Reviewed,
UniProtKB/Swiss-Prot Q9HYA4 (ASPD_PSEAE)
Last modified
June 16, 2009.
Version 46.
History...
Clusters with 100%,
90%,
50% identity |
Documents (2) |
Third-party data |
Customize display | text xml rdf/xml gff fasta |
Names and origin
| Protein names | Recommended name: Probable L-aspartate dehydrogenase EC=1.4.1.21 | ||||
| Gene names |
| ||||
| Organism | Pseudomonas aeruginosa [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 287 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Proteobacteria › Gammaproteobacteria › Pseudomonadales › Pseudomonadaceae › Pseudomonas |
Protein attributes
| Sequence length | 267 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is not processed. |
| Protein existence | Inferred from homology. |
General annotation (Comments)
| Function | Specifically catalyzes the NAD or NADP-dependent dehydrogenation of L-aspartate to iminoaspartate By similarity. |
| 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. |
| 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 oxidation reductionInferred from electronic annotation. Source: UniProtKB-KW |
| Molecular function | NAD or NADH binding Inferred from electronic annotation. Source: HAMAP NADP or NADPH 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 – 267 | 267 | Probable L-aspartate dehydrogenase HAMAP MF_01265 | PRO_0000144890 | |||||
Sites | |||||||||
| Active site | 220 | 1 | By similarity | ||||||
| Binding site | 124 | 1 | NAD; via amide nitrogen By similarity | ||||||
| Binding site | 190 | 1 | NAD By similarity | ||||||
Sequences
| ||||||||||||||||||
References
| [1] | "Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic pathogen." Stover C.K., Pham X.-Q.T., Erwin A.L., Mizoguchi S.D., Warrener P., Hickey M.J., Brinkman F.S.L., Hufnagle W.O., Kowalik D.J., Lagrou M., Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y., Brody L.L., Coulter S.N., Folger K.R. Olson M.V.Nature 406:959-964(2000) [PubMed: 10984043] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228. |
Cross-references
Sequence databases | |
|---|---|
| AE004091 Genomic DNA. Translation: AAG06893.1. | |
| PIR | G83206. |
| RefSeq | NP_252195.1. |
3D structure databases | |
| ModBase | Search... |
Genome annotation databases | |
| GeneID | 879175. |
| GenomeReviews | Gene locus PA3505 in contig AE004091_GR. |
| KEGG | pae:PA3505. |
| NMPDR | fig|208964.1.peg.3505. |
Organism-specific databases | |
| PseudoCAP | PA3505. |
| CMR | Search... |
Phylogenomic databases | |
| HOGENOM | Q9HYA4. |
| OMA | Q9HYA4. ECAGHSA. |
Enzyme and pathway databases | |
| BioCyc | PAER208964:PA3505-MON. |
| BRENDA | 1.4.1.21. 354. |
Family and domain databases | |
| HAMAP | MF_01265. [Tree] |
| InterPro | IPR005106. Asp/hSer_DH_NAD-bd. IPR002811. Asp_DH. IPR011182. Asp_DH_NAD_syn. [Graphical view] |
| Pfam | PF01958. DUF108. 1 hit. PF03447. NAD_binding_3. 1 hit. [Graphical view] |
| PIRSF | PIRSF005227. Asp_dh_NAD_syn. 1 hit. |
| ProDom | PD017325. Asp_dh. 1 hit. [Graphical view] [Entries sharing at least one domain] |
| ProtoNet | Search... |
Entry information
| Entry name | ASPD_PSEAE | ||||||||
| Accession | Primary (citable) accession number: Q9HYA4 | ||||||||
| Entry history |
| ||||||||
| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes) | ||||||||
Relevant documents
| PATHWAY comments Index of metabolic and biosynthesis pathways |
| SIMILARITY comments Index of protein domains and families |

Clusters with


