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Protein

Malate dehydrogenase, cytoplasmic

Gene

MDH1

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.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei92 – 921Substrate
Binding sitei98 – 981Substrate
Binding sitei105 – 1051NAD1 Publication
Binding sitei112 – 1121NAD1 Publication
Binding sitei131 – 1311Substrate
Binding sitei162 – 1621Substrate
Active sitei187 – 1871Proton acceptor

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi11 – 177NAD1 Publication
Nucleotide bindingi129 – 1313NAD1 Publication

GO - Molecular functioni

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

GO - Biological processi

  1. cellular carbohydrate metabolic process Source: InterPro
  2. malate metabolic process Source: InterPro
  3. 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

BioCyciMetaCyc:MONOMER-13033.
SABIO-RKP11708.

Names & Taxonomyi

Protein namesi
Recommended name:
Malate dehydrogenase, cytoplasmic (EC:1.1.1.37)
Alternative name(s):
Cytosolic malate dehydrogenase
Gene namesi
Name:MDH1
OrganismiSus scrofa (Pig)
Taxonomic identifieri9823 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaSuinaSuidaeSus
ProteomesiUP000008227: Unplaced

Subcellular locationi

GO - Cellular componenti

  1. cytosol Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed
Chaini2 – 334333Malate dehydrogenase, cytoplasmicPRO_0000113411Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserine1 Publication
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

PRIDEiP11708.

Interactioni

Subunit structurei

Homodimer.1 Publication

Structurei

Secondary structure

1
334
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi5 – 117Combined sources
Helixi15 – 184Combined sources
Helixi21 – 255Combined sources
Turni26 – 305Combined sources
Beta strandi36 – 416Combined sources
Helixi44 – 463Combined sources
Helixi47 – 5913Combined sources
Beta strandi65 – 728Combined sources
Helixi74 – 774Combined sources
Turni78 – 803Combined sources
Beta strandi82 – 865Combined sources
Turni98 – 1014Combined sources
Helixi102 – 11918Combined sources
Beta strandi125 – 1284Combined sources
Beta strandi130 – 1323Combined sources
Helixi133 – 14210Combined sources
Helixi149 – 1513Combined sources
Beta strandi152 – 1543Combined sources
Helixi157 – 17115Combined sources
Helixi175 – 1773Combined sources
Beta strandi182 – 1854Combined sources
Beta strandi192 – 1943Combined sources
Beta strandi199 – 2013Combined sources
Beta strandi206 – 2083Combined sources
Helixi209 – 2135Combined sources
Helixi216 – 2205Combined sources
Helixi222 – 23817Combined sources
Helixi244 – 25916Combined sources
Beta strandi267 – 2726Combined sources
Beta strandi277 – 2793Combined sources
Beta strandi285 – 2939Combined sources
Beta strandi296 – 2994Combined sources
Helixi307 – 33327Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4MDHX-ray2.50A/B2-334[»]
5MDHX-ray2.40A/B2-334[»]
ProteinModelPortaliP11708.
SMRiP11708. Positions 2-334.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP11708.

Family & Domainsi

Sequence similaritiesi

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

Phylogenomic databases

HOVERGENiHBG006340.
InParanoidiP11708.
KOiK00025.

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.

P11708-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSEPIRVLVT GAAGQIAYSL LYSIGNGSVF GKDQPIILVL LDITPMMGVL
60 70 80 90 100
DGVLMELQDC ALPLLKDVIA TDKEEIAFKD LDVAILVGSM PRRDGMERKD
110 120 130 140 150
LLKANVKIFK CQGAALDKYA KKSVKVIVVG NPANTNCLTA SKSAPSIPKE
160 170 180 190 200
NFSCLTRLDH NRAKAQIALK LGVTSDDVKN VIIWGNHSST QYPDVNHAKV
210 220 230 240 250
KLQAKEVGVY EAVKDDSWLK GEFITTVQQR GAAVIKARKL SSAMSAAKAI
260 270 280 290 300
CDHVRDIWFG TPEGEFVSMG IISDGNSYGV PDDLLYSFPV TIKDKTWKIV
310 320 330
EGLPINDFSR EKMDLTAKEL AEEKETAFEF LSSA
Length:334
Mass (Da):36,454
Last modified:January 23, 2007 - v4
Checksum:i2574A8F3C2DD2C84
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti238 – 2381R → Q in AAA31072 (PubMed:3312200).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U44846 mRNA. Translation: AAC48610.1.
M29463 mRNA. Translation: AAA31072.1.
PIRiJC4876. A32472.
RefSeqiNP_999039.1. NM_213874.1.
UniGeneiSsc.11103.

Genome annotation databases

GeneIDi396894.
KEGGissc:396894.

Cross-referencesi

Web resourcesi

Worthington enzyme manual

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U44846 mRNA. Translation: AAC48610.1.
M29463 mRNA. Translation: AAA31072.1.
PIRiJC4876. A32472.
RefSeqiNP_999039.1. NM_213874.1.
UniGeneiSsc.11103.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4MDHX-ray2.50A/B2-334[»]
5MDHX-ray2.40A/B2-334[»]
ProteinModelPortaliP11708.
SMRiP11708. Positions 2-334.
ModBaseiSearch...
MobiDBiSearch...

Chemistry

BindingDBiP11708.
ChEMBLiCHEMBL4048.

Proteomic databases

PRIDEiP11708.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi396894.
KEGGissc:396894.

Organism-specific databases

CTDi4190.

Phylogenomic databases

HOVERGENiHBG006340.
InParanoidiP11708.
KOiK00025.

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-13033.
SABIO-RKP11708.

Miscellaneous databases

EvolutionaryTraceiP11708.

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

  1. "Cloning, sequencing and functional expression of a DNA encoding pig cytosolic malate dehydrogenase: purification and characterization of the recombinant enzyme."
    Trejo F., Costa M., Gelpi J.L., Busquets M., Clarke A.R., Holbrook J.J., Cortes A.
    Gene 172:303-308(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Heart.
  2. "Cloning and sequence analysis of cDNAs encoding mammalian cytosolic malate dehydrogenase. Comparison of the amino acid sequences of mammalian and bacterial malate dehydrogenase."
    Joh T., Takeshima H., Tsuzuki T., Setoyama C., Shimada K., Tanase S., Kuramitsu S., Kagamiyama H., Morino Y.
    J. Biol. Chem. 262:15127-15131(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 46-334.
  3. "Structure of porcine heart cytoplasmic malate dehydrogenase: combining X-ray diffraction and chemical sequence data in structural studies."
    Birktoft J.J., Bradshaw R.A., Banaszak L.J.
    Biochemistry 26:2722-2734(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS), PARTIAL PROTEIN SEQUENCE.
  4. "Refined crystal structure of cytoplasmic malate dehydrogenase at 2.5-A resolution."
    Birktoft J.J., Rhodes G., Banaszak L.J.
    Biochemistry 28:6065-6081(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).
  5. "Structural basis of substrate specificity in malate dehydrogenases: crystal structure of a ternary complex of porcine cytoplasmic malate dehydrogenase, alpha-ketomalonate and tetrahydoNAD."
    Chapman A.D., Cortes A., Dafforn T.R., Clarke A.R., Brady R.L.
    J. Mol. Biol. 285:703-712(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) IN COMPLEX WITH NAD AND SUBSTRATE ANALOG, SUBUNIT.

Entry informationi

Entry nameiMDHC_PIG
AccessioniPrimary (citable) accession number: P11708
Secondary accession number(s): Q29560
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1989
Last sequence update: January 23, 2007
Last modified: March 4, 2015
This is version 134 of the entry and version 4 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

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.