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UniProtKB/Swiss-Prot entry P22133


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name MDHC_YEAST
Primary accession number P22133
Secondary accession numbers None
Integrated into Swiss-Prot on August 1, 1991
Sequence was last modified on January 23, 2007 (Sequence version 2)
Annotations were last modified on    September 2, 2008 (Entry version 83)
Name and origin of the protein
Protein name Malate dehydrogenase, cytoplasmic
Synonym EC 1.1.1.37
Gene name
Name: MDH2
OrderedLocusNames: YOL126C
From
Saccharomyces cerevisiae (Baker's yeast) [TaxID: 4932] 
Taxonomy Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 2-17.
PubMed=1986231 [NCBI, ExPASy, EBI, Israel, Japan]
Minard K.I., McAlister-Henn L.;
"Isolation, nucleotide sequence analysis, and disruption of the MDH2 gene from Saccharomyces cerevisiae: evidence for three isozymes of yeast malate dehydrogenase.";
Mol. Cell. Biol. 11:370-380(1991).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=ATCC 96604 / S288c / FY1679;
DOI=10.1002/(SICI)1097-0061(199609)12:10B<1013::AID-YEA980>3.3.CO;2-X; PubMed=8896265 [NCBI, ExPASy, EBI, Israel, Japan]
Casamayor A., Khalid H., Balcells L., Aldea M., Casas C., Herrero E., Arino J.;
"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.";
Yeast 12:1013-1020(1996).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 96604 / S288c / FY1679;
PubMed=9169874 [NCBI, ExPASy, EBI, Israel, Japan]
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., de Haan M., Delius H., Durand P., Fairhead C., Feldmann H., Gaillon L., Galisson F., Gamo F.-J., Gancedo C., Goffeau A., Goulding S.E., Grivell L.A., Habbig B., Hand N.J., Hani J., Hattenhorst U., Hebling U., Hernando Y., Herrero E., Heumann K., Hiesel R., Hilger F., Hofmann B., Hollenberg C.P., Hughes B., Jauniaux J.-C., Kalogeropoulos A., Katsoulou C., Kordes E., Lafuente M.J., Landt O., Louis E.J., Maarse A.C., Madania A., Mannhaupt G., Marck C., Martin R.P., Mewes H.-W., Michaux G., Paces V., Parle-McDermott A.G., Pearson B.M., Perrin A., Pettersson B., Poch O., Pohl T.M., Poirey R., Portetelle D., Pujol A., Purnelle B., Ramezani Rad M., Rechmann S., Schwager C., Schweizer M., Sor F., Sterky F., Tarassov I.A., Teodoru C., Tettelin H., Thierry A., Tobiasch E., Tzermia M., Uhlen M., Unseld M., Valens M., Vandenbol M., Vetter I., Vlcek C., Voet M., Volckaert G., Voss H., Wambutt R., Wedler H., Wiemann S., Winsor B., Wolfe K.H., Zollner A., Zumstein E., Kleine K.;
"The nucleotide sequence of Saccharomyces cerevisiae chromosome XV.";
Nature 387:98-102(1997).
[4]
PROTEIN SEQUENCE OF 2-35.
DOI=10.1016/0167-4838(87)90044-6; PubMed=3552052 [NCBI, ExPASy, EBI, Israel, Japan]
Kopetzki E., Entian K.-D., Lottspeich F., Mecke D.;
"Purification procedure and N-terminal amino acid sequence of yeast malate dehydrogenase isoenzymes.";
Biochim. Biophys. Acta 912:398-403(1987).
[5]
LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
DOI=10.1038/nature02046; PubMed=14562106 [NCBI, ExPASy, EBI, Israel, Japan]
Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S.;
"Global analysis of protein expression in yeast.";
Nature 425:737-741(2003).
[6]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-6, AND MASS SPECTROMETRY.
DOI=10.1074/mcp.M700468-MCP200; PubMed=18407956 [NCBI, ExPASy, EBI, Israel, Japan]
Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
"A multidimensional chromatography technology for in-depth phosphoproteome analysis.";
Mol. Cell. Proteomics 7:1389-1396(2008).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
M62808; AAA34766.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U41293; AAC49466.1; ALT_INIT; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
Z74868; CAA99145.1; ALT_INIT; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR S63444; DEBYMC.
RefSeq NP_014515.2; -.
3D structure databases
HSSP P00346; 1MLD. [HSSP ENTRY / PDB]
ModBase P22133.
Protein-protein interaction databases
DIP DIP:4211N; -.
IntAct P22133; -.
Organism-specific databases
CYGD YOL126c; -.
SGD S000005486; MDH2.
Yeast-GFP YOL126C.
Gene expression databases
ArrayExpress P22133; -.
GermOnline YOL126C; Saccharomyces cerevisiae.
Ontologies
GO
GO:0005829; Cellular component: cytosol (traceable author statement from SGD).
GO:0030060; Molecular function: L-malate dehydrogenase activity (inferred from mutant phenotype from SGD).
GO:0005515; Molecular function: protein binding (inferred from physical interaction from IntAct).
GO:0006094; Biological process: gluconeogenesis (inferred from expression pattern from SGD).
GO:0006108; Biological process: malate metabolic process (traceable author statement from SGD).
QuickGo view.
Family and domain databases
InterPro IPR001557; L-lactate/malate_DHase.
IPR001236; Lactate/malate_DHase.
IPR015955; Lactate_DHase/Glyco_Ohase_4_C.
IPR001252; Malate_DHase_AS.
IPR010097; Malate_DHase_NAD-dep_euk_g_bac.
IPR016040; NAD(P)-bd.
Graphical view of domain structure.
Gene3D G3DSA:3.90.110.10; lact_mal_DH; 1.
G3DSA:3.40.50.720; NAD(P)-bd; 1.
PANTHER PTHR11540:SF1; MDH_euk_g_bac; 1.
Pfam PF02866; Ldh_1_C; 1.
PF00056; Ldh_1_N; 1.
Pfam graphical view of domain structure.
PIRSF PIRSF000102; Lac_mal_DH; 1.
TIGRFAMs TIGR01772; MDH_euk_gproteo; 1.
PROSITE PS00068; MDH; 1.
BLOCKS P22133.
Proteomic databases
PeptideAtlas P22133; -.
Genome annotation databases
Ensembl YOL126C; Saccharomyces cerevisiae. [Contig view]
GeneID 853994; -.
GenomeReviews Y13140_GR; YOL126C.
KEGG sce:YOL126C; -.
NMPDR fig|4932.3.peg.5601; -.
Phylogenomic databases
HOGENOM P22133; -.
Other
LinkHub P22133; -.
ProtoNet P22133.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Complete proteome; Cytoplasm; Direct protein sequencing; NAD; Oxidoreductase; Phosphoprotein; Tricarboxylic acid cycle.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
INIT_MET   1     1        Removed. 
CHAIN   2   377  376     Malate dehydrogenase, cytoplasmic. PRO_0000113338
NP_BIND   20    26  7     NAD (By similarity). 
NP_BIND   144   146  3     NAD (By similarity). 
ACT_SITE   215   215        Proton acceptor (By similarity). 
BINDING   57    57        NAD (By similarity). 
BINDING   106   106        Substrate (By similarity). 
BINDING   112   112        Substrate (By similarity). 
BINDING   119   119        NAD (By similarity). 
BINDING   146   146        Substrate (By similarity). 
BINDING   185   185        Substrate (By similarity). 
BINDING   266   266        NAD (By similarity). 
MOD_RES   6     6        Phosphothreonine. 
Sequence information
Length: 377 AA [This is the length of the unprocessed precursor] Molecular weight: 40731 Da [This is the MW of the unprocessed precursor] CRC64: CAF4784FA7DD6E27 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MPHSVTPSIE QDSLKIAILG AAGGIGQSLS LLLKAQLQYQ LKESNRSVTH IHLALYDVNQ 

        70         80         90        100        110        120 
EAINGVTADL SHIDTPISVS SHSPAGGIEN CLHNASIVVI PAGVPRKPGM TRDDLFNVNA 

       130        140        150        160        170        180 
GIISQLGDSI AECCDLSKVF VLVISNPVNS LVPVMVSNIL KNHPQSRNSG IERRIMGVTK 

       190        200        210        220        230        240 
LDIVRASTFL REINIESGLT PRVNSMPDVP VIGGHSGETI IPLFSQSNFL SRLNEDQLKY 

       250        260        270        280        290        300 
LIHRVQYGGD EVVKAKNGKG SATLSMAHAG YKCVVQFVSL LLGNIEQIHG TYYVPLKDAN 

       310        320        330        340        350        360 
NFPIAPGADQ LLPLVDGADY FAIPLTITTK GVSYVDYDIV NRMNDMERNQ MLPICVSQLK 

       370 
KNIDKGLEFV ASRSASS 

P22133 in FASTA format

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