P80459 (MDH_RHORU) Reviewed, UniProtKB/Swiss-Prot
Last modified
March 6, 2013.
Version 45.
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: Malate dehydrogenase EC=1.1.1.37 | ||
| Gene names |
| ||
| Organism | Rhodospirillum rubrum | ||
| Taxonomic identifier | 1085 [NCBI] | ||
| Taxonomic lineage | Bacteria › Proteobacteria › Alphaproteobacteria › Rhodospirillales › Rhodospirillaceae › Rhodospirillum![]() |
Protein attributes
| Sequence length | 27 AA. |
| Sequence status | Fragment. |
| Protein existence | Evidence at protein level |
General annotation (Comments)
| Function | Catalyzes the reversible oxidation of malate to oxaloacetate By similarity. HAMAP-Rule MF_00487 |
| Catalytic activity | (S)-malate + NAD+ = oxaloacetate + NADH. HAMAP-Rule MF_00487 |
| Sequence similarities | Belongs to the LDH/MDH superfamily. MDH type 3 family. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Tricarboxylic acid cycle |
| Ligand | NAD |
| Molecular function | Oxidoreductase |
| Technical term | Direct protein sequencing |
| Gene Ontology (GO) | |
| Biological_process | tricarboxylic acid cycle Inferred from electronic annotation. Source: UniProtKB-KW |
| Molecular_function | L-malate dehydrogenase activity Inferred from electronic annotation. Source: EC nucleotide bindingInferred from electronic annotation. Source: InterPro |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – ›27 | ›27 | Malate dehydrogenase HAMAP-Rule MF_00487 | PRO_0000113466 | |||||
Regions | |||||||||
| Nucleotide binding | 9 – 14 | 6 | NAD By similarity | ||||||
Experimental info | |||||||||
| Non-terminal residue | 27 | 1 | |||||||
Sequences
References
| [1] | Naterstad K., Synstad B., Sirevag R. Submitted (SEP-1996) to UniProtKB Cited for: PROTEIN SEQUENCE. |
Cross-references
3D structure databases | |
|---|---|
| ModBase | Search... |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Family and domain databases | |
| Gene3D | 3.40.50.720. 1 hit. |
| HAMAP | MF_00487. Malate_dehydrog_3. |
| InterPro | IPR016040. NAD(P)-bd_dom. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | MDH_RHORU | ||||||||
| Accession | Primary (citable) accession number: P80459 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Prokaryotic Protein Annotation Program | ||||||||
Relevant documents
| SIMILARITY comments Index of protein domains and families |

Clusters with
