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Protein

Malate dehydrogenase, cytoplasmic

Gene

Mdh1

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Catalytic activityi

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei92 – 921SubstrateBy similarity
Binding sitei98 – 981SubstrateBy similarity
Binding sitei105 – 1051NADBy similarity
Binding sitei112 – 1121NADBy similarity
Binding sitei131 – 1311SubstrateBy similarity
Binding sitei162 – 1621SubstrateBy similarity
Active sitei187 – 1871Proton acceptorBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi11 – 177NADBy similarity
Nucleotide bindingi129 – 1313NADBy similarity

GO - Molecular functioni

  • L-malate dehydrogenase activity Source: RGD
  • malate dehydrogenase activity Source: RGD
  • NAD binding Source: RGD

GO - Biological processi

  • carbohydrate metabolic process Source: InterPro
  • malate metabolic process Source: RGD
  • NADH metabolic process Source: RGD
  • NAD metabolic process Source: RGD
  • oxaloacetate metabolic process Source: RGD
  • regulation of mitochondrion degradation Source: Ensembl
  • 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

ReactomeiREACT_331968. Gluconeogenesis.

Names & Taxonomyi

Protein namesi
Recommended name:
Malate dehydrogenase, cytoplasmic (EC:1.1.1.37)
Alternative name(s):
Cytosolic malate dehydrogenase
Gene namesi
Name:Mdh1
Synonyms:Mdh
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
ProteomesiUP000002494 Componenti: Chromosome 14

Organism-specific databases

RGDi3072. Mdh1.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11RemovedBy similarity
Chaini2 – 334333Malate dehydrogenase, cytoplasmicPRO_0000226737Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserineBy similarity
Modified residuei110 – 1101N6-succinyllysineBy similarity
Modified residuei118 – 1181N6-acetyllysineBy similarity
Modified residuei121 – 1211N6-acetyllysineBy similarity
Modified residuei214 – 2141N6-succinyllysineBy similarity
Modified residuei241 – 2411PhosphoserineBy similarity
Modified residuei298 – 2981N6-acetyllysine; alternateBy similarity
Modified residuei298 – 2981N6-succinyllysine; alternateBy similarity
Modified residuei318 – 3181N6-succinyllysineBy similarity
Modified residuei333 – 3331PhosphoserineBy similarity

Post-translational modificationi

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

Keywords - PTMi

Acetylation, Phosphoprotein, Ubl conjugation

Proteomic databases

PaxDbiO88989.
PRIDEiO88989.

2D gel databases

World-2DPAGE0004:O88989.

PTM databases

PhosphoSiteiO88989.

Expressioni

Gene expression databases

GenevisibleiO88989. RN.

Interactioni

Subunit structurei

Homodimer.By similarity

Protein-protein interaction databases

BioGridi246700. 3 interactions.
IntActiO88989. 1 interaction.
MINTiMINT-4580226.
STRINGi10116.ENSRNOP00000011429.

Structurei

3D structure databases

ProteinModelPortaliO88989.
SMRiO88989. Positions 2-334.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiCOG0039.
GeneTreeiENSGT00530000063410.
HOGENOMiHOG000220953.
HOVERGENiHBG006340.
InParanoidiO88989.
KOiK00025.
OMAiWNNDVFL.
OrthoDBiEOG78H3TM.
PhylomeDBiO88989.
TreeFamiTF105826.

Family and domain databases

Gene3Di3.40.50.720. 1 hit.
3.90.110.10. 1 hit.
HAMAPiMF_01517. Malate_dehydrog_2.
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.
IPR011274. Malate_DH_NAD-dep_euk.
IPR010945. Malate_DH_type2.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
PANTHERiPTHR23382. PTHR23382. 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.
TIGRFAMsiTIGR01759. MalateDH-SF1. 1 hit.
TIGR01758. MDH_euk_cyt. 1 hit.
PROSITEiPS00068. MDH. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

O88989-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSEPIRVLVT GAAGQIAYSL LYSIGNGSVF GKDQPIILVL LDITPMMGVL
60 70 80 90 100
DGVLMELQDC ALPLLQDVIA TDKEEVAFKD LDVAVLVGSM PRREGMERKD
110 120 130 140 150
LLKANVKIFK SQGAALEKYA KKSVKVIVVG NPANTNCLTA SKSAPSIPKE
160 170 180 190 200
NFSCLTRLDH NRAKSQIALK LGVTADDVKN VIIWGNHSST QYPDVNHAKV
210 220 230 240 250
KLQGKEVGVY EALKDDSWLK GEFITTVQQR GAAVIKARKL SSAMSAAKAI
260 270 280 290 300
SDHIRDIWFG TPEGEFVSMG VISDGNSYGV PDDLLYSFPV VIKNKTWKFV
310 320 330
EGLPINDFSR EKMDLTAKEL TEEKETAFEF LSSA
Length:334
Mass (Da):36,483
Last modified:January 23, 2007 - v3
Checksum:i8F6778722A607B3C
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti251 – 2511S → A in AAC26799 (Ref. 4) Curated
Sequence conflicti276 – 2761N → D in AAH59124 (PubMed:15489334).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF093773 mRNA. Translation: AAC64180.1.
BC059124 mRNA. Translation: AAH59124.1.
AF075574 mRNA. Translation: AAC26799.1.
RefSeqiNP_150238.1. NM_033235.1.
UniGeneiRn.13492.

Genome annotation databases

EnsembliENSRNOT00000011429; ENSRNOP00000011429; ENSRNOG00000008103.
GeneIDi24551.
KEGGirno:24551.
UCSCiRGD:3072. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF093773 mRNA. Translation: AAC64180.1.
BC059124 mRNA. Translation: AAH59124.1.
AF075574 mRNA. Translation: AAC26799.1.
RefSeqiNP_150238.1. NM_033235.1.
UniGeneiRn.13492.

3D structure databases

ProteinModelPortaliO88989.
SMRiO88989. Positions 2-334.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi246700. 3 interactions.
IntActiO88989. 1 interaction.
MINTiMINT-4580226.
STRINGi10116.ENSRNOP00000011429.

PTM databases

PhosphoSiteiO88989.

2D gel databases

World-2DPAGE0004:O88989.

Proteomic databases

PaxDbiO88989.
PRIDEiO88989.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000011429; ENSRNOP00000011429; ENSRNOG00000008103.
GeneIDi24551.
KEGGirno:24551.
UCSCiRGD:3072. rat.

Organism-specific databases

CTDi4190.
RGDi3072. Mdh1.

Phylogenomic databases

eggNOGiCOG0039.
GeneTreeiENSGT00530000063410.
HOGENOMiHOG000220953.
HOVERGENiHBG006340.
InParanoidiO88989.
KOiK00025.
OMAiWNNDVFL.
OrthoDBiEOG78H3TM.
PhylomeDBiO88989.
TreeFamiTF105826.

Enzyme and pathway databases

ReactomeiREACT_331968. Gluconeogenesis.

Miscellaneous databases

NextBioi603654.
PROiO88989.

Gene expression databases

GenevisibleiO88989. RN.

Family and domain databases

Gene3Di3.40.50.720. 1 hit.
3.90.110.10. 1 hit.
HAMAPiMF_01517. Malate_dehydrog_2.
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.
IPR011274. Malate_DH_NAD-dep_euk.
IPR010945. Malate_DH_type2.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
PANTHERiPTHR23382. PTHR23382. 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.
TIGRFAMsiTIGR01759. MalateDH-SF1. 1 hit.
TIGR01758. MDH_euk_cyt. 1 hit.
PROSITEiPS00068. MDH. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Cloning of rat cytosolic malate dehydrogenase."
    Achenbach P., Steinbrenner H., Reindl G., Seissler J.
    Submitted (SEP-1998) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Pituitary.
  3. Lubec G., Afjehi-Sadat L., Diao W., Kang S.U.
    Submitted (JUL-2007) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 7-32; 80-92; 126-157; 171-199; 206-230; 239-255; 299-310 AND 319-334, IDENTIFICATION BY MASS SPECTROMETRY.
    Strain: Sprague-Dawley.
    Tissue: Brain, Hippocampus and Spinal cord.
  4. "Partial sequence of rat malate dehydrogenase (MDH) mRNA."
    Earley S.
    Submitted (JUN-1998) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 251-284.

Entry informationi

Entry nameiMDHC_RAT
AccessioniPrimary (citable) accession number: O88989
Secondary accession number(s): O88585, Q6PCV2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 7, 2006
Last sequence update: January 23, 2007
Last modified: July 22, 2015
This is version 111 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.