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Protein

Dihydrolipoyl dehydrogenase, mitochondrial

Gene

Dld

Organism
Rattus norvegicus (Rat)
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 an E3 component of the alpha-ketoacid dehydrogenase complexes (pyruvate-, alpha-ketoglutarate-, and branched-chain amino acid-dehydrogenase complex). In monomeric form has additional moonlighting function as serine protease (By similarity). Involved in the hyperactivation of spermatazoa during capacitation and in the spermatazoal acrosome reaction (By similarity).By similarity

Miscellaneous

The active site is a redox-active disulfide bond.

Catalytic activityi

Protein N6-(dihydrolipoyl)lysine + NAD+ = protein N6-(lipoyl)lysine + NADH.By similarity

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
Sitei448Important for interaction with PDHX and activity of pyruvate dehydrogenase complexBy similarity1
Sitei473Important for interaction with PDHX and activity of pyruvate dehydrogenase complexBy 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

  • dihydrolipoyl dehydrogenase activity Source: RGD
  • electron carrier activity Source: InterPro
  • flavin adenine dinucleotide binding Source: RGD
  • lipoamide binding Source: RGD
  • NAD binding Source: RGD
  • pyruvate dehydrogenase (NAD+) activity Source: Ensembl

GO - Biological processi

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

Keywordsi

Molecular functionOxidoreductase
LigandFAD, Flavoprotein, NAD

Enzyme and pathway databases

ReactomeiR-RNO-204174. Regulation of pyruvate dehydrogenase (PDH) complex.
R-RNO-389661. Glyoxylate metabolism and glycine degradation.
R-RNO-5362517. Signaling by Retinoic Acid.
R-RNO-6783984. Glycine degradation.
R-RNO-70268. Pyruvate metabolism.
R-RNO-70895. Branched-chain amino acid catabolism.
R-RNO-71064. Lysine catabolism.
R-RNO-71403. Citric acid cycle (TCA cycle).
SABIO-RKiQ6P6R2.

Names & Taxonomyi

Protein namesi
Recommended name:
Dihydrolipoyl dehydrogenase, mitochondrial (EC:1.8.1.4By similarity)
Alternative name(s):
Dihydrolipoamide dehydrogenase
Gene namesi
Name:Dld
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 6

Organism-specific databases

RGDi735073. Dld.

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Cell projection, Cilium, Cytoplasmic vesicle, Flagellum, Mitochondrion

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Transit peptidei1 – 35MitochondrionBy similarityAdd BLAST35
ChainiPRO_000026022836 – 509Dihydrolipoyl dehydrogenase, mitochondrialAdd BLAST474

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei66N6-acetyllysine; alternateBy similarity1
Modified residuei66N6-succinyllysine; alternateBy similarity1
Disulfide bondi80 ↔ 85Redox-activeBy similarity
Modified residuei104N6-acetyllysine; alternateBy similarity1
Modified residuei104N6-succinyllysine; alternateBy similarity1
Modified residuei122N6-acetyllysine; alternateBy similarity1
Modified residuei122N6-succinyllysine; alternateBy similarity1
Modified residuei132N6-acetyllysine; alternateBy similarity1
Modified residuei132N6-succinyllysine; alternateBy similarity1
Modified residuei143N6-acetyllysine; alternateBy similarity1
Modified residuei143N6-succinyllysine; alternateBy similarity1
Modified residuei159N6-succinyllysineBy similarity1
Modified residuei273N6-succinyllysineBy similarity1
Modified residuei277N6-succinyllysineBy similarity1
Modified residuei285PhosphoserineBy similarity1
Modified residuei297PhosphoserineCombined sources1
Modified residuei346N6-acetyllysineBy similarity1
Modified residuei410N6-acetyllysine; alternateBy similarity1
Modified residuei410N6-succinyllysine; alternateBy similarity1
Modified residuei417N6-acetyllysineBy similarity1
Modified residuei420N6-acetyllysineBy similarity1
Modified residuei430N6-succinyllysineBy similarity1
Modified residuei502PhosphoserineBy similarity1
Modified residuei505N6-acetyllysine; alternateBy similarity1
Modified residuei505N6-succinyllysine; alternateBy similarity1

Post-translational modificationi

Tyrosine phosphorylated.By similarity

Keywords - PTMi

Acetylation, Disulfide bond, Phosphoprotein

Proteomic databases

PaxDbiQ6P6R2.
PRIDEiQ6P6R2.

PTM databases

iPTMnetiQ6P6R2.
PhosphoSitePlusiQ6P6R2.

Expressioni

Gene expression databases

BgeeiENSRNOG00000006364.
GenevisibleiQ6P6R2. RN.

Interactioni

Subunit structurei

Homodimer. Part of the multimeric pyruvate dehydrogenase complex that contains multiple copies of pyruvate dehydrogenase (subunits PDH1A and PDHB, E1), dihydrolipoamide acetyltransferase (DLAT, E2) and lipoamide dehydrogenase (DLD, E3). These subunits are bound to an inner core composed of about 48 DLAT and 12 PDHX molecules (by non covalent bonds). Interacts with PDHX.By similarity

Protein-protein interaction databases

BioGridi256067. 1 interactor.
IntActiQ6P6R2. 1 interactor.
MINTiMINT-1775384.
STRINGi10116.ENSRNOP00000008980.

Structurei

3D structure databases

ProteinModelPortaliQ6P6R2.
SMRiQ6P6R2.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Redox-active center, Transit peptide

Phylogenomic databases

eggNOGiKOG1335. Eukaryota.
COG1249. LUCA.
GeneTreeiENSGT00550000074844.
HOGENOMiHOG000276708.
HOVERGENiHBG002290.
InParanoidiQ6P6R2.
KOiK00382.
OMAiTMSEAVM.
OrthoDBiEOG091G05AA.
PhylomeDBiQ6P6R2.
TreeFamiTF300414.

Family and domain databases

Gene3Di3.30.390.30. 1 hit.
3.50.50.60. 1 hit.
InterProiView protein in InterPro
IPR036188. FAD/NAD-bd_sf.
IPR023753. FAD/NAD-binding_dom.
IPR016156. FAD/NAD-linked_Rdtase_dimer_sf.
IPR006258. Lipoamide_DH.
IPR001100. Pyr_nuc-diS_OxRdtase.
IPR004099. Pyr_nucl-diS_OxRdtase_dimer.
IPR012999. Pyr_OxRdtase_I_AS.
PfamiView protein in Pfam
PF07992. Pyr_redox_2. 1 hit.
PF02852. Pyr_redox_dim. 1 hit.
PIRSFiPIRSF000350. Mercury_reductase_MerA. 1 hit.
SUPFAMiSSF51905. SSF51905. 1 hit.
SSF55424. SSF55424. 1 hit.
TIGRFAMsiTIGR01350. lipoamide_DH. 1 hit.
PROSITEiView protein in PROSITE
PS00076. PYRIDINE_REDOX_1. 1 hit.

Sequencei

Sequence statusi: Complete.

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

Q6P6R2-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MQSWSRVYCS LAKKGHFNRL SHGLQGASSV PLRTYSDQPI DADVTVIGSG
60 70 80 90 100
PGGYVAAIKA AQLGFKTVCI EKNETLGGTC LNVGCIPSKA LLNNSHYYHL
110 120 130 140 150
AHGKDFASRG IEIPEVRLNL EKMMEQKRSA VKALTGGIAH LFKQNKVVHV
160 170 180 190 200
NGFGKITGKN QVTATTADGS TQVIGTKNIL IATGSEVTPF PGITIDEDTI
210 220 230 240 250
VSSTGALSLK KVPEKLVVIG AGVIGVELGS VWQRLGADVT AVEFLGHVGG
260 270 280 290 300
IGIDMEISKN FQRILQKQGF KFKLNTKVTG ATKKSDGKID VSVEAASGGK
310 320 330 340 350
AEVITCDVLL VCIGRRPFTQ NLGLEELGIE LDPKGRIPVN TRFQTKIPNI
360 370 380 390 400
FAIGDVVAGP MLAHKAEDEG IICVEGMAGG AVHIDYNCVP SVIYTHPEVA
410 420 430 440 450
WVGKSEEQLK EEGVEFKVGK FPFAANSRAK TNADTDGMVK ILGHKSTDRI
460 470 480 490 500
LGAHILGPGA GEMVNEAALA LEYGASCEDV ARVCHAHPTL SEAFREANLA

ASFGKPINF
Length:509
Mass (Da):54,038
Last modified:July 5, 2004 - v1
Checksum:i854802DBFE36573A
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BC062069 mRNA. Translation: AAH62069.1.
RefSeqiNP_955417.1. NM_199385.2.
UniGeneiRn.86962.

Genome annotation databases

EnsembliENSRNOT00000008980; ENSRNOP00000008980; ENSRNOG00000006364.
GeneIDi298942.
KEGGirno:298942.
UCSCiRGD:735073. rat.

Similar proteinsi

Entry informationi

Entry nameiDLDH_RAT
AccessioniPrimary (citable) accession number: Q6P6R2
Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 28, 2006
Last sequence update: July 5, 2004
Last modified: November 22, 2017
This is version 119 of the entry and version 1 of the sequence. See 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