P0C1G5 (MDH_KLEPR) Reviewed, UniProtKB/Swiss-Prot
Last modified
March 6, 2013.
Version 33.
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 | Klebsiella pneumoniae subsp. rhinoscleromatis | ||
| Taxonomic identifier | 39831 [NCBI] | ||
| Taxonomic lineage | Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Klebsiella › ![]() |
Protein attributes
| Sequence length | 114 AA. |
| Sequence status | Fragment. |
| Protein existence | Inferred from homology |
General annotation (Comments)
| Function | Catalyzes the reversible oxidation of malate to oxaloacetate By similarity. HAMAP-Rule MF_01516 |
| Catalytic activity | (S)-malate + NAD+ = oxaloacetate + NADH. HAMAP-Rule MF_01516 |
| Subunit structure | Homodimer By similarity. |
| Sequence similarities | Belongs to the LDH/MDH superfamily. MDH type 1 family. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Tricarboxylic acid cycle |
| Ligand | NAD |
| Molecular function | Oxidoreductase |
| Gene Ontology (GO) | |
| Biological_process | cellular carbohydrate metabolic process Inferred from electronic annotation. Source: InterPro tricarboxylic acid cycleInferred 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 – ›114 | ›114 | Malate dehydrogenase HAMAP-Rule MF_01516 | PRO_0000240201 | |||||
Regions | |||||||||
| Nucleotide binding | 87 – 89 | 3 | NAD By similarity | ||||||
Sites | |||||||||
| Binding site | 4 | 1 | NAD By similarity | ||||||
| Binding site | 51 | 1 | Substrate By similarity | ||||||
| Binding site | 57 | 1 | Substrate By similarity | ||||||
| Binding site | 64 | 1 | NAD By similarity | ||||||
| Binding site | 89 | 1 | Substrate By similarity | ||||||
Experimental info | |||||||||
| Non-terminal residue | 1 | 1 | |||||||
| Non-terminal residue | 114 | 1 | |||||||
Sequences
References
| [1] | "Diversity and evolution of the class A chromosomal beta-lactamase gene in Klebsiella pneumoniae." Haeggman S., Loefdahl S., Paauw A., Verhoef J., Brisse S. Antimicrob. Agents Chemother. 48:2400-2408(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 13884 / JCM 1664 / LMG 3184 / NCTC 5046 / R-70. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | AJ635391 Genomic DNA. Translation: CAG25802.1. |
3D structure databases | |
| ProteinModelPortal | P0C1G5. |
| SMR | P0C1G5. Positions 1-114. |
| ModBase | Search... |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Family and domain databases | |
| Gene3D | 3.40.50.720. 1 hit. |
| HAMAP | MF_01516. Malate_dehydrog_1. |
| InterPro | IPR001557. L-lactate/malate_DH. IPR001236. Lactate/malate_DH_N. IPR016040. NAD(P)-bd_dom. [Graphical view] |
| PANTHER | PTHR11540. PTHR11540. 1 hit. |
| Pfam | PF00056. Ldh_1_N. 1 hit. [Graphical view] |
| PROSITE | PS00068. MDH. Partial match. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | MDH_KLEPR | ||||||||
| Accession | Primary (citable) accession number: P0C1G5 Secondary accession number(s): P80535 | ||||||||
| 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
