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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)DescriptionActionsGraphical viewLength
Binding sitei42NAD2 Publications1
Binding sitei92Substrate1 Publication1
Binding sitei98Substrate1 Publication1
Binding sitei105NAD1 Publication1
Binding sitei112NAD1 Publication1
Binding sitei131Substrate1 Publication1
Binding sitei162Substrate1 Publication1
Active sitei187Proton acceptor1 Publication1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi11 – 17NAD2 Publications7
Nucleotide bindingi129 – 131NAD2 Publications3

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

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
Proteomesi
  • UP000008227 Componenti: Unplaced

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: MGI
  • mitochondrion Source: GO_Central
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Chemistry databases

ChEMBLiCHEMBL4048.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemoved
ChainiPRO_00001134112 – 334Malate dehydrogenase, cytoplasmicAdd BLAST333

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylserine1 Publication1
Modified residuei110N6-succinyllysineBy similarity1
Modified residuei118N6-acetyllysineBy similarity1
Modified residuei121N6-acetyllysineBy similarity1
Modified residuei214N6-succinyllysineBy similarity1
Modified residuei217PhosphoserineBy similarity1
Modified residuei230Omega-N-methylarginineBy similarity1
Modified residuei241PhosphoserineBy similarity1
Modified residuei298N6-acetyllysine; alternateBy similarity1
Modified residuei298N6-succinyllysine; alternateBy similarity1
Modified residuei309PhosphoserineBy similarity1
Modified residuei318N6-succinyllysineBy similarity1
Modified residuei332PhosphoserineBy similarity1
Modified residuei333PhosphoserineBy similarity1

Post-translational modificationi

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

Keywords - PTMi

Acetylation, Methylation, Phosphoprotein, Ubl conjugation

Proteomic databases

PaxDbiP11708.
PeptideAtlasiP11708.
PRIDEiP11708.

Interactioni

Subunit structurei

Homodimer.1 Publication

Protein-protein interaction databases

STRINGi9823.ENSSSCP00000021561.

Chemistry databases

BindingDBiP11708.

Structurei

Secondary structure

1334
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi5 – 11Combined sources7
Helixi15 – 18Combined sources4
Helixi21 – 25Combined sources5
Turni26 – 30Combined sources5
Beta strandi36 – 41Combined sources6
Helixi44 – 46Combined sources3
Helixi47 – 59Combined sources13
Beta strandi65 – 72Combined sources8
Helixi74 – 77Combined sources4
Turni78 – 80Combined sources3
Beta strandi82 – 86Combined sources5
Turni98 – 101Combined sources4
Helixi102 – 119Combined sources18
Beta strandi125 – 128Combined sources4
Beta strandi130 – 132Combined sources3
Helixi133 – 142Combined sources10
Helixi149 – 151Combined sources3
Beta strandi152 – 154Combined sources3
Helixi157 – 171Combined sources15
Helixi175 – 177Combined sources3
Beta strandi182 – 185Combined sources4
Beta strandi192 – 194Combined sources3
Beta strandi199 – 201Combined sources3
Beta strandi206 – 208Combined sources3
Helixi209 – 213Combined sources5
Helixi216 – 220Combined sources5
Helixi222 – 238Combined sources17
Helixi244 – 259Combined sources16
Beta strandi267 – 272Combined sources6
Beta strandi277 – 279Combined sources3
Beta strandi285 – 293Combined sources9
Beta strandi296 – 299Combined sources4
Helixi307 – 333Combined sources27

3D structure databases

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

Miscellaneous databases

EvolutionaryTraceiP11708.

Family & Domainsi

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiKOG1496. Eukaryota.
COG0039. LUCA.
HOVERGENiHBG006340.
InParanoidiP11708.
KOiK00025.

Family and domain databases

CDDicd01336. MDH_cytoplasmic_cytosolic. 1 hit.
Gene3Di3.40.50.720. 1 hit.
3.90.110.10. 1 hit.
HAMAPiMF_01517. Malate_dehydrog_2. 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.
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.
SUPFAMiSSF51735. SSF51735. 1 hit.
SSF56327. 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)DescriptionActionsGraphical viewLength
Sequence conflicti238R → Q in AAA31072 (PubMed:3312200).Curated1

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.
XP_013851563.1. XM_013996109.1.
UniGeneiSsc.11103.

Genome annotation databases

GeneIDi102163346.
396894.
KEGGissc:102163346.
ssc: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.
XP_013851563.1. XM_013996109.1.
UniGeneiSsc.11103.

3D structure databases

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

Protein-protein interaction databases

STRINGi9823.ENSSSCP00000021561.

Chemistry databases

BindingDBiP11708.
ChEMBLiCHEMBL4048.

Proteomic databases

PaxDbiP11708.
PeptideAtlasiP11708.
PRIDEiP11708.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi102163346.
396894.
KEGGissc:102163346.
ssc:396894.

Organism-specific databases

CTDi4190.

Phylogenomic databases

eggNOGiKOG1496. Eukaryota.
COG0039. LUCA.
HOVERGENiHBG006340.
InParanoidiP11708.
KOiK00025.

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-13033.
SABIO-RKP11708.

Miscellaneous databases

EvolutionaryTraceiP11708.
PROiP11708.

Family and domain databases

CDDicd01336. MDH_cytoplasmic_cytosolic. 1 hit.
Gene3Di3.40.50.720. 1 hit.
3.90.110.10. 1 hit.
HAMAPiMF_01517. Malate_dehydrog_2. 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.
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.
SUPFAMiSSF51735. SSF51735. 1 hit.
SSF56327. SSF56327. 1 hit.
TIGRFAMsiTIGR01759. MalateDH-SF1. 1 hit.
TIGR01758. MDH_euk_cyt. 1 hit.
PROSITEiPS00068. MDH. 1 hit.
[Graphical view]
ProtoNetiSearch...

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: November 30, 2016
This is version 147 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

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.