A3M928 (MDH_ACIBT) Reviewed, UniProtKB/Swiss-Prot
Last modified
May 1, 2013.
Version 43.
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 | Acinetobacter baumannii (strain ATCC 17978 / NCDC KC 755) [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 400667 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Proteobacteria › Gammaproteobacteria › Pseudomonadales › Moraxellaceae › Acinetobacter › Acinetobacter calcoaceticus/baumannii complex › ![]() |
Protein attributes
| Sequence length | 328 AA. |
| Sequence status | Complete. |
| Protein existence | Inferred from homology |
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 | Complete proteome |
| 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: HAMAP |
| Molecular_function | L-malate dehydrogenase activity Inferred from electronic annotation. Source: HAMAP 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 – 328 | 328 | Malate dehydrogenase HAMAP-Rule MF_01517 | PRO_0000294371 | |||||
Regions | |||||||||
| Nucleotide binding | 11 – 17 | 7 | NAD By similarity | ||||||
| Nucleotide binding | 131 – 133 | 3 | NAD By similarity | ||||||
Sites | |||||||||
| Active site | 189 | 1 | Proton acceptor By similarity | ||||||
| Binding site | 94 | 1 | Substrate By similarity | ||||||
| Binding site | 100 | 1 | Substrate By similarity | ||||||
| Binding site | 107 | 1 | NAD By similarity | ||||||
| Binding site | 114 | 1 | NAD By similarity | ||||||
| Binding site | 133 | 1 | Substrate By similarity | ||||||
| Binding site | 164 | 1 | Substrate By similarity | ||||||
Sequences
| ||||||||||||||||||
References
| [1] | "New insights into Acinetobacter baumannii pathogenesis revealed by high-density pyrosequencing and transposon mutagenesis." Smith M.G., Gianoulis T.A., Pukatzki S., Mekalanos J.J., Ornston L.N., Gerstein M., Snyder M. Genes Dev. 21:601-614(2007) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 17978 / NCDC KC 755. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | CP000521 Genomic DNA. Translation: ABO13422.2. |
3D structure databases | |
| ProteinModelPortal | A3M928. |
| SMR | A3M928. Positions 2-327. |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | 400667.A1S_3025. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| PATRIC | 20722386. VBIAciBau103176_3065. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| eggNOG | COG0039. |
| HOGENOM | HOG000220953. |
| ProtClustDB | PRK05442. |
Enzyme and pathway databases | |
| BioCyc | ABAU400667:GI0Q-3012-MONOMER. |
Family and domain databases | |
| Gene3D | 3.40.50.720. 1 hit. 3.90.110.10. 1 hit. |
| HAMAP | MF_01517. Malate_dehydrog_2. |
| InterPro | IPR001557. L-lactate/malate_DH. IPR022383. Lactate/malate_DH_C. IPR001236. Lactate/malate_DH_N. IPR015955. Lactate_DH/Glyco_Ohase_4_C. IPR010945. Malate_DH_type2. IPR016040. NAD(P)-bd_dom. [Graphical view] |
| PANTHER | PTHR23382. PTHR23382. 1 hit. |
| Pfam | PF02866. Ldh_1_C. 1 hit. PF00056. Ldh_1_N. 1 hit. [Graphical view] |
| PIRSF | PIRSF000102. Lac_mal_DH. 1 hit. |
| SUPFAM | SSF56327. Lactate_DH/Glyco_hydro_4_C. 1 hit. |
| TIGRFAMs | TIGR01759. MalateDH-SF1. 1 hit. |
| PROSITE | PS00068. MDH. False negative. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | MDH_ACIBT | ||||||||
| Accession | Primary (citable) accession number: A3M928 | ||||||||
| Entry history |
| ||||||||
| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Prokaryotic Protein Annotation Program | ||||||||
Relevant documents
| SIMILARITY comments Index of protein domains and families |

Clusters with
