Q32LG3 (MDHM_BOVIN) Reviewed, UniProtKB/Swiss-Prot
Last modified
April 3, 2013.
Version 62.
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, mitochondrial EC=1.1.1.37 | ||
| Gene names |
| ||
| Organism | Bos taurus (Bovine) [Reference proteome] | ||
| Taxonomic identifier | 9913 [NCBI] | ||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Cetartiodactyla › Ruminantia › Pecora › Bovidae › Bovinae › Bos![]() |
Protein attributes
| Sequence length | 338 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)
| Catalytic activity | (S)-malate + NAD+ = oxaloacetate + NADH. |
| Enzyme regulation | Enzyme activity is enhanced by acetylation By similarity. |
| Subunit structure | Homodimer By similarity. |
| Subcellular location | Mitochondrion matrix By similarity. |
| Post-translational modification | Acetylation is enhanced by up to 67% after treatment either with trichostin A (TCA) or with nicotinamide (NAM) with the appearance of tri-and tetraacetylations. Glucose also increases acetylation by about 60% By similarity. |
| Sequence similarities | Belongs to the LDH/MDH superfamily. MDH type 1 family. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Tricarboxylic acid cycle |
| Cellular component | Mitochondrion |
| Domain | Transit peptide |
| Ligand | NAD |
| Molecular function | Oxidoreductase |
| PTM | Acetylation |
| Technical term | Complete proteome Reference proteome |
| Gene Ontology (GO) | |
| Biological_process | cellular carbohydrate metabolic process Inferred from electronic annotation. Source: InterPro internal protein amino acid acetylationInferred from sequence or structural similarity. Source: UniProtKB malate metabolic processInferred from electronic annotation. Source: InterPro tricarboxylic acid cycleInferred from electronic annotation. Source: UniProtKB-KW |
| Cellular_component | mitochondrial matrix Inferred from electronic annotation. Source: UniProtKB-SubCell |
| 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 | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Transit peptide | 1 – 24 | 24 | Mitochondrion By similarity | ||||||
| Chain | 25 – 338 | 314 | Malate dehydrogenase, mitochondrial | PRO_0000260267 | |||||
Regions | |||||||||
| Nucleotide binding | 31 – 37 | 7 | NAD By similarity | ||||||
| Nucleotide binding | 140 – 142 | 3 | NAD By similarity | ||||||
Sites | |||||||||
| Active site | 200 | 1 | Proton acceptor By similarity | ||||||
| Binding site | 57 | 1 | NAD By similarity | ||||||
| Binding site | 104 | 1 | Substrate By similarity | ||||||
| Binding site | 110 | 1 | Substrate By similarity | ||||||
| Binding site | 117 | 1 | NAD By similarity | ||||||
| Binding site | 142 | 1 | Substrate By similarity | ||||||
| Binding site | 176 | 1 | Substrate By similarity | ||||||
| Binding site | 251 | 1 | NAD By similarity | ||||||
Amino acid modifications | |||||||||
| Modified residue | 157 | 1 | N6-acetyllysine By similarity | ||||||
| Modified residue | 165 | 1 | N6-acetyllysine By similarity | ||||||
| Modified residue | 185 | 1 | N6-acetyllysine Ref.2 | ||||||
| Modified residue | 239 | 1 | N6-malonyllysine; alternate Ref.2 | ||||||
| Modified residue | 239 | 1 | N6-succinyllysine; alternate Ref.2 | ||||||
| Modified residue | 301 | 1 | N6-acetyllysine By similarity | ||||||
| Modified residue | 301 | 1 | N6-succinyllysine; alternate Ref.2 | ||||||
| Modified residue | 307 | 1 | N6-acetyllysine; alternate Ref.2 | ||||||
| Modified residue | 307 | 1 | N6-malonyllysine; alternate By similarity | ||||||
| Modified residue | 314 | 1 | N6-acetyllysine Ref.2 | ||||||
| Modified residue | 328 | 1 | N6-acetyllysine; alternate Ref.2 | ||||||
| Modified residue | 328 | 1 | N6-succinyllysine; alternate Ref.2 | ||||||
| Modified residue | 329 | 1 | N6-acetyllysine By similarity | ||||||
| Modified residue | 329 | 1 | N6-malonyllysine; alternate Ref.2 | ||||||
| Modified residue | 335 | 1 | N6-acetyllysine By similarity | ||||||
Sequences
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References
| « Hide 'large scale' references | |
| [1] | NIH - Mammalian Gene Collection (MGC) project Submitted (NOV-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: Crossbred X Angus. Tissue: Liver. |
| [2] | "Sirt5 is a NAD-dependent protein lysine demalonylase and desuccinylase." Du J., Zhou Y., Su X., Yu J.J., Khan S., Jiang H., Kim J., Woo J., Kim J.H., Choi B.H., He B., Chen W., Zhang S., Cerione R.A., Auwerx J., Hao Q., Lin H. Science 334:806-809(2011) [PubMed] [Europe PMC] [Abstract] Cited for: ACETYLATION AT LYS-185; LYS-307; LYS-314 AND LYS-328, MALONYLATION AT LYS-239 AND LYS-329, SUCCINYLATION AT LYS-239; LYS-301 AND LYS-328. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | BC109597 mRNA. Translation: AAI09598.1. |
| IPI | IPI00712250. |
| UniGene | Bt.7915. |
3D structure databases | |
| HSSP | HSSP built from PDB template 2DFD based on UniProtKB P40926. |
| ProteinModelPortal | Q32LG3. |
| SMR | Q32LG3. Positions 25-337. |
| ModBase | Search... |
Protein-protein interaction databases | |
| IntAct | Q32LG3. 1 interaction. |
| STRING | 9913.ENSBTAP00000041906. |
Proteomic databases | |
| PaxDb | Q32LG3. |
| PRIDE | Q32LG3. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Phylogenomic databases | |
| eggNOG | COG0039. |
| HOGENOM | HOG000213792. |
| HOVERGEN | HBG001662. |
| InParanoid | Q32LG3. |
| OrthoDB | EOG4MKNGM. |
Enzyme and pathway databases | |
| SABIO-RK | Q32LG3. |
Family and domain databases | |
| Gene3D | 3.40.50.720. 1 hit. 3.90.110.10. 1 hit. |
| 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. IPR010097. Malate_DH_type1. IPR016040. NAD(P)-bd_dom. [Graphical view] |
| PANTHER | PTHR11540. PTHR11540. 1 hit. PTHR11540:SF1. PTHR11540:SF1. 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 | TIGR01772. MDH_euk_gproteo. 1 hit. |
| PROSITE | PS00068. MDH. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | MDHM_BOVIN | ||||||||
| Accession | Primary (citable) accession number: Q32LG3 | ||||||||
| Entry history |
| ||||||||
| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Chordata Protein Annotation Program | ||||||||
Relevant documents
| SIMILARITY comments Index of protein domains and families |

Clusters with
