P61897 (MDH_PECCC) Reviewed, UniProtKB/Swiss-Prot
Last modified
March 6, 2013.
Version 46.
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 | Pectobacterium carotovorum subsp. carotovorum (Erwinia carotovora subsp. carotovora) | ||
| Taxonomic identifier | 555 [NCBI] | ||
| Taxonomic lineage | Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Pectobacterium › ![]() |
Protein attributes
| Sequence length | 154 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 malate metabolic processInferred 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 – ›154 | ›154 | Malate dehydrogenase HAMAP-Rule MF_01516 | PRO_0000113318 | |||||
Regions | |||||||||
| Nucleotide binding | 39 – 41 | 3 | NAD By similarity | ||||||
Sites | |||||||||
| Active site | 99 | 1 | Proton acceptor By similarity | ||||||
| Binding site | 3 | 1 | Substrate By similarity | ||||||
| Binding site | 9 | 1 | Substrate By similarity | ||||||
| Binding site | 16 | 1 | NAD By similarity | ||||||
| Binding site | 41 | 1 | Substrate By similarity | ||||||
| Binding site | 75 | 1 | Substrate By similarity | ||||||
| Binding site | 149 | 1 | NAD By similarity | ||||||
Natural variations | |||||||||
| Natural variant | 15 – 17 | 3 | VNA → LPF in strain: WPP3. | ||||||
| Natural variant | 23 – 24 | 2 | LV → WH in strain: WPP3. | ||||||
| Natural variant | 32 | 1 | P → R in strain: WPP3. | ||||||
| Natural variant | 49 | 1 | I → M in strain: WPP7. | ||||||
| Natural variant | 106 – 107 | 2 | PL → LC in strain: WPP25. | ||||||
| Natural variant | 111 | 1 | V → D in strain: WPP25. | ||||||
| Natural variant | 117 | 1 | S → N in strain: WPP3 and WPP8. | ||||||
| Natural variant | 133 – 134 | 2 | TE → AQ in strain: WPP3. | ||||||
| Natural variant | 137 – 140 | 4 | EAKA → KPKQ in strain: WPP19. | ||||||
| Natural variant | 137 | 1 | E → K in strain: WPP3. | ||||||
| Natural variant | 141 | 1 | G → R in strain: WPP25. | ||||||
| Natural variant | 142 | 1 | G → A in strain: WPP9 and WPP10. | ||||||
| Natural variant | 150 – 154 | 5 | GQVPG → ARLPA in strain: WPP25. | ||||||
| Natural variant | 152 – 154 | 3 | VPG → AAR in strain: WPP20, WPP22 and WPP7. | ||||||
| Natural variant | 152 – 154 | 3 | VPG → AGR in strain: WPP5. | ||||||
| Natural variant | 152 – 153 | 2 | VP → AA in strain: WPP12 and WPP21. | ||||||
| Natural variant | 152 | 1 | V → A in strain: WPP24. | ||||||
| Natural variant | 153 | 1 | P → A in strain: WPP4. | ||||||
Experimental info | |||||||||
| Non-terminal residue | 1 | 1 | |||||||
| Non-terminal residue | 154 | 1 | |||||||
Sequences
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References
| [1] | "Genomic diversity of Erwinia carotovora subsp. carotovora and its correlation with virulence." Yap M.-N., Barak J.D., Charkowski A.O. Appl. Environ. Microbiol. 70:3013-3023(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: WPP1, WPP10, WPP11, WPP12, WPP13, WPP14, WPP15, WPP17, WPP18, WPP19, WPP2, WPP20, WPP21, WPP22, WPP24, WPP25, WPP3, WPP4, WPP5, WPP6, WPP7, WPP8 and WPP9. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | AY428968 Genomic DNA. Translation: AAR11889.1. AY428969 Genomic DNA. Translation: AAR11890.1. AY428970 Genomic DNA. Translation: AAR11891.1. AY428971 Genomic DNA. Translation: AAR11892.1. AY428972 Genomic DNA. Translation: AAR11893.1. AY428973 Genomic DNA. Translation: AAR11894.1. AY428974 Genomic DNA. Translation: AAR11895.1. AY428975 Genomic DNA. Translation: AAR11896.1. AY428976 Genomic DNA. Translation: AAR11897.1. AY428977 Genomic DNA. Translation: AAR11898.1. AY428978 Genomic DNA. Translation: AAR11899.1. AY428979 Genomic DNA. Translation: AAR11900.1. AY428980 Genomic DNA. Translation: AAR11901.1. AY428981 Genomic DNA. Translation: AAR11902.1. AY428982 Genomic DNA. Translation: AAR11903.1. AY428983 Genomic DNA. Translation: AAR11904.1. AY428984 Genomic DNA. Translation: AAR11905.1. AY428985 Genomic DNA. Translation: AAR11906.1. AY428986 Genomic DNA. Translation: AAR11907.1. AY428987 Genomic DNA. Translation: AAR11908.1. AY428988 Genomic DNA. Translation: AAR11909.1. AY428989 Genomic DNA. Translation: AAR11910.1. AY428990 Genomic DNA. Translation: AAR11911.1. |
3D structure databases | |
| ProteinModelPortal | P61897. |
| SMR | P61897. Positions 1-151. |
| ModBase | Search... |
Proteomic databases | |
| PRIDE | P61897. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Family and domain databases | |
| Gene3D | 3.40.50.720. 1 hit. 3.90.110.10. 1 hit. |
| HAMAP | MF_01516. Malate_dehydrog_1. |
| InterPro | IPR001557. L-lactate/malate_DH. IPR022383. Lactate/malate_DH_C. IPR001236. Lactate/malate_DH_N. IPR015955. Lactate_DH/Glyco_Ohase_4_C. IPR001252. Malate_DH_AS. IPR016040. NAD(P)-bd_dom. [Graphical view] |
| PANTHER | PTHR11540. PTHR11540. 1 hit. |
| Pfam | PF02866. Ldh_1_C. 1 hit. PF00056. Ldh_1_N. 1 hit. [Graphical view] |
| SUPFAM | SSF56327. Lactate_DH/Glyco_hydro_4_C. 1 hit. |
| PROSITE | PS00068. MDH. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | MDH_PECCC | ||||||||
| Accession | Primary (citable) accession number: P61897 | ||||||||
| 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
