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P11708 (MDHC_PIG) Reviewed, UniProtKB/Swiss-Prot

Last modified March 19, 2014. Version 129. 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·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Malate dehydrogenase, cytoplasmic

EC=1.1.1.37
Alternative name(s):
Cytosolic malate dehydrogenase
Gene names
Name:MDH1
OrganismSus scrofa (Pig) [Reference proteome]
Taxonomic identifier9823 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaSuinaSuidaeSus

Protein attributes

Sequence length334 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. HAMAP-Rule MF_01517

Subunit structure

Homodimer. Ref.5

Subcellular location

Cytoplasm HAMAP-Rule MF_01517.

Post-translational modification

ISGylated By similarity. HAMAP-Rule MF_01517

Acetylation at Lys-118 dramatically enhances enzymatic activity and promotes adipogenic differentiation By similarity. HAMAP-Rule MF_01517

Sequence similarities

Belongs to the LDH/MDH superfamily. MDH type 2 family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed HAMAP-Rule MF_01517
Chain2 – 334333Malate dehydrogenase, cytoplasmic HAMAP-Rule MF_01517
PRO_0000113411

Regions

Nucleotide binding11 – 177NAD HAMAP-Rule MF_01517
Nucleotide binding129 – 1313NAD HAMAP-Rule MF_01517

Sites

Active site1871Proton acceptor
Binding site921Substrate
Binding site981Substrate
Binding site1051NAD
Binding site1121NAD
Binding site1311Substrate
Binding site1621Substrate

Amino acid modifications

Modified residue21N-acetylserine HAMAP-Rule MF_01517
Modified residue1101N6-succinyllysine By similarity
Modified residue1181N6-acetyllysine By similarity
Modified residue1211N6-acetyllysine By similarity
Modified residue2141N6-succinyllysine By similarity
Modified residue2981N6-acetyllysine; alternate By similarity
Modified residue2981N6-succinyllysine; alternate By similarity
Modified residue3181N6-succinyllysine By similarity
Modified residue3331Phosphoserine By similarity

Experimental info

Sequence conflict2381R → Q in AAA31072. Ref.2

Secondary structure

............................................................ 334
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P11708 [UniParc].

Last modified January 23, 2007. Version 4.
Checksum: 2574A8F3C2DD2C84

FASTA33436,454
        10         20         30         40         50         60 
MSEPIRVLVT GAAGQIAYSL LYSIGNGSVF GKDQPIILVL LDITPMMGVL DGVLMELQDC 

        70         80         90        100        110        120 
ALPLLKDVIA TDKEEIAFKD LDVAILVGSM PRRDGMERKD LLKANVKIFK CQGAALDKYA 

       130        140        150        160        170        180 
KKSVKVIVVG NPANTNCLTA SKSAPSIPKE NFSCLTRLDH NRAKAQIALK LGVTSDDVKN 

       190        200        210        220        230        240 
VIIWGNHSST QYPDVNHAKV KLQAKEVGVY EAVKDDSWLK GEFITTVQQR GAAVIKARKL 

       250        260        270        280        290        300 
SSAMSAAKAI CDHVRDIWFG TPEGEFVSMG IISDGNSYGV PDDLLYSFPV TIKDKTWKIV 

       310        320        330 
EGLPINDFSR EKMDLTAKEL AEEKETAFEF LSSA 

« Hide

References

[1]"Cloning, sequencing and functional expression of a DNA encoding pig cytosolic malate dehydrogenase: purification and characterization of the recombinant enzyme."
Trejo F., Costa M., Gelpi J.L., Busquets M., Clarke A.R., Holbrook J.J., Cortes A.
Gene 172:303-308(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Heart.
[2]"Cloning and sequence analysis of cDNAs encoding mammalian cytosolic malate dehydrogenase. Comparison of the amino acid sequences of mammalian and bacterial malate dehydrogenase."
Joh T., Takeshima H., Tsuzuki T., Setoyama C., Shimada K., Tanase S., Kuramitsu S., Kagamiyama H., Morino Y.
J. Biol. Chem. 262:15127-15131(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 46-334.
[3]"Structure of porcine heart cytoplasmic malate dehydrogenase: combining X-ray diffraction and chemical sequence data in structural studies."
Birktoft J.J., Bradshaw R.A., Banaszak L.J.
Biochemistry 26:2722-2734(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS), PARTIAL PROTEIN SEQUENCE.
[4]"Refined crystal structure of cytoplasmic malate dehydrogenase at 2.5-A resolution."
Birktoft J.J., Rhodes G., Banaszak L.J.
Biochemistry 28:6065-6081(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).
[5]"Structural basis of substrate specificity in malate dehydrogenases: crystal structure of a ternary complex of porcine cytoplasmic malate dehydrogenase, alpha-ketomalonate and tetrahydoNAD."
Chapman A.D., Cortes A., Dafforn T.R., Clarke A.R., Brady R.L.
J. Mol. Biol. 285:703-712(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) IN COMPLEX WITH NAD AND SUBSTRATE ANALOG, SUBUNIT.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U44846 mRNA. Translation: AAC48610.1.
M29463 mRNA. Translation: AAA31072.1.
PIRA32472. JC4876.
RefSeqNP_999039.1. NM_213874.1.
UniGeneSsc.11103.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
4MDHX-ray2.50A/B2-334[»]
5MDHX-ray2.40A/B2-334[»]
ProteinModelPortalP11708.
SMRP11708. Positions 2-334.
ModBaseSearch...
MobiDBSearch...

Chemistry

BindingDBP11708.
ChEMBLCHEMBL4048.

Proteomic databases

PRIDEP11708.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID396894.
KEGGssc:396894.

Organism-specific databases

CTD4190.

Phylogenomic databases

HOVERGENHBG006340.
KOK00025.

Enzyme and pathway databases

BioCycMetaCyc:MONOMER-13033.
SABIO-RKP11708.

Family and domain databases

Gene3D3.40.50.720. 1 hit.
3.90.110.10. 1 hit.
HAMAPMF_01517. Malate_dehydrog_2.
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.
IPR011274. Malate_DH_NAD-dep_euk.
IPR010945. Malate_DH_type2.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
PANTHERPTHR23382. PTHR23382. 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.
TIGRFAMsTIGR01759. MalateDH-SF1. 1 hit.
TIGR01758. MDH_euk_cyt. 1 hit.
PROSITEPS00068. MDH. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP11708.

Entry information

Entry nameMDHC_PIG
AccessionPrimary (citable) accession number: P11708
Secondary accession number(s): Q29560
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1989
Last sequence update: January 23, 2007
Last modified: March 19, 2014
This is version 129 of the entry and version 4 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