Reviewed,
UniProtKB/Swiss-Prot Q8PV99 (ASPD_METMA)
Last modified
January 19, 2010.
Version 49.
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 | Methanosarcina mazei (Methanosarcina frisia) [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 2209 [NCBI] | ||||
| Taxonomic lineage | Archaea › Euryarchaeota › Methanomicrobia › Methanosarcinales › Methanosarcinaceae › Methanosarcina |
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 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: 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 – 271 | 271 | Probable L-aspartate dehydrogenase HAMAP MF_01265 | PRO_0000144898 | |||||
Sites | |||||||||
| Active site | 222 | 1 | By similarity | ||||||
| Binding site | 124 | 1 | NAD; via amide nitrogen By similarity | ||||||
| Binding site | 192 | 1 | NAD By similarity | ||||||
Sequences
| ||||||||||||||||||
References
| [1] | "The genome of Methanosarcina mazei: evidence for lateral gene transfer between Bacteria and Archaea." Deppenmeier U., Johann A., Hartsch T., Merkl R., Schmitz R.A., Martinez-Arias R., Henne A., Wiezer A., Baeumer S., Jacobi C., Brueggemann H., Lienard T., Christmann A., Boemecke M., Steckel S., Bhattacharyya A., Lykidis A., Overbeek R. Gottschalk G.J. Mol. Microbiol. Biotechnol. 4:453-461(2002) [PubMed: 12125824] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM 11883 / OCM 88. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | AE008384 Genomic DNA. Translation: AAM31768.1. Different initiation. |
| RefSeq | NP_634096.1. |
3D structure databases | |
| SMR | Q8PV99. Positions 2-269. |
| ModBase | Search... |
Genome annotation databases | |
| GeneID | 1480414. |
| GenomeReviews | Gene locus MM_2072 in contig AE008384_GR. |
| KEGG | mma:MM_2072. |
| NMPDR | fig|192952.1.peg.2072. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| HOGENOM | HBG649642. |
| OMA | ECAGHSA. |
Enzyme and pathway databases | |
| BioCyc | MMAZ192952:MM2072-MONOMER. |
| BRENDA | 1.4.1.21. 261165. |
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. |
| 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_METMA | ||||||||
| Accession | Primary (citable) accession number: Q8PV99 | ||||||||
| 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


