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Protein

Malate dehydrogenase, mitochondrial

Gene

MDH2

Organism
Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at transcript 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 sitei104SubstratePROSITE-ProRule annotation1
Binding sitei110SubstratePROSITE-ProRule annotation1
Binding sitei117NADBy similarity1
Binding sitei142SubstratePROSITE-ProRule annotation1
Binding sitei176SubstratePROSITE-ProRule annotation1
Active sitei200Proton acceptorBy similarity1
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

Names & Taxonomyi

Protein namesi
Recommended name:
Malate dehydrogenase, mitochondrial (EC:1.1.1.37)
Gene namesi
Name:MDH2
OrganismiPongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii)
Taxonomic identifieri9601 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaePongo
Proteomesi
  • UP000001595 Componenti: Unplaced

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Transit peptidei1 – 24MitochondrionBy similarityAdd BLAST24
ChainiPRO_000028504425 – 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

PRIDEiQ5NVR2.

Interactioni

Subunit structurei

Homodimer.By similarity

Structurei

3D structure databases

ProteinModelPortaliQ5NVR2.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

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

Keywords - Domaini

Transit peptide

Phylogenomic databases

HOVERGENiHBG001662.
InParanoidiQ5NVR2.
KOiK00026.

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.

Q5NVR2-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLSALARPAS AVLRRSFSTS AQNNAKVAVL GASGGIGQPL SLLLKNSPLV
60 70 80 90 100
SRLTLYDIAH TPGVAADLSH IETKATVKGY LGPEQLPDCL KGCDVVVIPA
110 120 130 140 150
GVPRKPGMTR DDLFNTNATI VATLTSACAQ HCPEAMICVI ANPVNSTIPI
160 170 180 190 200
TAEVFKKHGV YNPNKIFGVT TLDIVRANTF VAELKGLDPA RVNVPVIGGH
210 220 230 240 250
AGKTIIPLIS QCTPKVDFPQ DQLTALTGRI QEAGTEVVKA KAGAGSATLS
260 270 280 290 300
MAYAGARFVF SLVDAMNGKE GVVECSFVKS QETECTYFST PLLLGKKGIE
310 320 330
KNLGIGKVSS FEEKMISDAI PELKASIKKG EDFVKTLK
Length:338
Mass (Da):35,577
Last modified:January 4, 2005 - v1
Checksum:i24F1E70F25AD20A4
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CR925943 mRNA. Translation: CAI29601.1.
RefSeqiNP_001127677.1. NM_001134205.1.

Genome annotation databases

GeneIDi100174759.
KEGGipon:100174759.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CR925943 mRNA. Translation: CAI29601.1.
RefSeqiNP_001127677.1. NM_001134205.1.

3D structure databases

ProteinModelPortaliQ5NVR2.
ModBaseiSearch...
MobiDBiSearch...

Proteomic databases

PRIDEiQ5NVR2.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi100174759.
KEGGipon:100174759.

Organism-specific databases

CTDi4191.

Phylogenomic databases

HOVERGENiHBG001662.
InParanoidiQ5NVR2.
KOiK00026.

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_PONAB
AccessioniPrimary (citable) accession number: Q5NVR2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 1, 2007
Last sequence update: January 4, 2005
Last modified: October 5, 2016
This is version 80 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. 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.