Malate dehydrogenase, cytoplasmic - Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)

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P22133 (MDHC_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 127. History...

Clusters with 100%, 90%, 50% identity |

Documents (3) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Malate dehydrogenase, cytoplasmic
EC=1.1.1.37

Gene names

Name:	MDH2
Ordered Locus Names:	YOL126C

Organism

Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]

Taxonomic identifier

559292 [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	Cytoplasm.
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.
Sequence similarities	Belongs to the LDH/MDH superfamily. MDH type 1 family.
Sequence caution	The sequence AAC49466.1 differs from that shown. Reason: Erroneous initiation. The sequence CAA99145.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
Biological process	Tricarboxylic acid cycle
Cellular component	Cytoplasm
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 gluconeogenesis Inferred from mutant phenotype PubMed 12730240. Source: SGD malate metabolic process Traceable author statement PubMed 9175438. Source: SGD protein import into peroxisome matrix Inferred from mutant phenotype PubMed 19118449. Source: SGD tricarboxylic acid cycle Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	cytosol Inferred from direct assay Ref.1. Source: SGD
Molecular_function	L-malate dehydrogenase activity Inferred from mutant phenotype Ref.1. Source: SGD nucleotide binding Inferred 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

Removed Ref.1 Ref.5

Chain

2 – 377

376

Malate dehydrogenase, cytoplasmic

PRO_0000113338

Regions

Nucleotide binding

20 – 26

NAD By similarity

Nucleotide binding

144 – 146

NAD By similarity

Sites

Active site

215

Proton acceptor By similarity

Binding site

NAD By similarity

Binding site

106

Substrate By similarity

Binding site

112

Substrate By similarity

Binding site

119

NAD By similarity

Binding site

146

Substrate By similarity

Binding site

185

Substrate By similarity

Binding site

266

NAD By similarity

Amino acid modifications

Modified residue

Phosphothreonine Ref.7

Sequences

Sequence

Length

Mass (Da)

Tools

P22133 [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: CAF4784FA7DD6E27
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FASTA

377

40,731

        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

« Hide

References

	« Hide 'large scale' referencesShow '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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 96604 / S288c / FY1679.
[4]	Saccharomyces Genome Database Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases Cited for: GENOME REANNOTATION. Strain: ATCC 204508 / S288c.
[5]	"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] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 2-35.
[6]	"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] [Europe PMC] [Abstract] Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
[7]	"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] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-6, MASS SPECTROMETRY.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	M62808 Genomic DNA. Translation: AAA34766.1. U41293 Genomic DNA. Translation: AAC49466.1. Different initiation. Z74868 Genomic DNA. Translation: CAA99145.1. Different initiation. BK006948 Genomic DNA. Translation: DAA10658.1.
PIR	DEBYMC. S63444.
RefSeq	NP_014515.2. NM_001183380.1.
3D structure databases
ProteinModelPortal	P22133.
SMR	P22133. Positions 14-370.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-4211N.
IntAct	P22133. 11 interactions.
MINT	MINT-568274.
STRING	4932.YOL126C.
Proteomic databases
PaxDb	P22133.
PeptideAtlas	P22133.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblFungi	YOL126C; YOL126C; YOL126C.
GeneID	853994.
KEGG	sce:YOL126C.
Organism-specific databases
SGD	S000005486. MDH2.
Phylogenomic databases
eggNOG	COG0039.
GeneTree	ENSGT00550000075847.
HOGENOM	HOG000213792.
KO	K00026.
OMA	ETIIPLF.
OrthoDB	EOG4G4M0J.
Enzyme and pathway databases
SABIO-RK	P22133.
Gene expression databases
Genevestigator	P22133.
GermOnline	YOL126C. Saccharomyces cerevisiae.
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...
Other
NextBio	975482.

Entry information

Entry name

MDHC_YEAST

Accession

Primary (citable) accession number: P22133
Secondary accession number(s): D6W1U2

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 1, 1991
Last sequence update:	January 23, 2007
Last modified:	May 1, 2013
This is version 127 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program

Relevant documents

Yeast

Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD

Yeast chromosome XV

Yeast (Saccharomyces cerevisiae) chromosome XV: entries and gene names

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Amino acid modifications

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents