Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Malate dehydrogenase, mitochondrial

Gene

MDH2

Organism
Sus scrofa (Pig)
Status
Reviewed-Annotation score: 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)DescriptionActionsGraphical viewLength
Binding sitei57NADBy similarity1
Binding sitei104Substrate1
Binding sitei110Substrate1
Binding sitei117NADBy similarity1
Binding sitei142Substrate1
Binding sitei176Substrate1
Active sitei200Proton acceptor1
Binding sitei251NADBy similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi31 – 37NADBy similarity7
Nucleotide bindingi140 – 142NADBy similarity3

GO - Molecular functioni

GO - Biological processi

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
Proteomesi
  • UP000008227 Componenti: Unplaced

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

Pathology & Biotechi

Chemistry databases

ChEMBLiCHEMBL3444.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Transit peptidei1 – 24Mitochondrion1 PublicationAdd BLAST24
ChainiPRO_000001863025 – 338Malate dehydrogenase, mitochondrialAdd BLAST314

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi33O-linked (GlcNAc)By similarity1
Modified residuei78N6-acetyllysine; alternateBy similarity1
Modified residuei78N6-succinyllysine; alternateBy similarity1
Modified residuei91N6-acetyllysine; alternateBy similarity1
Modified residuei91N6-succinyllysine; alternateBy similarity1
Modified residuei165N6-acetyllysineBy similarity1
Modified residuei185N6-acetyllysine; alternateBy similarity1
Modified residuei185N6-succinyllysine; alternateBy similarity1
Modified residuei203N6-succinyllysineBy similarity1
Modified residuei215N6-acetyllysine; alternateBy similarity1
Modified residuei215N6-succinyllysine; alternateBy similarity1
Modified residuei239N6-acetyllysine; alternateBy similarity1
Modified residuei239N6-malonyllysine; alternateBy similarity1
Modified residuei239N6-succinyllysine; alternateBy similarity1
Modified residuei246PhosphoserineBy similarity1
Modified residuei269N6-succinyllysineBy similarity1
Modified residuei296N6-acetyllysine; alternateBy similarity1
Modified residuei296N6-succinyllysine; alternateBy similarity1
Modified residuei301N6-acetyllysine; alternateBy similarity1
Modified residuei301N6-succinyllysine; alternateBy similarity1
Modified residuei307N6-acetyllysine; alternateBy similarity1
Modified residuei307N6-malonyllysine; alternateBy similarity1
Modified residuei307N6-succinyllysine; alternateBy similarity1
Modified residuei314N6-acetyllysine; alternateBy similarity1
Modified residuei314N6-succinyllysine; alternateBy similarity1
Modified residuei324N6-acetyllysine; alternateBy similarity1
Modified residuei324N6-succinyllysine; alternateBy similarity1
Modified residuei326PhosphoserineBy similarity1
Modified residuei328N6-acetyllysine; alternateBy similarity1
Modified residuei328N6-succinyllysine; alternateBy similarity1
Modified residuei329N6-acetyllysine; alternateBy similarity1
Modified residuei329N6-malonyllysine; alternateBy similarity1
Modified residuei335N6-acetyllysine; alternateBy similarity1
Modified residuei335N6-succinyllysine; alternateBy similarity1

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, Phosphoprotein

Proteomic databases

PaxDbiP00346.
PeptideAtlasiP00346.
PRIDEiP00346.

PTM databases

iPTMnetiP00346.

Interactioni

Subunit structurei

Homodimer.1 Publication

Protein-protein interaction databases

IntActiP00346. 3 interactors.
MINTiMINT-8375368.
STRINGi9823.ENSSSCP00000025866.

Chemistry databases

BindingDBiP00346.

Structurei

Secondary structure

1338
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi26 – 31Combined sources6
Helixi37 – 45Combined sources9
Beta strandi51 – 60Combined sources10
Helixi61 – 68Combined sources8
Beta strandi71 – 74Combined sources4
Beta strandi76 – 82Combined sources7
Helixi83 – 85Combined sources3
Helixi86 – 90Combined sources5
Beta strandi94 – 98Combined sources5
Helixi110 – 113Combined sources4
Helixi114 – 131Combined sources18
Beta strandi135 – 139Combined sources5
Helixi144 – 157Combined sources14
Beta strandi165 – 168Combined sources4
Helixi171 – 184Combined sources14
Helixi189 – 191Combined sources3
Beta strandi196 – 198Combined sources3
Helixi202 – 204Combined sources3
Beta strandi205 – 207Combined sources3
Helixi209 – 211Combined sources3
Helixi220 – 241Combined sources22
Helixi249 – 267Combined sources19
Beta strandi273 – 279Combined sources7
Beta strandi282 – 295Combined sources14
Beta strandi298 – 302Combined sources5
Helixi310 – 334Combined sources25

3D structure databases

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

eggNOGiKOG1494. Eukaryota.
COG0039. LUCA.
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.
SUPFAMiSSF51735. SSF51735. 1 hit.
SSF56327. 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)DescriptionActionsGraphical viewLength
Sequence conflicti120I → M in AAA31071 (PubMed:3038184).Curated1
Sequence conflicti126A → V in AAA31071 (PubMed:3038184).Curated1
Sequence conflicti150I → M in AAA31071 (PubMed:3038184).Curated1
Sequence conflicti304G → R in AAA31071 (PubMed:3038184).Curated1
Sequence conflicti337M → T in AAA31071 (PubMed:3038184).Curated1

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.
PIRiA00355. DEPGMM.
UniGeneiSsc.12417.

3D structure databases

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

Protein-protein interaction databases

IntActiP00346. 3 interactors.
MINTiMINT-8375368.
STRINGi9823.ENSSSCP00000025866.

Chemistry databases

BindingDBiP00346.
ChEMBLiCHEMBL3444.

PTM databases

iPTMnetiP00346.

Proteomic databases

PaxDbiP00346.
PeptideAtlasiP00346.
PRIDEiP00346.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

eggNOGiKOG1494. Eukaryota.
COG0039. LUCA.
HOVERGENiHBG001662.
InParanoidiP00346.

Enzyme and pathway databases

SABIO-RKP00346.

Miscellaneous databases

EvolutionaryTraceiP00346.

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.
SUPFAMiSSF51735. SSF51735. 1 hit.
SSF56327. SSF56327. 1 hit.
TIGRFAMsiTIGR01772. MDH_euk_gproteo. 1 hit.
PROSITEiPS00068. MDH. 1 hit.
[Graphical view]
ProtoNetiSearch...

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 2, 2016
This is version 132 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.