Q8TZ45 (ASPD_METKA) Reviewed, UniProtKB/Swiss-Prot
Last modified
May 1, 2013.
Version 70.
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 | Methanopyrus kandleri (strain AV19 / DSM 6324 / JCM 9639 / NBRC 100938) [Reference proteome] [HAMAP] | ||||
| Taxonomic identifier | 190192 [NCBI] | ||||
| Taxonomic lineage | Archaea › Euryarchaeota › Methanopyri › Methanopyrales › Methanopyraceae › Methanopyrus › ![]() |
Protein attributes
| Sequence length | 262 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 Reference 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 – 262 | 262 | Probable L-aspartate dehydrogenase HAMAP-Rule MF_01265 | PRO_0000144897 | |||||
Sites | |||||||||
| Active site | 213 | 1 | By similarity | ||||||
| Binding site | 128 | 1 | NAD; via amide nitrogen By similarity | ||||||
| Binding site | 183 | 1 | NAD By similarity | ||||||
Sequences
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References
| [1] | "The complete genome of hyperthermophile Methanopyrus kandleri AV19 and monophyly of archaeal methanogens." Slesarev A.I., Mezhevaya K.V., Makarova K.S., Polushin N.N., Shcherbinina O.V., Shakhova V.V., Belova G.I., Aravind L., Natale D.A., Rogozin I.B., Tatusov R.L., Wolf Y.I., Stetter K.O., Malykh A.G., Koonin E.V., Kozyavkin S.A. Proc. Natl. Acad. Sci. U.S.A. 99:4644-4649(2002) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: AV19 / DSM 6324 / JCM 9639 / NBRC 100938. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | AE009439 Genomic DNA. Translation: AAM01311.1. |
| RefSeq | NP_613381.1. NC_003551.1. |
3D structure databases | |
| ProteinModelPortal | Q8TZ45. |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | 190192.MK0094. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| EnsemblBacteria | AAM01311; AAM01311; MK0094. |
| GeneID | 1477397. |
| KEGG | mka:MK0094. |
Phylogenomic databases | |
| eggNOG | COG1712. |
| HOGENOM | HOG000206326. |
| KO | K06989. |
| OMA | VVECAPA. |
Enzyme and pathway databases | |
| 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. IPR022487. Asp_DH_NAD_synth_arc. 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. |
| TIGRFAMs | TIGR03855. NAD_NadX. 1 hit. |
| ProtoNet | Search... |
Entry information
| Entry name | ASPD_METKA | ||||||||
| Accession | Primary (citable) accession number: Q8TZ45 | ||||||||
| 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
