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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.PROSITE-ProRule annotation

Enzyme regulationi

Enzyme activity is enhanced by acetylation.By similarity

Sites

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

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi31 – 377NADBy similarity
Nucleotide bindingi140 – 1423NADBy 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. mitochondrion Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 2424Mitochondrion1 PublicationAdd
BLAST
Chaini25 – 338314Malate dehydrogenase, mitochondrialPRO_0000018630Add
BLAST

Amino acid modifications

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

1
338
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi26 – 316Combined sources
Helixi37 – 459Combined sources
Beta strandi51 – 6010Combined sources
Helixi61 – 688Combined sources
Beta strandi71 – 744Combined sources
Beta strandi76 – 827Combined sources
Helixi83 – 853Combined sources
Helixi86 – 905Combined sources
Beta strandi94 – 985Combined sources
Helixi110 – 1134Combined sources
Helixi114 – 13118Combined sources
Beta strandi135 – 1395Combined sources
Helixi144 – 15714Combined sources
Beta strandi165 – 1684Combined sources
Helixi171 – 18414Combined sources
Helixi189 – 1913Combined sources
Beta strandi196 – 1983Combined sources
Helixi202 – 2043Combined sources
Beta strandi205 – 2073Combined sources
Helixi209 – 2113Combined sources
Helixi220 – 24122Combined sources
Helixi249 – 26719Combined sources
Beta strandi273 – 2797Combined sources
Beta strandi282 – 29514Combined sources
Beta strandi298 – 3025Combined sources
Helixi310 – 33425Combined sources

3D structure databases

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

Miscellaneous databases

EvolutionaryTraceiP00346.

Family & Domainsi

Sequence similaritiesi

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

Keywords - Domaini

Transit peptide

Phylogenomic databases

HOVERGENiHBG001662.
InParanoidiP00346.

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

        10         20         30         40         50
MLSALARPAG AALRRSFSTS XQNNAKVAVL GASGGIGQPL SLLLKNSPLV
60 70 80 90 100
SRLTLYDIAH TPGVAADLSH IETRATVKGY LGPEQLPDCL KGCDVVVIPA
110 120 130 140 150
GVPRKPGMTR DDLFNTNATI VATLTAACAQ HCPDAMICII SNPVNSTIPI
160 170 180 190 200
TAEVFKKHGV YNPNKIFGVT TLDIVRANAF VAELKGLDPA RVSVPVIGGH
210 220 230 240 250
AGKTIIPLIS QCTPKVDFPQ DQLSTLTGRI QEAGTEVVKA KAGAGSATLS
260 270 280 290 300
MAYAGARFVF SLVDAMNGKE GVVECSFVKS QETDCPYFST PLLLGKKGIE
310 320 330
KNLGIGKISP FEEKMIAEAI PELKASIKKG EEFVKNMK
Length:338
Mass (Da):35,596
Last modified:November 1, 1997 - v2
Checksum:iB0435E87383D0B1E
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti120 – 1201I → M in AAA31071. (PubMed:3038184)Curated
Sequence conflicti126 – 1261A → V in AAA31071. (PubMed:3038184)Curated
Sequence conflicti150 – 1501I → M in AAA31071. (PubMed:3038184)Curated
Sequence conflicti304 – 3041G → R in AAA31071. (PubMed:3038184)Curated
Sequence conflicti337 – 3371M → T in AAA31071. (PubMed:3038184)Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z81157 mRNA. Translation: CAB03545.1.
M16427 mRNA. Translation: AAA31071.1.
PIRiA00355. DEPGMM.
UniGeneiSsc.12417.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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:
PDBei
RCSB PDBi
PDBji
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.
InParanoidi P00346.

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: November 26, 2014
This is version 120 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