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P00346 (MDHM_PIG) Reviewed, UniProtKB/Swiss-Prot

Last modified March 19, 2014. Version 115. 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
OrganismSus scrofa (Pig) [Reference proteome]
Taxonomic identifier9823 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaSuinaSuidaeSus

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. Ref.4

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.

Sequence similarities

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 2424Mitochondrion Ref.2
Chain25 – 338314Malate dehydrogenase, mitochondrial
PRO_0000018630

Regions

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

Sites

Active site2001Proton acceptor
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 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 conflict1201I → M in AAA31071. Ref.3
Sequence conflict1261A → V in AAA31071. Ref.3
Sequence conflict1501I → M in AAA31071. Ref.3
Sequence conflict3041G → R in AAA31071. Ref.3
Sequence conflict3371M → T in AAA31071. Ref.3

Secondary structure

................................................ 338
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P00346 [UniParc].

Last modified November 1, 1997. Version 2.
Checksum: B0435E87383D0B1E

FASTA33835,596
        10         20         30         40         50         60 
MLSALARPAG AALRRSFSTS XQNNAKVAVL GASGGIGQPL SLLLKNSPLV SRLTLYDIAH 

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

       130        140        150        160        170        180 
VATLTAACAQ HCPDAMICII SNPVNSTIPI TAEVFKKHGV YNPNKIFGVT TLDIVRANAF 

       190        200        210        220        230        240 
VAELKGLDPA RVSVPVIGGH AGKTIIPLIS QCTPKVDFPQ DQLSTLTGRI QEAGTEVVKA 

       250        260        270        280        290        300 
KAGAGSATLS MAYAGARFVF SLVDAMNGKE GVVECSFVKS QETDCPYFST PLLLGKKGIE 

       310        320        330 
KNLGIGKISP FEEKMIAEAI PELKASIKKG EEFVKNMK 

« Hide

References

« Hide 'large scale' references
[1]"Evaluation and characterization of a porcine small intestine cDNA library: analysis of 839 clones."
Winteroe A.K., Fredholm M., Davies W.
Mamm. Genome 7:509-517(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-40.
Tissue: Small intestine.
[2]"Amino acid sequence homology among the 2-hydroxy acid dehydrogenases: mitochondrial and cytoplasmic malate dehydrogenases form a homologous system with lactate dehydrogenase."
Birktoft J.J., Fernley R.T., Bradshaw R.A., Banaszak L.J.
Proc. Natl. Acad. Sci. U.S.A. 79:6166-6170(1982) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 25-338.
[3]"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] OF 41-338.
[4]"Refined crystal structure of mitochondrial malate dehydrogenase from porcine heart and the consensus structure for dicarboxylic acid oxidoreductases."
Gleason W.B., Fu Z., Birktoft J.J., Banaszak L.J.
Biochemistry 33:2078-2088(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) IN COMPLEX WITH SUBSTRATE ANALOG, SUBUNIT.
Tissue: Heart.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
Z81157 mRNA. Translation: CAB03545.1.
M16427 mRNA. Translation: AAA31071.1.
PIRDEPGMM. A00355.
UniGeneSsc.12417.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1MLDX-ray1.83A/B/C/D25-338[»]
ProteinModelPortalP00346.
SMRP00346. Positions 25-337.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActP00346. 3 interactions.
MINTMINT-8375368.

Chemistry

ChEMBLCHEMBL3444.

Proteomic databases

PRIDEP00346.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Phylogenomic databases

HOVERGENHBG001662.

Enzyme and pathway databases

SABIO-RKP00346.

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.
PTHR11540:SF1. PTHR11540:SF1. 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

EvolutionaryTraceP00346.

Entry information

Entry nameMDHM_PIG
AccessionPrimary (citable) accession number: P00346
Secondary accession number(s): Q95308
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: November 1, 1997
Last modified: March 19, 2014
This is version 115 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references