Malate dehydrogenase, mitochondrial precursor

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P08249 (MDHM_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 137. History...

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

Documents (2) |

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, mitochondrial
EC=1.1.1.37

Gene names

Name:	Mdh2
Synonyms:	Mor1

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

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.
Subcellular location	Mitochondrion matrix.
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. Acetylation of Lys-239 and Lys-314 is observed in liver mitochondria from fasted mice but not from fed mice.
Sequence similarities	Belongs to the LDH/MDH superfamily. MDH type 1 family.
Sequence caution	The sequence BAC24986.1 differs from that shown. Reason: Frameshift at position 39.

Ontologies

Keywords
Biological process	Tricarboxylic acid cycle
Cellular component	Mitochondrion
Domain	Transit peptide
Ligand	NAD
Molecular function	Oxidoreductase
PTM	Acetylation
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	NADH metabolic process Inferred from electronic annotation. Source: Compara cellular carbohydrate metabolic process Inferred from electronic annotation. Source: InterPro internal protein amino acid acetylation Inferred from sequence or structural similarity. Source: UniProtKB malate metabolic process Inferred from sequence alignment PubMed 15809022. Source: MGI oxaloacetate metabolic process Inferred from electronic annotation. Source: Compara tricarboxylic acid cycle Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	mitochondrial inner membrane Inferred from direct assay PubMed 12865426. Source: MGI mitochondrial matrix Inferred from electronic annotation. Source: UniProtKB-SubCell nucleus Inferred from electronic annotation. Source: Compara plasma membrane Inferred from electronic annotation. Source: Compara
Molecular_function	L-malate dehydrogenase activity Inferred from direct assay PubMed 5496232. Source: MGI malate dehydrogenase (NADP+) activity Inferred from electronic annotation. Source: Compara 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

Transit peptide

1 – 24

Mitochondrion

Chain

25 – 338

314

Malate dehydrogenase, mitochondrial

PRO_0000018629

Regions

Nucleotide binding

31 – 37

NAD By similarity

Nucleotide binding

140 – 142

NAD By similarity

Sites

Active site

200

Proton acceptor By similarity

Binding site

NAD By similarity

Binding site

104

Substrate

Binding site

110

Substrate

Binding site

117

NAD By similarity

Binding site

142

Substrate

Binding site

176

Substrate

Binding site

251

NAD By similarity

Amino acid modifications

Modified residue

157

N6-acetyllysine Ref.7

Modified residue

165

N6-acetyllysine By similarity

Modified residue

185

N6-acetyllysine By similarity

Modified residue

239

N6-acetyllysine; alternate Probable

Modified residue

239

N6-malonyllysine; alternate By similarity

Modified residue

239

N6-succinyllysine; alternate By similarity

Modified residue

301

N6-acetyllysine By similarity

Modified residue

301

N6-succinyllysine; alternate By similarity

Modified residue

307

N6-acetyllysine; alternate By similarity

Modified residue

307

N6-malonyllysine; alternate By similarity

Modified residue

314

N6-acetyllysine Probable

Modified residue

328

N6-acetyllysine; alternate By similarity

Modified residue

328

N6-succinyllysine; alternate By similarity

Modified residue

329

N6-acetyllysine By similarity

Modified residue

329

N6-malonyllysine; alternate By similarity

Modified residue

335

N6-acetyllysine By similarity

Experimental info

Sequence conflict

N → K in AAA39509. Ref.1

Sequence conflict

269

K → L in AAA39509. Ref.1

Sequence conflict

269

K → L in CAA30274. Ref.2

Sequences

Sequence

Length

Mass (Da)

Tools

P08249 [UniParc].

Last modified May 1, 2007. Version 3.
Checksum: 99D13BB2099C19F1
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FASTA

338

35,611

        10         20         30         40         50         60 
MLSALARPAG AALRRSFSTS AQNNAKVAVL GASGGIGQPL SLLLKNSPLV SRLTLYDIAH 

        70         80         90        100        110        120 
TPGVAADLSH IETRANVKGY LGPEQLPDCL KGCDVVVIPA GVPRKPGMTR DDLFNTNATI 

       130        140        150        160        170        180 
VATLTAACAQ HCPEAMVCII ANPVNSTIPI TAEVFKKHGV YNPNKIFGVT TLDIVRANTF 

       190        200        210        220        230        240 
VAELKGLDPA RVNVPVIGGH AGKTIIPLIS QCTPKVDFPQ DQLATLTGRI QEAGTEVVKA 

       250        260        270        280        290        300 
KAGAGSATLS MAYAGARFVF SLVDAMNGKE GVVECSFVQS KETECTYFST PLLLGKKGLE 

       310        320        330 
KNLGIGKITP FEEKMIAEAI PELKASIKKG EDFVKNMK

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Cloning and sequence analysis of cDNAs encoding mammalian mitochondrial malate dehydrogenase." Joh T., Takeshima H., Tsuzuki T., Shimada K., Tanase S., Morino Y. Biochemistry 26:2515-2520(1987) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	"Structural organization of the mouse mitochondrial malate dehydrogenase gene." Takeshima H., Joh T., Tsuzuki T., Shimada K., Matsukado Y. J. Mol. Biol. 200:1-11(1988) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]	"The transcriptional landscape of the mammalian genome." Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. Hayashizaki Y. Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: BALB/c and C57BL/6J. Tissue: Cerebellum and Kidney.
[4]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: FVB/N. Tissue: Mammary tumor.
[5]	"Housekeeping genes for phylogenetic analysis of eutherian relationships." Kullberg M., Nilsson M.A., Arnason U., Harley E.H., Janke A. Mol. Biol. Evol. 23:1493-1503(2006) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 22-322. Tissue: Liver.
[6]	Lubec G., Kang S.U., Klug S., Yang J.W., Zigmond M., Sunyer B., Chen W.-Q. Submitted (JAN-2009) to UniProtKB Cited for: PROTEIN SEQUENCE OF 27-45; 53-74; 79-104; 166-185; 192-239; 242-257; 282-296 AND 308-324, MASS SPECTROMETRY. Strain: C57BL/6 and OF1. Tissue: Brain and Hippocampus.
[7]	"Substrate and functional diversity of lysine acetylation revealed by a proteomics survey." Kim S.C., Sprung R., Chen Y., Xu Y., Ball H., Pei J., Cheng T., Kho Y., Xiao H., Xiao L., Grishin N.V., White M., Yang X.-J., Zhao Y. Mol. Cell 23:607-618(2006) [PubMed] [Europe PMC] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-157; LYS-239 AND LYS-314, MASS SPECTROMETRY. Tissue: Liver.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	M16229 mRNA. Translation: AAA39509.1. X07295 X07301 Genomic DNA. Translation: CAA30274.1. AK002305 mRNA. Translation: BAC24986.1. Frameshift. AK167809 mRNA. Translation: BAE39836.1. AK160553 mRNA. Translation: BAE35869.1. AK135162 mRNA. Translation: BAE22447.1. BC023482 mRNA. Translation: AAH23482.1. DQ402950 mRNA. Translation: ABD77283.1.
IPI	IPI00323592.
PIR	DEMSMM. S01350.
RefSeq	NP_032643.2. NM_008617.2.
UniGene	Mm.297096.
3D structure databases
ProteinModelPortal	P08249.
SMR	P08249. Positions 25-337.
ModBase	Search...
Protein-protein interaction databases
IntAct	P08249. 3 interactions.
PTM databases
PhosphoSite	P08249.
2D gel databases
REPRODUCTION-2DPAGE	P08249.
SWISS-2DPAGE	P08249.
UCD-2DPAGE	P08249.
Proteomic databases
PaxDb	P08249.
PRIDE	P08249.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000019323; ENSMUSP00000019323; ENSMUSG00000019179.
GeneID	17448.
KEGG	mmu:17448.
UCSC	uc008zyz.1. mouse.
Organism-specific databases
CTD	4191.
MGI	MGI:97050. Mdh2.
Phylogenomic databases
eggNOG	COG0039.
GeneTree	ENSGT00390000016686.
HOGENOM	HOG000213792.
HOVERGEN	HBG001662.
InParanoid	P08249.
KO	K00026.
OMA	VEVKGFA.
OrthoDB	EOG4MKNGM.
Gene expression databases
Bgee	P08249.
CleanEx	MM_MDH2.
Genevestigator	P08249.
GermOnline	ENSMUSG00000019179. Mus musculus.
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
ChiTaRS	Mdh2. mouse.
NextBio	292084.
SOURCE	Search...

Entry information

Entry name

MDHM_MOUSE

Accession

Primary (citable) accession number: P08249
Secondary accession number(s): Q0QF44, Q8CF79, Q8R1P0

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 1, 1988
Last sequence update:	May 1, 2007
Last modified:	April 3, 2013
This is version 137 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Relevant documents

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

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

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

PTM databases

2D gel databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents