Q3JFK2 (ASPD_BURP1) Reviewed, UniProtKB/Swiss-Prot
Last modified
May 29, 2013.
Version 54.
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 |
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| Organism | Burkholderia pseudomallei (strain 1710b) [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 320372 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Proteobacteria › Betaproteobacteria › Burkholderiales › Burkholderiaceae › Burkholderia › pseudomallei group › ![]() |
Protein attributes
| Sequence length | 271 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-Rule MF_01265 |
| Catalytic activity | L-aspartate + H2O + NAD(P)+ = oxaloacetate + NH3 + NAD(P)H. HAMAP-Rule MF_01265 |
| Pathway | Cofactor biosynthesis; NAD(+) biosynthesis; iminoaspartate from L-aspartate (dehydrogenase route): step 1/1. HAMAP-Rule MF_01265 |
| Miscellaneous | The iminoaspartate product is unstable in aqueous solution and can decompose to oxaloacetate and ammonia By similarity. HAMAP-Rule 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: HAMAP NADP catabolic processInferred from electronic annotation. Source: InterPro |
| Molecular_function | NAD binding Inferred from electronic annotation. Source: HAMAP NADP bindingInferred from electronic annotation. Source: HAMAP aspartate dehydrogenase activityInferred from electronic annotation. Source: EC oxidoreductase activity, acting on the CH-NH2 group of donors, NAD or NADP as acceptorInferred from electronic annotation. Source: HAMAP |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 271 | 271 | Probable L-aspartate dehydrogenase HAMAP-Rule MF_01265 | PRO_1000067298 | |||||
Sites | |||||||||
| Active site | 224 | 1 | By similarity | ||||||
| Binding site | 128 | 1 | NAD; via amide nitrogen By similarity | ||||||
| Binding site | 194 | 1 | NAD By similarity | ||||||
Sequences
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References
| [1] | Woods D.E., Nierman W.C. Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 1710b. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | CP000125 Genomic DNA. Translation: ABA53762.1. |
| RefSeq | YP_337651.1. NC_007435.1. |
3D structure databases | |
| ProteinModelPortal | Q3JFK2. |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | 320372.BURPS1710b_A2501. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| EnsemblBacteria | ABA53762; ABA53762; BURPS1710b_A2501. |
| GeneID | 3693319. |
| KEGG | bpm:BURPS1710b_A2501. |
| PATRIC | 19245755. VBIBurPse115837_6708. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| eggNOG | COG1712. |
| HOGENOM | HOG000206326. |
| KO | K06989. |
| OMA | PKTSYLA. |
| ProtClustDB | PRK13303. |
Enzyme and pathway databases | |
| BioCyc | BPSE320372:GBYB-6299-MONOMER. |
| UniPathway | UPA00253; UER00456. |
Family and domain databases | |
| Gene3D | 3.40.50.720. 1 hit. |
| HAMAP | MF_01265. NadX. |
| 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] |
| 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_BURP1 | ||||||||
| Accession | Primary (citable) accession number: Q3JFK2 | ||||||||
| 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
