Q7YRU4 (MDHC_FELCA) Reviewed, UniProtKB/Swiss-Prot
Last modified
May 29, 2013.
Version 64.
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, cytoplasmic EC=1.1.1.37 Alternative name(s): Cytosolic malate dehydrogenase | ||
| Gene names |
| ||
| Organism | Felis catus (Cat) (Felis silvestris catus) [Complete proteome] | ||
| Taxonomic identifier | 9685 [NCBI] | ||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Carnivora › Feliformia › Felidae › Felinae › Felis![]() |
Protein attributes
| Sequence length | 334 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is further processed into a mature form. |
| Protein existence | Evidence at transcript level |
General annotation (Comments)
| Catalytic activity | (S)-malate + NAD+ = oxaloacetate + NADH. |
| Subunit structure | Homodimer By similarity. |
| Subcellular location | Cytoplasm By similarity. |
| Post-translational modification | ISGylated By similarity. Acetylation at Lys-118 dramatically enhances enzymatic activity and promotes adipogenic differentiation By similarity. |
| Sequence similarities | Belongs to the LDH/MDH superfamily. MDH type 2 family. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Tricarboxylic acid cycle |
| Cellular component | Cytoplasm |
| Ligand | NAD |
| Molecular function | Oxidoreductase |
| PTM | Acetylation Phosphoprotein Ubl conjugation |
| 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: UniProtKB-KW |
| Cellular_component | centrosome Inferred from electronic annotation. Source: Compara mitochondrionInferred from electronic annotation. Source: Compara |
| Molecular_function | L-malate dehydrogenase activity Inferred from electronic annotation. Source: EC |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Initiator methionine | 1 | 1 | Removed By similarity | ||||||
| Chain | 2 – 334 | 333 | Malate dehydrogenase, cytoplasmic | PRO_0000226736 | |||||
Regions | |||||||||
| Nucleotide binding | 11 – 17 | 7 | NAD By similarity | ||||||
| Nucleotide binding | 129 – 131 | 3 | NAD By similarity | ||||||
Sites | |||||||||
| Active site | 187 | 1 | Proton acceptor By similarity | ||||||
| Binding site | 92 | 1 | Substrate By similarity | ||||||
| Binding site | 98 | 1 | Substrate By similarity | ||||||
| Binding site | 105 | 1 | NAD By similarity | ||||||
| Binding site | 112 | 1 | NAD By similarity | ||||||
| Binding site | 131 | 1 | Substrate By similarity | ||||||
| Binding site | 162 | 1 | Substrate By similarity | ||||||
Amino acid modifications | |||||||||
| Modified residue | 2 | 1 | N-acetylserine By similarity | ||||||
| Modified residue | 118 | 1 | N6-acetyllysine By similarity | ||||||
| Modified residue | 121 | 1 | N6-acetyllysine By similarity | ||||||
| Modified residue | 210 | 1 | Phosphotyrosine By similarity | ||||||
| Modified residue | 241 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 298 | 1 | N6-acetyllysine By similarity | ||||||
| Modified residue | 333 | 1 | Phosphoserine By similarity | ||||||
Sequences
| ||||||||||||||||||
References
| [1] | "Cloning and characterization of feline cytosolic malate dehydrogenase." Nakamura M., Sasaki N., Arai T. Submitted (JUN-2003) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Liver. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | AB113364 mRNA. Translation: BAC78621.1. |
| RefSeq | NP_001009329.1. NM_001009329.1. |
3D structure databases | |
| ProteinModelPortal | Q7YRU4. |
| SMR | Q7YRU4. Positions 2-334. |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | 9685.ENSFCAP00000015559. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| GeneID | 493924. |
| KEGG | fca:493924. |
Organism-specific databases | |
| CTD | 4190. |
Phylogenomic databases | |
| eggNOG | COG0039. |
| GeneTree | ENSGT00530000063410. |
| HOVERGEN | HBG006340. |
| KO | K00025. |
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. IPR011274. Malate_DH_NAD-dep_euk. 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. TIGR01758. MDH_euk_cyt. 1 hit. |
| PROSITE | PS00068. MDH. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | MDHC_FELCA | ||||||||
| Accession | Primary (citable) accession number: Q7YRU4 | ||||||||
| 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
