bacillaceae › Bacillus › Bacillus cereus group |
Protein attributes
| Sequence length | 428 AA. |
| Sequence status | Complete. |
| Protein existence | Inferred from homology |
General annotation (Comments)
| Sequence similarities | Belongs to the Glu/Leu/Phe/Val dehydrogenases family. PIRNR PIRNR000185 |
Ontologies
| Keywords | |
|---|---|
| Molecular function | Oxidoreductase PIRNR PIRNR000185 EMBL AAS40546.1 |
| Technical term | Complete proteome |
| Gene Ontology (GO) | |
| Biological process | cellular amino acid metabolic process Inferred from electronic annotation. Source: InterPro |
| Molecular function | nucleotide binding Inferred from electronic annotation. Source: InterPro oxidoreductase activity, acting on the CH-NH2 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 | ||||
Sites | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Active site | 120 | 1 | By similarity PIRSR PIRSR000185-1 | ||||||
Sequences
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References
| [1] | "The genome sequence of Bacillus cereus ATCC 10987 reveals metabolic adaptations and a large plasmid related to Bacillus anthracis pXO1." Rasko D.A., Ravel J., Oekstad O.A., Helgason E., Cer R.Z., Jiang L., Shores K.A., Fouts D.E., Tourasse N.J., Angiuoli S.V., Kolonay J.F., Nelson W.C., Kolstoe A.-B., Fraser C.M., Read T.D. Nucleic Acids Res. 32:977-988(2004) [PubMed: 14960714] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | AE017194 Genomic DNA. Translation: AAS40546.1. |
| RefSeq | NP_977938.1. NC_003909.8. |
3D structure databases | |
| HSSP | HSSP built from PDB template 1B26 based on UniProtKB P96110. |
| ProteinModelPortal | Q73B03. |
| SMR | Q73B03. Positions 24-428. |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | Q73B03. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| EnsemblBacteria | EBBACT00000026730; EBBACP00000026080; EBBACG00000026721. |
| GeneID | 2751351. |
| GenomeReviews | Gene locus BCE_1617 in contig AE017194_GR. |
| KEGG | bca:BCE_1617. |
| PATRIC | 18852065. VBIBacCer118379_1536. |
| TIGR | BCE_1617. |
Phylogenomic databases | |
| eggNOG | COG0334. |
| GeneTree | EBGT00050000001222. |
| HOGENOM | HBG590661. |
| OMA | EGFRVQH. |
| ProtClustDB | CLSK918002. |
Family and domain databases | |
| InterPro | IPR006095. Glu/Leu/Phe/Val_DH. IPR006096. Glu/Leu/Phe/Val_DH_C. IPR006097. Glu/Leu/Phe/Val_DH_dimer_dom. IPR014362. Glu_DH. IPR016040. NAD(P)-bd_dom. [Graphical view] |
| Gene3D | G3DSA:3.40.50.720. NAD(P)-bd. 1 hit. |
| KO | K00260. |
| Pfam | PF00208. ELFV_dehydrog. 1 hit. PF02812. ELFV_dehydrog_N. 1 hit. [Graphical view] |
| PIRSF | PIRSF000185. Glu_DH. 1 hit. |
| PRINTS | PR00082. GLFDHDRGNASE. |
| SMART | SM00839. ELFV_dehydrog. 1 hit. [Graphical view] |
| PROSITE | PS00074. GLFV_DEHYDROGENASE. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | Q73B03_BACC1 | ||||||||
| Accession | Primary (citable) accession number: Q73B03 | ||||||||
| Entry history |
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| Entry status | Unreviewed (UniProtKB/TrEMBL) | ||||||||

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