A3M394 (ASPD_ACIBT) Reviewed, UniProtKB/Swiss-Prot
Last modified
December 14, 2011.
Version 41.
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 | Acinetobacter baumannii (strain ATCC 17978 / NCDC KC 755) [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 400667 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Proteobacteria › Gammaproteobacteria › Pseudomonadales › Moraxellaceae › Acinetobacter › Acinetobacter calcoaceticus/baumannii complex |
Protein attributes
| Sequence length | 263 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 – 263 | 263 | Probable L-aspartate dehydrogenase HAMAP MF_01265 | PRO_1000140084 | |||||
Sites | |||||||||
| Active site | 216 | 1 | By similarity | ||||||
| Binding site | 120 | 1 | NAD; via amide nitrogen By similarity | ||||||
| Binding site | 186 | 1 | NAD By similarity | ||||||
Sequences
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References
| [1] | "New insights into Acinetobacter baumannii pathogenesis revealed by high-density pyrosequencing and transposon mutagenesis." Smith M.G., Gianoulis T.A., Pukatzki S., Mekalanos J.J., Ornston L.N., Gerstein M., Snyder M. Genes Dev. 21:601-614(2007) [PubMed: 17344419] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 17978 / NCDC KC 755. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | CP000521 Genomic DNA. Translation: ABO11388.2. |
| RefSeq | YP_001083990.2. NC_009085.1. |
3D structure databases | |
| ProteinModelPortal | A3M394. |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | A3M394. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| GeneID | 4917096. |
| GenomeReviews | Gene locus A1S_0956 in contig CP000521_GR. |
| KEGG | acb:A1S_0956. |
| NMPDR | fig|400667.4.peg.982. |
| PATRIC | 20718112. VBIAciBau103176_0970. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| eggNOG | COG1712. |
| HOGENOM | HBG649642. |
| 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_ACIBT | ||||||||
| Accession | Primary (citable) accession number: A3M394 | ||||||||
| 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 |

Clusters with