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Reviewed, UniProtKB/Swiss-Prot P08249 (MDHM_MOUSE)

Last modified June 16, 2009. Version 101. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Malate dehydrogenase, mitochondrial
    EC=1.1.1.37
Gene names
Name: Mdh2
Synonyms: Mor1
OrganismMus musculus (Mouse)
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMus

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.

Subunit structure

Homodimer.

Subcellular location

Mitochondrion matrix.

Post-translational modification

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

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 residue561Phosphotyrosine By similarity
Modified residue1571N6-acetyllysine Ref.7
Modified residue2391N6-acetyllysine Ref.7
Modified residue3141N6-acetyllysine 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
P08249-1 [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: 3038184] [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: 3379635] [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: 16141072] [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: 15489334] [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: 16751257] [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: 16916647] [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

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.
IPIIPI00323592.
PIRDEMSMM. S01350.
RefSeqNP_032643.2.
UniGeneMm.297096

3D structure databases

HSSPHSSP built from PDB template 1MLD based on UniProtKB P00346.
SMRP08249. Positions 25-337.
ModBaseSearch...

PTM databases

PhosphoSiteP08249.

2-D gel databases

SWISS-2DPAGEP08249.
REPRODUCTION-2DPAGEP08249.

Proteomic databases

PRIDEP08249.

Genome annotation databases

EnsemblENSMUSG00000019179. Mus musculus. [Contig view]
GeneID17448.
KEGGmmu:17448.
NMPDRfig|10090.3.peg.12582.

Organism-specific databases

MGIMGI:97050. Mdh2.

Phylogenomic databases

HOGENOMP08249.
HOVERGENP08249.
OMAP08249. VRSEETE.

Enzyme and pathway databases

BRENDA1.1.1.37. 244.

Gene expression databases

ArrayExpressP08249.
BgeeP08249.
CleanExMM_MDH2.
GermOnlineENSMUSG00000019179. Mus musculus.

Family and domain databases

InterProIPR001557. 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]
Gene3DG3DSA:3.90.110.10. lact_mal_DH. 1 hit.
G3DSA:3.40.50.720. NAD(P)-bd. 1 hit.
PANTHERPTHR11540:SF1. MDH_euk_g_bac. 1 hit.
PfamPF02866. Ldh_1_C. 1 hit.
PF00056. Ldh_1_N. 1 hit.
[Graphical view]
PIRSFPIRSF000102. Lac_mal_DH. 1 hit.
TIGRFAMsTIGR01772. MDH_euk_gproteo. 1 hit.
PROSITEPS00068. MDH. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

NextBio292084.
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: June 16, 2009
This is version 101 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

Relevant documents

MGD cross-references

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

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents