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P00346

- MDHM_PIG

UniProt

P00346 - MDHM_PIG

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Protein
Malate dehydrogenase, mitochondrial
Gene
MDH2
Organism
Sus scrofa (Pig)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Catalytic activityi

(S)-malate + NAD+ = oxaloacetate + NADH.

Enzyme regulationi

Enzyme activity is enhanced by acetylation By similarity.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei57 – 571NAD By similarity
Binding sitei104 – 1041Substrate
Binding sitei110 – 1101Substrate
Binding sitei117 – 1171NAD By similarity
Binding sitei142 – 1421Substrate
Binding sitei176 – 1761Substrate
Active sitei200 – 2001Proton acceptor
Binding sitei251 – 2511NAD By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi31 – 377NAD By similarity
Nucleotide bindingi140 – 1423NAD By similarity

GO - Molecular functioni

  1. L-malate dehydrogenase activity Source: UniProtKB-EC

GO - Biological processi

  1. cellular carbohydrate metabolic process Source: InterPro
  2. internal protein amino acid acetylation Source: UniProtKB
  3. malate metabolic process Source: InterPro
  4. tricarboxylic acid cycle Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Tricarboxylic acid cycle

Keywords - Ligandi

NAD

Enzyme and pathway databases

SABIO-RKP00346.

Names & Taxonomyi

Protein namesi
Recommended name:
Malate dehydrogenase, mitochondrial (EC:1.1.1.37)
Gene namesi
Name:MDH2
OrganismiSus scrofa (Pig)
Taxonomic identifieri9823 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaSuinaSuidaeSus
ProteomesiUP000008227: Unplaced

Subcellular locationi

GO - Cellular componenti

  1. mitochondrial matrix Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 2424Mitochondrion1 Publication
Add
BLAST
Chaini25 – 338314Malate dehydrogenase, mitochondrial
PRO_0000018630Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi33 – 331O-linked (GlcNAc) By similarity
Modified residuei78 – 781N6-acetyllysine; alternate By similarity
Modified residuei78 – 781N6-succinyllysine; alternate By similarity
Modified residuei91 – 911N6-acetyllysine; alternate By similarity
Modified residuei91 – 911N6-succinyllysine; alternate By similarity
Modified residuei165 – 1651N6-acetyllysine By similarity
Modified residuei185 – 1851N6-acetyllysine; alternate By similarity
Modified residuei185 – 1851N6-succinyllysine; alternate By similarity
Modified residuei203 – 2031N6-succinyllysine By similarity
Modified residuei215 – 2151N6-acetyllysine; alternate By similarity
Modified residuei215 – 2151N6-succinyllysine; alternate By similarity
Modified residuei239 – 2391N6-acetyllysine; alternate By similarity
Modified residuei239 – 2391N6-malonyllysine; alternate By similarity
Modified residuei239 – 2391N6-succinyllysine; alternate By similarity
Modified residuei269 – 2691N6-succinyllysine By similarity
Modified residuei296 – 2961N6-acetyllysine; alternate By similarity
Modified residuei296 – 2961N6-succinyllysine; alternate By similarity
Modified residuei301 – 3011N6-acetyllysine; alternate By similarity
Modified residuei301 – 3011N6-succinyllysine; alternate By similarity
Modified residuei307 – 3071N6-acetyllysine; alternate By similarity
Modified residuei307 – 3071N6-malonyllysine; alternate By similarity
Modified residuei307 – 3071N6-succinyllysine; alternate By similarity
Modified residuei314 – 3141N6-acetyllysine; alternate By similarity
Modified residuei314 – 3141N6-succinyllysine; alternate By similarity
Modified residuei324 – 3241N6-acetyllysine; alternate By similarity
Modified residuei324 – 3241N6-succinyllysine; alternate By similarity
Modified residuei328 – 3281N6-acetyllysine; alternate By similarity
Modified residuei328 – 3281N6-succinyllysine; alternate By similarity
Modified residuei329 – 3291N6-acetyllysine; alternate By similarity
Modified residuei329 – 3291N6-malonyllysine; alternate By similarity
Modified residuei335 – 3351N6-acetyllysine; alternate By similarity
Modified residuei335 – 3351N6-succinyllysine; alternate By similarity

Post-translational modificationi

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.

Keywords - PTMi

Acetylation, Glycoprotein

Proteomic databases

PRIDEiP00346.

Interactioni

Subunit structurei

Homodimer.1 Publication

Protein-protein interaction databases

IntActiP00346. 3 interactions.
MINTiMINT-8375368.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi26 – 316
Helixi37 – 459
Beta strandi51 – 6010
Helixi61 – 688
Beta strandi71 – 744
Beta strandi76 – 827
Helixi83 – 853
Helixi86 – 905
Beta strandi94 – 985
Helixi110 – 1134
Helixi114 – 13118
Beta strandi135 – 1395
Helixi144 – 15714
Beta strandi165 – 1684
Helixi171 – 18414
Helixi189 – 1913
Beta strandi196 – 1983
Helixi202 – 2043
Beta strandi205 – 2073
Helixi209 – 2113
Helixi220 – 24122
Helixi249 – 26719
Beta strandi273 – 2797
Beta strandi282 – 29514
Beta strandi298 – 3025
Helixi310 – 33425

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1MLDX-ray1.83A/B/C/D25-338[»]
ProteinModelPortaliP00346.
SMRiP00346. Positions 25-337.

Miscellaneous databases

EvolutionaryTraceiP00346.

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Transit peptide

Phylogenomic databases

HOVERGENiHBG001662.

Family and domain databases

Gene3Di3.40.50.720. 1 hit.
3.90.110.10. 1 hit.
InterProiIPR001557. 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]
PANTHERiPTHR11540. PTHR11540. 1 hit.
PfamiPF02866. Ldh_1_C. 1 hit.
PF00056. Ldh_1_N. 1 hit.
[Graphical view]
PIRSFiPIRSF000102. Lac_mal_DH. 1 hit.
SUPFAMiSSF56327. SSF56327. 1 hit.
TIGRFAMsiTIGR01772. MDH_euk_gproteo. 1 hit.
PROSITEiPS00068. MDH. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P00346-1 [UniParc]FASTAAdd to Basket

« Hide

MLSALARPAG AALRRSFSTS XQNNAKVAVL GASGGIGQPL SLLLKNSPLV    50
SRLTLYDIAH TPGVAADLSH IETRATVKGY LGPEQLPDCL KGCDVVVIPA 100
GVPRKPGMTR DDLFNTNATI VATLTAACAQ HCPDAMICII SNPVNSTIPI 150
TAEVFKKHGV YNPNKIFGVT TLDIVRANAF VAELKGLDPA RVSVPVIGGH 200
AGKTIIPLIS QCTPKVDFPQ DQLSTLTGRI QEAGTEVVKA KAGAGSATLS 250
MAYAGARFVF SLVDAMNGKE GVVECSFVKS QETDCPYFST PLLLGKKGIE 300
KNLGIGKISP FEEKMIAEAI PELKASIKKG EEFVKNMK 338
Length:338
Mass (Da):35,596
Last modified:November 1, 1997 - v2
Checksum:iB0435E87383D0B1E
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti120 – 1201I → M in AAA31071. 1 Publication
Sequence conflicti126 – 1261A → V in AAA31071. 1 Publication
Sequence conflicti150 – 1501I → M in AAA31071. 1 Publication
Sequence conflicti304 – 3041G → R in AAA31071. 1 Publication
Sequence conflicti337 – 3371M → T in AAA31071. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
Z81157 mRNA. Translation: CAB03545.1.
M16427 mRNA. Translation: AAA31071.1.
PIRiA00355. DEPGMM.
UniGeneiSsc.12417.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
Z81157 mRNA. Translation: CAB03545.1 .
M16427 mRNA. Translation: AAA31071.1 .
PIRi A00355. DEPGMM.
UniGenei Ssc.12417.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1MLD X-ray 1.83 A/B/C/D 25-338 [» ]
ProteinModelPortali P00346.
SMRi P00346. Positions 25-337.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

IntActi P00346. 3 interactions.
MINTi MINT-8375368.

Chemistry

ChEMBLi CHEMBL3444.

Proteomic databases

PRIDEi P00346.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Phylogenomic databases

HOVERGENi HBG001662.

Enzyme and pathway databases

SABIO-RK P00346.

Miscellaneous databases

EvolutionaryTracei P00346.

Family and domain databases

Gene3Di 3.40.50.720. 1 hit.
3.90.110.10. 1 hit.
InterProi IPR001557. 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 ]
PANTHERi PTHR11540. PTHR11540. 1 hit.
Pfami PF02866. Ldh_1_C. 1 hit.
PF00056. Ldh_1_N. 1 hit.
[Graphical view ]
PIRSFi PIRSF000102. Lac_mal_DH. 1 hit.
SUPFAMi SSF56327. SSF56327. 1 hit.
TIGRFAMsi TIGR01772. MDH_euk_gproteo. 1 hit.
PROSITEi PS00068. MDH. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.

Entry informationi

Entry nameiMDHM_PIG
AccessioniPrimary (citable) accession number: P00346
Secondary accession number(s): Q95308
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: November 1, 1997
Last modified: September 3, 2014
This is version 117 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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