Reviewed,
UniProtKB/Swiss-Prot P22133 (MDHC_YEAST)
Last modified
June 16, 2009.
Version 89.
History...
Clusters with 100%,
90%,
50% identity |
Documents (2) |
Third-party data |
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Names and origin
| Protein names | Recommended name: Malate dehydrogenase, cytoplasmic EC=1.1.1.37 | ||||
| Gene names |
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| Organism | Saccharomyces cerevisiae (Baker's yeast) [Complete proteome] | ||||
| Taxonomic identifier | 4932 [NCBI] | ||||
| Taxonomic lineage | Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces |
Protein attributes
| Sequence length | 377 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 | The isoenzyme MDH2 may function primarily in the glyoxylate cycle. |
| Catalytic activity | (S)-malate + NAD+ = oxaloacetate + NADH. |
| Subunit structure | Homodimer. |
| Subcellular location | |
| Induction | By acetate as carbon source in the growth medium. Is inactivated by addition of glucose (catabolite inactivation). |
| Miscellaneous | Yeast contains at least 3 malate dehydrogenase isoenzymes: a mitochondrial (MDH1), a cytoplasmic (MDH2) and a peroxisomal (MDH3). Present with 5260 molecules/cell in log phase SD medium. Ref.5 |
| Sequence similarities | Belongs to the LDH/MDH superfamily. MDH type 1 family. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Tricarboxylic acid cycle |
| Cellular component | Cytoplasm |
| Ligand | NAD |
| Molecular function | Oxidoreductase |
| PTM | Phosphoprotein |
| Technical term | Complete proteome Direct protein sequencing |
| Gene Ontology (GO) | |
| Biological process | gluconeogenesis Inferred from mutant phenotype. Source: SGD glycolysisInferred from electronic annotation. Source: InterPro malate metabolic processTraceable author statement. Source: SGD oxidation reductionInferred from electronic annotation. Source: UniProtKB-KW protein import into peroxisome matrixInferred from mutant phenotype. Source: SGD tricarboxylic acid cycleInferred from electronic annotation. Source: UniProtKB-KW |
| Cellular component | cytosol Ref.1 Inferred from direct assay. Source: SGD |
| Molecular function | L-malate dehydrogenase activity Ref.1 Inferred from direct assay. Source: SGD protein bindingInferred from physical interaction. Source: IntAct |
| 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.4 | ||||||
| Chain | 2 – 377 | 376 | Malate dehydrogenase, cytoplasmic | PRO_0000113338 | |||||
Regions | |||||||||
| Nucleotide binding | 20 – 26 | 7 | NAD By similarity | ||||||
| Nucleotide binding | 144 – 146 | 3 | NAD By similarity | ||||||
Sites | |||||||||
| Active site | 215 | 1 | Proton acceptor By similarity | ||||||
| Binding site | 57 | 1 | NAD By similarity | ||||||
| Binding site | 106 | 1 | Substrate By similarity | ||||||
| Binding site | 112 | 1 | Substrate By similarity | ||||||
| Binding site | 119 | 1 | NAD By similarity | ||||||
| Binding site | 146 | 1 | Substrate By similarity | ||||||
| Binding site | 185 | 1 | Substrate By similarity | ||||||
| Binding site | 266 | 1 | NAD By similarity | ||||||
Amino acid modifications | |||||||||
| Modified residue | 6 | 1 | Phosphothreonine Ref.6 | ||||||
Sequences
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References
| « Hide 'large scale' references | |
| [1] | "Isolation, nucleotide sequence analysis, and disruption of the MDH2 gene from Saccharomyces cerevisiae: evidence for three isozymes of yeast malate dehydrogenase." Minard K.I., McAlister-Henn L. Mol. Cell. Biol. 11:370-380(1991) [PubMed: 1986231] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 2-17. |
| [2] | "Sequence analysis of a 13.4 kbp fragment from the left arm of chromosome XV reveals a malate dehydrogenase gene, a putative Ser/Thr protein kinase, the ribosomal L25 gene and four new open reading frames." Casamayor A., Khalid H., Balcells L., Aldea M., Casas C., Herrero E., Arino J. Yeast 12:1013-1020(1996) [PubMed: 8896265] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 96604 / S288c / FY1679. |
| [3] | "The nucleotide sequence of Saccharomyces cerevisiae chromosome XV." Dujon B., Albermann K., Aldea M., Alexandraki D., Ansorge W., Arino J., Benes V., Bohn C., Bolotin-Fukuhara M., Bordonne R., Boyer J., Camasses A., Casamayor A., Casas C., Cheret G., Cziepluch C., Daignan-Fornier B., Dang V.-D. Kleine K.Nature 387:98-102(1997) [PubMed: 9169874] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 96604 / S288c / FY1679. |
| [4] | "Purification procedure and N-terminal amino acid sequence of yeast malate dehydrogenase isoenzymes." Kopetzki E., Entian K.-D., Lottspeich F., Mecke D. Biochim. Biophys. Acta 912:398-403(1987) [PubMed: 3552052] [Abstract] Cited for: PROTEIN SEQUENCE OF 2-35. |
| [5] | "Global analysis of protein expression in yeast." Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S. Nature 425:737-741(2003) [PubMed: 14562106] [Abstract] Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS]. |
| [6] | "A multidimensional chromatography technology for in-depth phosphoproteome analysis." Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H. Mol. Cell. Proteomics 7:1389-1396(2008) [PubMed: 18407956] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-6, MASS SPECTROMETRY. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |
|---|---|
| M62808 Genomic DNA. Translation: AAA34766.1. U41293 Genomic DNA. Translation: AAC49466.1. Different initiation. Z74868 Genomic DNA. Translation: CAA99145.1. Different initiation. | |
| PIR | DEBYMC. S63444. |
| RefSeq | NP_014515.2. |
3D structure databases | |
| HSSP | HSSP built from PDB template 1MLD based on UniProtKB P00346. |
| ModBase | Search... |
Protein-protein interaction databases | |
| DIP | DIP:4211N. |
| IntAct | P22133. 8 interactions. |
Proteomic databases | |
| PeptideAtlas | P22133. |
Genome annotation databases | |
| Ensembl | YOL126C. Saccharomyces cerevisiae. [Contig view] |
| GeneID | 853994. |
| GenomeReviews | Gene locus YOL126C in contig Y13140_GR. |
| KEGG | sce:YOL126C. |
| NMPDR | fig|4932.3.peg.5601. |
Organism-specific databases | |
| CYGD | YOL126c. |
| SGD | S000005486. MDH2. |
| Yeast-GFP | Search... |
Phylogenomic databases | |
| HOGENOM | P22133. |
Enzyme and pathway databases | |
| BRENDA | 1.1.1.37. 250. |
Gene expression databases | |
| ArrayExpress | P22133. |
| GermOnline | YOL126C. Saccharomyces cerevisiae. |
Family and domain databases | |
| InterPro | IPR001557. L-lactate/malate_DH. IPR001236. Lactate/malate_DH. IPR015955. Lactate_DH/Glyco_Ohase_4_C. IPR001252. Malate_DH_AS. IPR010097. Malate_DH_NAD-dep_euk_g_bac. IPR016040. NAD(P)-bd_dom. [Graphical view] |
| Gene3D | G3DSA:3.90.110.10. lact_mal_DH. 1 hit. G3DSA:3.40.50.720. NAD(P)-bd. 1 hit. |
| PANTHER | PTHR11540:SF1. MDH_euk_g_bac. 1 hit. |
| Pfam | PF02866. Ldh_1_C. 1 hit. PF00056. Ldh_1_N. 1 hit. [Graphical view] |
| PIRSF | PIRSF000102. Lac_mal_DH. 1 hit. |
| TIGRFAMs | TIGR01772. MDH_euk_gproteo. 1 hit. |
| PROSITE | PS00068. MDH. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Other Resources | |
| NextBio | 975482. |
Entry information
| Entry name | MDHC_YEAST | ||||||||
| Accession | Primary (citable) accession number: P22133 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | FPAP (Fungal Proteome Annotation Project) | ||||||||
Relevant documents
| SIMILARITY comments Index of protein domains and families |
| Yeast Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD |

Clusters with


