Reviewed,
UniProtKB/Swiss-Prot P80540 (MDH_ACIDE)
Last modified
June 16, 2009.
Version 35.
History...
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Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents
Names and origin
| Protein names | Recommended name: Malate dehydrogenase EC=1.1.1.37 | ||
| Gene names |
| ||
| Organism | Acidovorax delafieldii | ||
| Taxonomic identifier | 47920 [NCBI] | ||
| Taxonomic lineage | Bacteria › Proteobacteria › Betaproteobacteria › Burkholderiales › Comamonadaceae › Acidovorax |
Protein attributes
| Sequence length | 17 AA. |
| Sequence status | Fragment. |
| Sequence processing | The displayed sequence is not processed. |
| Protein existence | Evidence at protein level. |
General annotation (Comments)
| Function | Catalyzes the reversible oxidation of malate to oxaloacetate By similarity. |
| Catalytic activity | (S)-malate + NAD+ = oxaloacetate + NADH. HAMAP MF_01517 |
| Subunit structure | Homodimer By similarity. |
| Sequence similarities | Belongs to the LDH/MDH superfamily. MDH type 2 family. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Tricarboxylic acid cycle |
| Ligand | NAD |
| Molecular function | Oxidoreductase |
| Technical term | Direct protein sequencing |
| Gene Ontology (GO) | |
| Biological process | oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW tricarboxylic acid cycleInferred from electronic annotation. Source: HAMAP |
| Molecular function | L-malate dehydrogenase activity Inferred 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 – ›17 | ›17 | Malate dehydrogenase HAMAP MF_01517 | PRO_0000113344 | ||||
Regions | ||||||||
| Nucleotide binding | 11 – 17 | 7 | NAD By similarity | |||||
Experimental info | ||||||||
| Non-terminal residue | 17 | 1 | ||||||
Sequences
References
| [1] | "Structural studies of malate dehydrogenases (MDHs): MDHs in Brevundimonas species are the first reported MDHs in Proteobacteria which resemble lactate dehydrogenases in primary structure." Charnock C. J. Bacteriol. 179:4066-4070(1997) [PubMed: 9190829] [Abstract] Cited for: PROTEIN SEQUENCE. Strain: CCUG 12929. |
Cross-references
3D structure databases | |
|---|---|
| ModBase | Search... |
Enzyme and pathway databases | |
| BRENDA | 1.1.1.37. 298367. |
Family and domain databases | |
| HAMAP | MF_01517. [Tree] |
| InterPro | IPR001252. Malate_DH_AS. [Graphical view] |
| PROSITE | PS00068. MDH. Partial match. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | MDH_ACIDE | ||||||||
| Accession | Primary (citable) accession number: P80540 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes) | ||||||||

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