B3R8S4 (ASPD_CUPTR) Reviewed, UniProtKB/Swiss-Prot
Last modified
January 25, 2012.
Version 28.
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 L-aspartate dehydrogenase EC=1.4.1.21 | ||||
| Gene names |
| ||||
| Organism | Cupriavidus taiwanensis (strain R1 / LMG 19424) (Ralstonia taiwanensis (strain LMG 19424)) [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 164546 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Proteobacteria › Betaproteobacteria › Burkholderiales › Burkholderiaceae › Cupriavidus |
Protein attributes
| Sequence length | 266 AA. |
| Sequence status | Complete. |
| Protein existence | Inferred from homology |
General annotation (Comments)
| Function | Specifically catalyzes the NAD or NADP-dependent dehydrogenation of L-aspartate to iminoaspartate By similarity. HAMAP MF_01265 |
| Catalytic activity | L-aspartate + H2O + NAD(P)+ = oxaloacetate + NH3 + NAD(P)H. HAMAP MF_01265 |
| Pathway | Cofactor biosynthesis; NAD(+) biosynthesis; iminoaspartate from L-aspartate (dehydrogenase route): step 1/1. HAMAP MF_01265 |
| Miscellaneous | The iminoaspartate product is unstable in aqueous solution and can decompose to oxaloacetate and ammonia By similarity. HAMAP MF_01265 |
| Sequence similarities | Belongs to the L-aspartate dehydrogenase family. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Pyridine nucleotide biosynthesis |
| Ligand | NAD NADP |
| Molecular function | Oxidoreductase |
| Technical term | Complete proteome |
| Gene Ontology (GO) | |
| Biological process | NAD biosynthetic process Inferred from electronic annotation. Source: InterPro NADP catabolic processInferred from electronic annotation. Source: InterPro |
| Molecular function | NADP binding Inferred from electronic annotation. Source: InterPro aspartate dehydrogenase activityInferred from electronic annotation. Source: EC |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 266 | 266 | Probable L-aspartate dehydrogenase HAMAP MF_01265 | PRO_1000140086 | |||||
Sites | |||||||||
| Active site | 219 | 1 | By similarity | ||||||
| Binding site | 123 | 1 | NAD; via amide nitrogen By similarity | ||||||
| Binding site | 189 | 1 | NAD By similarity | ||||||
Sequences
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References
| [1] | "Genome sequence of the beta-rhizobium Cupriavidus taiwanensis and comparative genomics of rhizobia." Amadou C., Pascal G., Mangenot S., Glew M., Bontemps C., Capela D., Carrere S., Cruveiller S., Dossat C., Lajus A., Marchetti M., Poinsot V., Rouy Z., Servin B., Saad M., Schenowitz C., Barbe V., Batut J., Medigue C., Masson-Boivin C. Genome Res. 18:1472-1483(2008) [PubMed: 18490699] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: R1 / LMG 19424. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | CU633750 Genomic DNA. Translation: CAQ71192.1. |
| RefSeq | YP_002007253.1. NC_010530.1. |
3D structure databases | |
| ProteinModelPortal | B3R8S4. |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | B3R8S4. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| GeneID | 6455299. |
| GenomeReviews | Gene locus RALTA_B0572 in contig CU633750_GR. |
| KEGG | cti:RALTA_B0572. |
| PATRIC | 21534923. VBICupTai42494_4076. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| HOGENOM | HBG649642. |
| OMA | ECAGHSA. |
| ProtClustDB | PRK13303. |
Family and domain databases | |
| HAMAP | MF_01265. NadX. [Tree] |
| InterPro | IPR005106. Asp/hSer_DH_NAD-bd. IPR002811. Asp_DH. IPR011182. Asp_DH_NAD_syn. IPR020626. Asp_DH_NAD_syn_prok. IPR016040. NAD(P)-bd_dom. [Graphical view] |
| Gene3D | G3DSA:3.40.50.720. NAD(P)-bd. 1 hit. |
| KO | K06989. |
| Pfam | PF01958. DUF108. 1 hit. PF03447. NAD_binding_3. 1 hit. [Graphical view] |
| PIRSF | PIRSF005227. Asp_dh_NAD_syn. 1 hit. |
| ProtoNet | Search... |
Entry information
| Entry name | ASPD_CUPTR | ||||||||
| Accession | Primary (citable) accession number: B3R8S4 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Prokaryotic Protein Annotation Program | ||||||||
Relevant documents
| PATHWAY comments Index of metabolic and biosynthesis pathways |
| SIMILARITY comments Index of protein domains and families |

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