Q8PV99 (ASPD_METMA) Reviewed, UniProtKB/Swiss-Prot
Last modified
November 16, 2011.
Version 62.
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 | Methanosarcina mazei (strain ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM 11833 / OCM 88) (Methanosarcina frisia) [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 192952 [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. |
| Sequence caution | The sequence AAM31768.1 differs from that shown. Reason: Erroneous initiation. |
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 – 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
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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 11833 / OCM 88. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | AE008384 Genomic DNA. Translation: AAM31768.1. Different initiation. |
| RefSeq | NP_634096.1. NC_003901.1. |
3D structure databases | |
| ProteinModelPortal | Q8PV99. |
| ModBase | Search... |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | 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. |
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. IPR022487. Asp_DH_NAD_synth_arc. 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. |
| TIGRFAMs | TIGR03855. NAD_NadX. 1 hit. |
| ProtoNet | Search... |
Entry information
| Entry name | ASPD_METMA | ||||||||
| Accession | Primary (citable) accession number: Q8PV99 | ||||||||
| 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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