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Protein

Dihydrolipoyl dehydrogenase, mitochondrial

Gene

Dld

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Lipoamide dehydrogenase is a component of the glycine cleavage system as well as of the alpha-ketoacid dehydrogenase complexes. Involved in the hyperactivation of spermatazoa during capacitation and in the spermatazoal acrosome reaction.

Catalytic activityi

Protein N(6)-(dihydrolipoyl)lysine + NAD+ = protein N(6)-(lipoyl)lysine + NADH.

Cofactori

FADBy similarityNote: Binds 1 FAD per subunit.By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei89FADBy similarity1
Binding sitei154FAD; via amide nitrogen and carbonyl oxygenBy similarity1
Binding sitei243NADBy similarity1
Binding sitei278NAD; via amide nitrogen and carbonyl oxygenBy similarity1
Binding sitei314NAD; via amide nitrogenBy similarity1
Binding sitei355FADBy similarity1
Active sitei487Proton acceptorBy similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi71 – 80FADBy similarity10
Nucleotide bindingi183 – 185FADBy similarity3
Nucleotide bindingi220 – 227NADBy similarity8
Nucleotide bindingi361 – 364FADBy similarity4

GO - Molecular functioni

GO - Biological processi

  • 2-oxoglutarate metabolic process Source: Ensembl
  • aging Source: Ensembl
  • cell redox homeostasis Source: InterPro
  • dihydrolipoamide metabolic process Source: Ensembl
  • gastrulation Source: MGI
  • lipoate metabolic process Source: Ensembl
  • mitochondrial acetyl-CoA biosynthetic process from pyruvate Source: MGI
  • mitochondrial electron transport, NADH to ubiquinone Source: MGI
  • proteolysis Source: MGI
  • regulation of membrane potential Source: MGI
  • sperm capacitation Source: MGI
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

FAD, Flavoprotein, NAD

Enzyme and pathway databases

ReactomeiR-MMU-204174. Regulation of pyruvate dehydrogenase (PDH) complex.
R-MMU-389661. Glyoxylate metabolism and glycine degradation.
R-MMU-5362517. Signaling by Retinoic Acid.
R-MMU-6783984. Glycine degradation.
R-MMU-70268. Pyruvate metabolism.
R-MMU-70895. Branched-chain amino acid catabolism.
R-MMU-71064. Lysine catabolism.
R-MMU-71403. Citric acid cycle (TCA cycle).

Names & Taxonomyi

Protein namesi
Recommended name:
Dihydrolipoyl dehydrogenase, mitochondrial (EC:1.8.1.4)
Alternative name(s):
Dihydrolipoamide dehydrogenase
Gene namesi
Name:Dld
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 12

Organism-specific databases

MGIiMGI:107450. Dld.

Subcellular locationi

GO - Cellular componenti

  • acrosomal matrix Source: MGI
  • cilium Source: MGI
  • mitochondrial matrix Source: UniProtKB-SubCell
  • mitochondrion Source: MGI
  • myelin sheath Source: UniProtKB
  • nucleoplasm Source: MGI
  • oxoglutarate dehydrogenase complex Source: Ensembl
  • pyruvate dehydrogenase complex Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

Pathology & Biotechi

Chemistry databases

ChEMBLiCHEMBL2176826.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Transit peptidei1 – 35MitochondrionBy similarityAdd BLAST35
ChainiPRO_000003029736 – 509Dihydrolipoyl dehydrogenase, mitochondrialAdd BLAST474

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei66N6-acetyllysine; alternateCombined sources1
Modified residuei66N6-succinyllysine; alternateCombined sources1
Disulfide bondi80 ↔ 85Redox-activeBy similarity
Modified residuei104N6-acetyllysine; alternateCombined sources1
Modified residuei104N6-succinyllysine; alternateCombined sources1
Modified residuei122N6-acetyllysine; alternateCombined sources1
Modified residuei122N6-succinyllysine; alternateCombined sources1
Modified residuei132N6-acetyllysine; alternateCombined sources1
Modified residuei132N6-succinyllysine; alternateCombined sources1
Modified residuei143N6-acetyllysine; alternateCombined sources1
Modified residuei143N6-succinyllysine; alternateCombined sources1
Modified residuei159N6-succinyllysineCombined sources1
Modified residuei166N6-succinyllysineCombined sources1
Modified residuei273N6-succinyllysineCombined sources1
Modified residuei277N6-succinyllysineCombined sources1
Modified residuei285PhosphoserineCombined sources1
Modified residuei297PhosphoserineBy similarity1
Modified residuei334N6-acetyllysine; alternateCombined sources1
Modified residuei334N6-succinyllysine; alternateCombined sources1
Modified residuei346N6-acetyllysineCombined sources1
Modified residuei410N6-acetyllysine; alternateCombined sources1
Modified residuei410N6-succinyllysine; alternateCombined sources1
Modified residuei417N6-acetyllysineBy similarity1
Modified residuei420N6-acetyllysineCombined sources1
Modified residuei430N6-succinyllysineCombined sources1
Modified residuei505N6-acetyllysine; alternateCombined sources1
Modified residuei505N6-succinyllysine; alternateCombined sources1

Post-translational modificationi

Acetylation of Lys-127 is observed in liver mitochondria from fasted mice but not from fed mice.
Tyrosine phosphorylated.By similarity

Keywords - PTMi

Acetylation, Disulfide bond, Phosphoprotein

Proteomic databases

EPDiO08749.
MaxQBiO08749.
PaxDbiO08749.
PeptideAtlasiO08749.
PRIDEiO08749.

2D gel databases

REPRODUCTION-2DPAGEO08749.
SWISS-2DPAGEO08749.

PTM databases

iPTMnetiO08749.
PhosphoSitePlusiO08749.
SwissPalmiO08749.

Expressioni

Gene expression databases

BgeeiENSMUSG00000020664.
CleanExiMM_DLD.
GenevisibleiO08749. MM.

Interactioni

Subunit structurei

Homodimer. Eukaryotic pyruvate dehydrogenase complexes are organized about a core consisting of the oligomeric dihydrolipoamide acetyl-transferase, around which are arranged multiple copies of pyruvate dehydrogenase, dihydrolipoamide dehydrogenase and protein X bound by non-covalent bonds (By similarity).By similarity

Protein-protein interaction databases

BioGridi199227. 4 interactors.
IntActiO08749. 10 interactors.
MINTiMINT-4124146.
STRINGi10090.ENSMUSP00000106481.

Structurei

3D structure databases

ProteinModelPortaliO08749.
SMRiO08749.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Redox-active center, Transit peptide

Phylogenomic databases

eggNOGiKOG1335. Eukaryota.
COG1249. LUCA.
GeneTreeiENSGT00550000074844.
HOGENOMiHOG000276708.
HOVERGENiHBG002290.
InParanoidiO08749.
KOiK00382.
OMAiVYTQPEI.
OrthoDBiEOG091G05AA.
PhylomeDBiO08749.
TreeFamiTF300414.

Family and domain databases

Gene3Di3.30.390.30. 1 hit.
3.50.50.60. 2 hits.
InterProiIPR023753. FAD/NAD-binding_dom.
IPR016156. FAD/NAD-linked_Rdtase_dimer.
IPR006258. Lipoamide_DH.
IPR004099. Pyr_nucl-diS_OxRdtase_dimer.
IPR012999. Pyr_OxRdtase_I_AS.
[Graphical view]
PfamiPF07992. Pyr_redox_2. 1 hit.
PF02852. Pyr_redox_dim. 1 hit.
[Graphical view]
SUPFAMiSSF51905. SSF51905. 1 hit.
SSF55424. SSF55424. 1 hit.
TIGRFAMsiTIGR01350. lipoamide_DH. 1 hit.
PROSITEiPS00076. PYRIDINE_REDOX_1. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

O08749-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MQSWSRVYRS LAKKGHFNRI SHGLQGVSSV PLRTYADQPI EADVTVIGSG
60 70 80 90 100
PGGYVAAIKS AQLGFKTVCI EKNETLGGTC LNVGCIPSKA LLNNSHYYHM
110 120 130 140 150
AHGKDFASRG IEIPEVRLNL EKMMEQKHSA VKALTGGIAH LFKQNKVVHV
160 170 180 190 200
NGFGKITGKN QVTATKADGS TQVIDTKNIL VATGSEVTPF PGITIDEDTI
210 220 230 240 250
VSSTGALSLK KVPEKLVVIG AGVIGVELGS VWQRLGADVT AVEFLGHVGG
260 270 280 290 300
IGIDMEISKN FQRILQRQGF KFKLNTKVTG ATKKSDGKID VSVEAASGGK
310 320 330 340 350
AEVITCDVLL VCIGRRPFTQ NLGLEELGIE LDPKGRIPVN NRFQTKIPNI
360 370 380 390 400
YAIGDVVAGP MLAHKAEDEG IICVEGMAGG AVHIDYNCVP SVIYTHPEVA
410 420 430 440 450
WVGKSEEQLK EEGIEFKIGK FPFAANSRAK TNADTDGMVK ILGHKSTDRV
460 470 480 490 500
LGAHILGPGA GEMVNEAALA LEYGASCEDI ARVCHAHPTL SEAFREANLA

AAFGKPINF
Length:509
Mass (Da):54,272
Last modified:November 28, 2006 - v2
Checksum:i2C381852BAAD0441
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti54Y → C in AAC53170 (PubMed:9169128).Curated1
Sequence conflicti144Q → T in BAE22867 (PubMed:16141072).Curated1
Sequence conflicti149H → L in BAE31961 (PubMed:16141072).Curated1
Sequence conflicti283K → E in BAE40693 (PubMed:16141072).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U73445 mRNA. Translation: AAC53170.1.
AK117104 mRNA. Translation: BAE43405.1.
AK136193 mRNA. Translation: BAE22867.1.
AK153399 mRNA. Translation: BAE31961.1.
AK168875 mRNA. Translation: BAE40693.1.
BC003368 mRNA. Translation: AAH03368.1.
CCDSiCCDS36428.1.
RefSeqiNP_031887.2. NM_007861.5.
UniGeneiMm.3131.
Mm.471230.

Genome annotation databases

EnsembliENSMUST00000110857; ENSMUSP00000106481; ENSMUSG00000020664.
GeneIDi13382.
KEGGimmu:13382.
UCSCiuc007nhg.3. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U73445 mRNA. Translation: AAC53170.1.
AK117104 mRNA. Translation: BAE43405.1.
AK136193 mRNA. Translation: BAE22867.1.
AK153399 mRNA. Translation: BAE31961.1.
AK168875 mRNA. Translation: BAE40693.1.
BC003368 mRNA. Translation: AAH03368.1.
CCDSiCCDS36428.1.
RefSeqiNP_031887.2. NM_007861.5.
UniGeneiMm.3131.
Mm.471230.

3D structure databases

ProteinModelPortaliO08749.
SMRiO08749.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi199227. 4 interactors.
IntActiO08749. 10 interactors.
MINTiMINT-4124146.
STRINGi10090.ENSMUSP00000106481.

Chemistry databases

ChEMBLiCHEMBL2176826.

PTM databases

iPTMnetiO08749.
PhosphoSitePlusiO08749.
SwissPalmiO08749.

2D gel databases

REPRODUCTION-2DPAGEO08749.
SWISS-2DPAGEO08749.

Proteomic databases

EPDiO08749.
MaxQBiO08749.
PaxDbiO08749.
PeptideAtlasiO08749.
PRIDEiO08749.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000110857; ENSMUSP00000106481; ENSMUSG00000020664.
GeneIDi13382.
KEGGimmu:13382.
UCSCiuc007nhg.3. mouse.

Organism-specific databases

CTDi1738.
MGIiMGI:107450. Dld.

Phylogenomic databases

eggNOGiKOG1335. Eukaryota.
COG1249. LUCA.
GeneTreeiENSGT00550000074844.
HOGENOMiHOG000276708.
HOVERGENiHBG002290.
InParanoidiO08749.
KOiK00382.
OMAiVYTQPEI.
OrthoDBiEOG091G05AA.
PhylomeDBiO08749.
TreeFamiTF300414.

Enzyme and pathway databases

ReactomeiR-MMU-204174. Regulation of pyruvate dehydrogenase (PDH) complex.
R-MMU-389661. Glyoxylate metabolism and glycine degradation.
R-MMU-5362517. Signaling by Retinoic Acid.
R-MMU-6783984. Glycine degradation.
R-MMU-70268. Pyruvate metabolism.
R-MMU-70895. Branched-chain amino acid catabolism.
R-MMU-71064. Lysine catabolism.
R-MMU-71403. Citric acid cycle (TCA cycle).

Miscellaneous databases

PROiO08749.
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000020664.
CleanExiMM_DLD.
GenevisibleiO08749. MM.

Family and domain databases

Gene3Di3.30.390.30. 1 hit.
3.50.50.60. 2 hits.
InterProiIPR023753. FAD/NAD-binding_dom.
IPR016156. FAD/NAD-linked_Rdtase_dimer.
IPR006258. Lipoamide_DH.
IPR004099. Pyr_nucl-diS_OxRdtase_dimer.
IPR012999. Pyr_OxRdtase_I_AS.
[Graphical view]
PfamiPF07992. Pyr_redox_2. 1 hit.
PF02852. Pyr_redox_dim. 1 hit.
[Graphical view]
SUPFAMiSSF51905. SSF51905. 1 hit.
SSF55424. SSF55424. 1 hit.
TIGRFAMsiTIGR01350. lipoamide_DH. 1 hit.
PROSITEiPS00076. PYRIDINE_REDOX_1. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiDLDH_MOUSE
AccessioniPrimary (citable) accession number: O08749
Secondary accession number(s): Q3TG55
, Q3U5W5, Q3UWP7, Q99LD3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 15, 1999
Last sequence update: November 28, 2006
Last modified: November 2, 2016
This is version 151 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Miscellaneous

The active site is a redox-active disulfide bond.

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  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.