P80537 (MDH_BURCE) Reviewed, UniProtKB/Swiss-Prot
Last modified
April 3, 2013.
Version 49.
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 | Burkholderia cepacia (Pseudomonas cepacia) | ||
| Taxonomic identifier | 292 [NCBI] | ||
| Taxonomic lineage | Bacteria › Proteobacteria › Betaproteobacteria › Burkholderiales › Burkholderiaceae › Burkholderia › Burkholderia cepacia complex![]() |
Protein attributes
| Sequence length | 21 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_01517 |
| Catalytic activity | (S)-malate + NAD+ = oxaloacetate + NADH. HAMAP-Rule 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 | tricarboxylic acid cycle Inferred from electronic annotation. Source: UniProtKB-KW |
| Molecular_function | L-malate dehydrogenase activity Inferred 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 – ›21 | ›21 | Malate dehydrogenase HAMAP-Rule MF_01517 | PRO_0000113352 | |||||
Regions | |||||||||
| Nucleotide binding | 11 – 17 | 7 | NAD By similarity | ||||||
Experimental info | |||||||||
| Non-terminal residue | 21 | 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] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE. Strain: ATCC 25416 / DSM 7288 / JCM 5964 / NBRC 14074 / NCTC 10743. |
Cross-references
Entry information
| Entry name | MDH_BURCE | ||||||||
| Accession | Primary (citable) accession number: P80537 | ||||||||
| 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
