P49814 (MDH_BACSU) Reviewed, UniProtKB/Swiss-Prot
Last modified
May 1, 2013.
Version 112.
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 Alternative name(s): Vegetative protein 69 Short name=VEG69 | ||||||
| Gene names |
| ||||||
| Organism | Bacillus subtilis (strain 168) [Reference proteome] [HAMAP] | ||||||
| Taxonomic identifier | 224308 [NCBI] | ||||||
| Taxonomic lineage | Bacteria › Firmicutes › Bacilli › Bacillales › Bacillaceae › Bacillus › ![]() |
Protein attributes
| Sequence length | 312 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is further processed into a mature form. |
| Protein existence | Evidence at protein level |
General annotation (Comments)
| Function | Catalyzes the reversible oxidation of malate to oxaloacetate By similarity. HAMAP-Rule MF_00487 |
| Catalytic activity | (S)-malate + NAD+ = oxaloacetate + NADH. HAMAP-Rule MF_00487 |
| Sequence similarities | Belongs to the LDH/MDH superfamily. MDH type 3 family. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Tricarboxylic acid cycle |
| Ligand | NAD |
| Molecular function | Oxidoreductase |
| PTM | Phosphoprotein |
| Technical term | Complete proteome Direct protein sequencing Reference 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 | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Initiator methionine | 1 | 1 | Removed Ref.1 Ref.5 | ||||||
| Chain | 2 – 312 | 311 | Malate dehydrogenase HAMAP-Rule MF_00487 | PRO_0000113434 | |||||
Regions | |||||||||
| Nucleotide binding | 12 – 17 | 6 | NAD By similarity | ||||||
| Nucleotide binding | 123 – 125 | 3 | NAD By similarity | ||||||
Sites | |||||||||
| Active site | 180 | 1 | Proton acceptor By similarity | ||||||
| Binding site | 36 | 1 | NAD By similarity | ||||||
| Binding site | 87 | 1 | Substrate By similarity | ||||||
| Binding site | 93 | 1 | Substrate By similarity | ||||||
| Binding site | 100 | 1 | NAD By similarity | ||||||
| Binding site | 125 | 1 | Substrate By similarity | ||||||
| Binding site | 156 | 1 | Substrate By similarity | ||||||
Amino acid modifications | |||||||||
| Modified residue | 149 | 1 | Phosphoserine Ref.6 | ||||||
Sequences
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References
| « Hide 'large scale' references | |
| [1] | "Identification of two distinct Bacillus subtilis citrate synthase genes." Jin S., Sonenshein A.L. J. Bacteriol. 176:4669-4679(1994) [PubMed] [Europe PMC] [Abstract] Cited for: PRELIMINARY PROTEIN SEQUENCE OF 2-312. Strain: 168 / SMY. |
| [2] | "A Bacillus subtilis malate dehydrogenase gene." Jin S., de Jesus-Berrios M., Sonenshein A.L. J. Bacteriol. 178:560-563(1996) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: 168 / SMY. |
| [3] | "Sequencing and functional annotation of the Bacillus subtilis genes in the 200 kb rrnB-dnaB region." Lapidus A., Galleron N., Sorokin A., Ehrlich S.D. Microbiology 143:3431-3441(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: 168. |
| [4] | "The complete genome sequence of the Gram-positive bacterium Bacillus subtilis." Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V., Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R., Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S., Bruschi C.V. Danchin A.Nature 390:249-256(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 168. |
| [5] | "First steps from a two-dimensional protein index towards a response-regulation map for Bacillus subtilis." Antelmann H., Bernhardt J., Schmid R., Mach H., Voelker U., Hecker M. Electrophoresis 18:1451-1463(1997) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 2-16. Strain: 168 / IS58. |
| [6] | "The serine/threonine/tyrosine phosphoproteome of the model bacterium Bacillus subtilis." Macek B., Mijakovic I., Olsen J.V., Gnad F., Kumar C., Jensen P.R., Mann M. Mol. Cell. Proteomics 6:697-707(2007) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-149, MASS SPECTROMETRY. Strain: 168. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | U05257 Genomic DNA. Translation: AAA96343.1. AF008220 Genomic DNA. Translation: AAC00347.1. AL009126 Genomic DNA. Translation: CAB14872.1. |
| PIR | I40383. |
| RefSeq | NP_390790.1. NC_000964.3. |
3D structure databases | |
| ProteinModelPortal | P49814. |
| SMR | P49814. Positions 5-311. |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | 224308.BSU29120. |
PTM databases | |
| PhosSite | P0802202. |
Proteomic databases | |
| PaxDb | P49814. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| EnsemblBacteria | CAB14872; CAB14872; BSU29120. |
| GeneID | 937385. |
| KEGG | bsu:BSU29120. |
| PATRIC | 18977718. VBIBacSub10457_3047. |
Organism-specific databases | |
| GenoList | BSU29120. [Micado] |
Phylogenomic databases | |
| eggNOG | COG0039. |
| HOGENOM | HOG000213794. |
| KO | K00024. |
| OMA | DAMTYVM. |
| ProtClustDB | PRK06223. |
Enzyme and pathway databases | |
| BioCyc | BSUB:BSU29120-MONOMER. |
Family and domain databases | |
| Gene3D | 3.40.50.720. 1 hit. 3.90.110.10. 1 hit. |
| HAMAP | MF_00487. Malate_dehydrog_3. |
| InterPro | IPR001557. L-lactate/malate_DH. IPR022383. Lactate/malate_DH_C. IPR001236. Lactate/malate_DH_N. IPR015955. Lactate_DH/Glyco_Ohase_4_C. IPR011275. Malate_DH_type3. 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] |
| PIRSF | PIRSF000102. Lac_mal_DH. 1 hit. |
| PRINTS | PR00086. LLDHDRGNASE. |
| SUPFAM | SSF56327. Lactate_DH/Glyco_hydro_4_C. 1 hit. |
| TIGRFAMs | TIGR01763. MalateDH_bact. 1 hit. |
| ProtoNet | Search... |
Entry information
| Entry name | MDH_BACSU | ||||||||
| Accession | Primary (citable) accession number: P49814 | ||||||||
| Entry history |
| ||||||||
| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Prokaryotic Protein Annotation Program | ||||||||
Relevant documents
| Bacillus subtilis Bacillus subtilis (strain 168): entries, gene names and cross-references to SubtiList |
| SIMILARITY comments Index of protein domains and families |

Clusters with
