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P08249 (MDHM_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 150. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Malate dehydrogenase, mitochondrial

EC=1.1.1.37
Gene names
Name:Mdh2
Synonyms:Mor1
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length338 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence 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 processTricarboxylic acid cycle
   Cellular componentMitochondrion
   DomainTransit peptide
   LigandNAD
   Molecular functionOxidoreductase
   PTMAcetylation
   Technical termComplete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processNADH metabolic process

Inferred from electronic annotation. Source: Ensembl

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: Ensembl

tricarboxylic acid cycle

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentmitochondrial inner membrane

Inferred from direct assay PubMed 12865426. Source: MGI

mitochondrial matrix

Inferred from electronic annotation. Source: UniProtKB-SubCell

mitochondrion

Inferred from direct assay PubMed 14651853PubMed 18614015. Source: MGI

nucleus

Inferred from electronic annotation. Source: Ensembl

plasma membrane

Inferred from electronic annotation. Source: Ensembl

   Molecular_functionL-malate dehydrogenase activity

Inferred from direct assay PubMed 5496232. Source: MGI

malate dehydrogenase (NADP+) activity

Inferred from electronic annotation. Source: Ensembl

malate dehydrogenase activity

Inferred from sequence alignment PubMed 15809022. Source: MGI

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 2424Mitochondrion
Chain25 – 338314Malate dehydrogenase, mitochondrial
PRO_0000018629

Regions

Nucleotide binding31 – 377NAD By similarity
Nucleotide binding140 – 1423NAD By similarity

Sites

Active site2001Proton acceptor By similarity
Binding site571NAD By similarity
Binding site1041Substrate
Binding site1101Substrate
Binding site1171NAD By similarity
Binding site1421Substrate
Binding site1761Substrate
Binding site2511NAD By similarity

Amino acid modifications

Modified residue781N6-acetyllysine; alternate Ref.8
Modified residue781N6-succinyllysine; alternate Ref.7
Modified residue911N6-acetyllysine; alternate Ref.8
Modified residue911N6-succinyllysine; alternate Ref.7
Modified residue1651N6-acetyllysine Ref.8
Modified residue1851N6-acetyllysine; alternate Ref.8
Modified residue1851N6-succinyllysine; alternate Ref.7
Modified residue2031N6-succinyllysine Ref.7
Modified residue2151N6-acetyllysine; alternate Ref.8
Modified residue2151N6-succinyllysine; alternate Ref.7
Modified residue2391N6-acetyllysine; alternate Ref.7 Ref.8
Modified residue2391N6-malonyllysine; alternate By similarity
Modified residue2391N6-succinyllysine; alternate Ref.7
Modified residue2691N6-succinyllysine Ref.7
Modified residue2961N6-acetyllysine; alternate Ref.8
Modified residue2961N6-succinyllysine; alternate Ref.7
Modified residue3011N6-acetyllysine; alternate Ref.8
Modified residue3011N6-succinyllysine; alternate Ref.7
Modified residue3071N6-acetyllysine; alternate Ref.8
Modified residue3071N6-malonyllysine; alternate By similarity
Modified residue3071N6-succinyllysine; alternate Ref.7
Modified residue3141N6-acetyllysine; alternate Ref.8
Modified residue3141N6-succinyllysine; alternate Ref.7
Modified residue3241N6-acetyllysine; alternate Ref.8
Modified residue3241N6-succinyllysine; alternate Ref.7
Modified residue3281N6-acetyllysine; alternate By similarity
Modified residue3281N6-succinyllysine; alternate By similarity
Modified residue3291N6-acetyllysine; alternate Ref.8
Modified residue3291N6-malonyllysine; alternate By similarity
Modified residue3351N6-acetyllysine; alternate Ref.8
Modified residue3351N6-succinyllysine; alternate Ref.7

Experimental info

Sequence conflict761N → K in AAA39509. Ref.1
Sequence conflict2691K → L in AAA39509. Ref.1
Sequence conflict2691K → L in CAA30274. Ref.2

Sequences

Sequence LengthMass (Da)Tools
P08249 [UniParc].

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

FASTA33835,611
        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' 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. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai 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, IDENTIFICATION BY MASS SPECTROMETRY.
Strain: C57BL/6 and OF1.
Tissue: Brain and Hippocampus.
[7]"SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-239, SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-78; LYS-91; LYS-185; LYS-203; LYS-215; LYS-239; LYS-269; LYS-296; LYS-301; LYS-307; LYS-314; LYS-324 AND LYS-335, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Embryonic fibroblast and Liver.
[8]"Label-free quantitative proteomics of the lysine acetylome in mitochondria identifies substrates of SIRT3 in metabolic pathways."
Rardin M.J., Newman J.C., Held J.M., Cusack M.P., Sorensen D.J., Li B., Schilling B., Mooney S.D., Kahn C.R., Verdin E., Gibson B.W.
Proc. Natl. Acad. Sci. U.S.A. 110:6601-6606(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-78; LYS-91; LYS-165; LYS-185; LYS-215; LYS-239; LYS-296; LYS-301; LYS-307; LYS-314; LYS-324; LYS-329 AND LYS-335, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Liver.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M16229 mRNA. Translation: AAA39509.1.
X07295 expand/collapse EMBL AC list , X07296, X07297, X07298, X07299, X07300, 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.
CCDSCCDS19746.1.
PIRDEMSMM. S01350.
RefSeqNP_032643.2. NM_008617.2.
UniGeneMm.297096.

3D structure databases

ProteinModelPortalP08249.
SMRP08249. Positions 25-337.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid201467. 3 interactions.
IntActP08249. 7 interactions.
MINTMINT-4101644.

PTM databases

PhosphoSiteP08249.

2D gel databases

REPRODUCTION-2DPAGEP08249.
SWISS-2DPAGEP08249.
UCD-2DPAGEP08249.

Proteomic databases

MaxQBP08249.
PaxDbP08249.
PRIDEP08249.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000019323; ENSMUSP00000019323; ENSMUSG00000019179.
GeneID17448.
KEGGmmu:17448.
UCSCuc008zyz.1. mouse.

Organism-specific databases

CTD4191.
MGIMGI:97050. Mdh2.

Phylogenomic databases

eggNOGCOG0039.
GeneTreeENSGT00390000016686.
HOGENOMHOG000213792.
HOVERGENHBG001662.
InParanoidP08249.
KOK00026.
OMAVEVKGFA.
OrthoDBEOG74R1R7.
PhylomeDBP08249.
TreeFamTF300834.

Gene expression databases

ArrayExpressP08249.
BgeeP08249.
CleanExMM_MDH2.
GenevestigatorP08249.

Family and domain databases

Gene3D3.40.50.720. 1 hit.
3.90.110.10. 1 hit.
InterProIPR001557. 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]
PANTHERPTHR11540. PTHR11540. 1 hit.
PfamPF02866. Ldh_1_C. 1 hit.
PF00056. Ldh_1_N. 1 hit.
[Graphical view]
PIRSFPIRSF000102. Lac_mal_DH. 1 hit.
SUPFAMSSF56327. SSF56327. 1 hit.
TIGRFAMsTIGR01772. MDH_euk_gproteo. 1 hit.
PROSITEPS00068. MDH. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSMdh2. mouse.
NextBio292084.
PROP08249.
SOURCESearch...

Entry information

Entry nameMDHM_MOUSE
AccessionPrimary (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: July 9, 2014
This is version 150 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

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