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P04636 (MDHM_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 136. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | 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
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

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.

Tissue specificity

Expressed in flagella of epididymal sperm. Ref.5

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.

Sequence similarities

Belongs to the LDH/MDH superfamily. MDH type 1 family.

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 direct assay PubMed 12351438. Source: RGD

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 direct assay PubMed 12351438PubMed 1898089PubMed 938457. Source: RGD

oxaloacetate metabolic process

Inferred from direct assay PubMed 938457. Source: RGD

tricarboxylic acid cycle

Inferred from direct assay PubMed 938457. Source: RGD

   Cellular_componentmitochondrial inner membrane

Inferred from electronic annotation. Source: Ensembl

mitochondrial matrix

Inferred from direct assay PubMed 6409145. Source: RGD

mitochondrion

Inferred from direct assay PubMed 16737718PubMed 1898089PubMed 938457. Source: RGD

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 12351438PubMed 938457. Source: RGD

malate dehydrogenase (NADP+) activity

Inferred from direct assay PubMed 16737718. Source: RGD

malate dehydrogenase activity

Inferred from direct assay PubMed 1898089. Source: RGD

protein binding

Inferred from physical interaction PubMed 15809022. Source: RGD

protein self-association

Inferred from direct assay PubMed 3580173. Source: RGD

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 2424Mitochondrion Ref.3
Chain25 – 338314Malate dehydrogenase, mitochondrial
PRO_0000018631

Regions

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

Sites

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

Amino acid modifications

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

Experimental info

Sequence conflict2291R → K in CAA27812. Ref.1

Sequences

Sequence LengthMass (Da)Tools
P04636 [UniParc].

Last modified January 9, 2007. Version 2.
Checksum: 13849CCFB78C87E7

FASTA33835,684
        10         20         30         40         50         60 
MLSALARPVG AALRRSFSTS AQNNAKVAVL GASGGIGQPL SLLLKNSPLV SRLTLYDIAH 

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

       130        140        150        160        170        180 
VATLTAACAQ HCPEAMICII SNPVNSTIPI TAEVFKKHGV YNPNKIFGVT TLDIVRANTF 

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

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

       310        320        330 
KNLGIGKITP FEEKMIAEAI PELKASIKKG EDFVKNMK 

« Hide

References

« Hide 'large scale' references
[1]"Isolation and nucleotide sequence of a cDNA clone encoding rat mitochondrial malate dehydrogenase."
Grant P.M., Tellam J., May V.L., Strauss A.W.
Nucleic Acids Res. 14:6053-6066(1986) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"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].
Tissue: Pituitary anterior lobe.
[3]"Comparison of the precursor and mature forms of rat heart mitochondrial malate dehydrogenase."
Grant P.M., Roderick S.L., Grant G.A., Banaszak L.J., Strauss A.W.
Biochemistry 26:128-134(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 25-338.
[4]Lubec G., Afjehi-Sadat L., Chen W.-Q., Kang S.U.
Submitted (JUL-2007) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 27-52; 53-74; 166-185; 192-203; 216-239; 242-296 AND 308-324, IDENTIFICATION BY MASS SPECTROMETRY.
Strain: Sprague-Dawley.
Tissue: Brain, Hippocampus and Spinal cord.
[5]"Identification of novel immunodominant epididymal sperm proteins using combinatorial approach."
Khan S.A., Suryawanshi A.R., Ranpura S.A., Jadhav S.V., Khole V.V.
Reproduction 138:81-93(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY, TISSUE SPECIFICITY.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X04240 mRNA. Translation: CAA27812.1.
BC063165 mRNA. Translation: AAH63165.1.
PIRDERTMM. A25509.
RefSeqNP_112413.2. NM_031151.2.
UniGeneRn.1011.

3D structure databases

ProteinModelPortalP04636.
SMRP04636. Positions 25-337.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid249687. 1 interaction.
IntActP04636. 2 interactions.

Chemistry

ChEMBLCHEMBL2176835.

PTM databases

PhosphoSiteP04636.

2D gel databases

World-2DPAGE0004:P04636.

Proteomic databases

PaxDbP04636.
PRIDEP04636.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSRNOT00000001958; ENSRNOP00000001958; ENSRNOG00000001440.
GeneID81829.
KEGGrno:81829.
UCSCRGD:619719. rat.

Organism-specific databases

CTD4191.
RGD619719. Mdh2.

Phylogenomic databases

eggNOGCOG0039.
GeneTreeENSGT00390000016686.
HOGENOMHOG000213792.
HOVERGENHBG001662.
InParanoidP04636.
KOK00026.
OMAMVAEAMS.
OrthoDBEOG74R1R7.
PhylomeDBP04636.
TreeFamTF300834.

Gene expression databases

GenevestigatorP04636.

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

NextBio615775.
PROP04636.

Entry information

Entry nameMDHM_RAT
AccessionPrimary (citable) accession number: P04636
Secondary accession number(s): Q6GSM4
Entry history
Integrated into UniProtKB/Swiss-Prot: August 13, 1987
Last sequence update: January 9, 2007
Last modified: June 11, 2014
This is version 136 of the entry and version 2 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