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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 of the alpha-ketoacid dehydrogenase complexes. Involved in the hyperactivation of spermatazoa during capacitation and in the spermatazoal acrosome reaction (By similarity).By similarity

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)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei89 – 891FADBy similarity
Binding sitei154 – 1541FAD; via amide nitrogen and carbonyl oxygenBy similarity
Binding sitei243 – 2431NADBy similarity
Binding sitei278 – 2781NAD; via amide nitrogen and carbonyl oxygenBy similarity
Binding sitei314 – 3141NAD; via amide nitrogenBy similarity
Binding sitei355 – 3551FADBy similarity
Active sitei487 – 4871Proton acceptorBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi71 – 8010FADBy similarity
Nucleotide bindingi183 – 1853FADBy similarity
Nucleotide bindingi220 – 2278NADBy similarity
Nucleotide bindingi361 – 3644FADBy similarity

GO - Molecular functioni

  • dihydrolipoyl dehydrogenase activity Source: RGD
  • flavin adenine dinucleotide binding Source: RGD
  • lipoamide binding Source: RGD
  • NAD binding Source: RGD

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
  • lipoate metabolic process Source: RGD
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

FAD, Flavoprotein, NAD

Enzyme and pathway databases

ReactomeiREACT_275973. Pyruvate metabolism.
REACT_296860. Branched-chain amino acid catabolism.
REACT_312589. Signaling by Retinoic Acid.
REACT_321551. Regulation of pyruvate dehydrogenase (PDH) complex.
REACT_338796. Citric acid cycle (TCA cycle).
REACT_346799. Lysine catabolism.
SABIO-RKQ6P6R2.

Names & Taxonomyi

Protein namesi
Recommended name:
Dihydrolipoyl dehydrogenase, mitochondrial (EC:1.8.1.4)
Alternative name(s):
Dihydrolipoamide dehydrogenase
Gene namesi
Name:Dld
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
ProteomesiUP000002494 Componenti: Chromosome 6

Organism-specific databases

RGDi735073. Dld.

Subcellular locationi

GO - Cellular componenti

  • mitochondrial matrix Source: UniProtKB-SubCell
  • mitochondrion Source: RGD
  • oxoglutarate dehydrogenase complex Source: RGD
  • pyruvate dehydrogenase complex Source: RGD
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 3535MitochondrionBy similarityAdd
BLAST
Chaini36 – 509474Dihydrolipoyl dehydrogenase, mitochondrialPRO_0000260228Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei66 – 661N6-acetyllysine; alternateBy similarity
Modified residuei66 – 661N6-succinyllysine; alternateBy similarity
Disulfide bondi80 ↔ 85Redox-activeBy similarity
Modified residuei104 – 1041N6-acetyllysine; alternateBy similarity
Modified residuei104 – 1041N6-succinyllysine; alternateBy similarity
Modified residuei122 – 1221N6-acetyllysine; alternateBy similarity
Modified residuei122 – 1221N6-succinyllysine; alternateBy similarity
Modified residuei132 – 1321N6-acetyllysine; alternateBy similarity
Modified residuei132 – 1321N6-succinyllysine; alternateBy similarity
Modified residuei143 – 1431N6-acetyllysine; alternateBy similarity
Modified residuei143 – 1431N6-succinyllysine; alternateBy similarity
Modified residuei159 – 1591N6-succinyllysineBy similarity
Modified residuei273 – 2731N6-succinyllysineBy similarity
Modified residuei277 – 2771N6-succinyllysineBy similarity
Modified residuei346 – 3461N6-acetyllysineBy similarity
Modified residuei410 – 4101N6-acetyllysine; alternateBy similarity
Modified residuei410 – 4101N6-succinyllysine; alternateBy similarity
Modified residuei417 – 4171N6-acetyllysineBy similarity
Modified residuei420 – 4201N6-acetyllysineBy similarity
Modified residuei430 – 4301N6-succinyllysineBy similarity
Modified residuei505 – 5051N6-acetyllysine; alternateBy similarity
Modified residuei505 – 5051N6-succinyllysine; alternateBy similarity

Post-translational modificationi

Tyrosine phosphorylated.By similarity

Keywords - PTMi

Acetylation, Disulfide bond, Phosphoprotein

Proteomic databases

PaxDbiQ6P6R2.
PRIDEiQ6P6R2.

PTM databases

PhosphoSiteiQ6P6R2.

Expressioni

Gene expression databases

GenevisibleiQ6P6R2. RN.

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

IntActiQ6P6R2. 1 interaction.
MINTiMINT-1775384.
STRINGi10116.ENSRNOP00000008980.

Structurei

3D structure databases

ProteinModelPortaliQ6P6R2.
SMRiQ6P6R2. Positions 37-509.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Redox-active center, Transit peptide

Phylogenomic databases

eggNOGiCOG1249.
GeneTreeiENSGT00550000074844.
HOGENOMiHOG000276708.
HOVERGENiHBG002290.
InParanoidiQ6P6R2.
KOiK00382.
OMAiHDDPRVW.
OrthoDBiEOG77126S.
PhylomeDBiQ6P6R2.
TreeFamiTF300414.

Family and domain databases

Gene3Di3.30.390.30. 1 hit.
InterProiIPR016156. FAD/NAD-linked_Rdtase_dimer.
IPR006258. Lipoamide_DH.
IPR004099. Pyr_nucl-diS_OxRdtase_dimer.
IPR023753. Pyr_nucl-diS_OxRdtase_FAD/NAD.
IPR012999. Pyr_OxRdtase_I_AS.
IPR001327. Pyr_OxRdtase_NAD-bd_dom.
[Graphical view]
PfamiPF00070. Pyr_redox. 1 hit.
PF07992. Pyr_redox_2. 1 hit.
PF02852. Pyr_redox_dim. 1 hit.
[Graphical view]
SUPFAMiSSF55424. 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.

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.

Cross-referencesi

Sequence databases

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

3D structure databases

ProteinModelPortaliQ6P6R2.
SMRiQ6P6R2. Positions 37-509.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ6P6R2. 1 interaction.
MINTiMINT-1775384.
STRINGi10116.ENSRNOP00000008980.

PTM databases

PhosphoSiteiQ6P6R2.

Proteomic databases

PaxDbiQ6P6R2.
PRIDEiQ6P6R2.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi1738.
RGDi735073. Dld.

Phylogenomic databases

eggNOGiCOG1249.
GeneTreeiENSGT00550000074844.
HOGENOMiHOG000276708.
HOVERGENiHBG002290.
InParanoidiQ6P6R2.
KOiK00382.
OMAiHDDPRVW.
OrthoDBiEOG77126S.
PhylomeDBiQ6P6R2.
TreeFamiTF300414.

Enzyme and pathway databases

ReactomeiREACT_275973. Pyruvate metabolism.
REACT_296860. Branched-chain amino acid catabolism.
REACT_312589. Signaling by Retinoic Acid.
REACT_321551. Regulation of pyruvate dehydrogenase (PDH) complex.
REACT_338796. Citric acid cycle (TCA cycle).
REACT_346799. Lysine catabolism.
SABIO-RKQ6P6R2.

Miscellaneous databases

NextBioi644542.
PROiQ6P6R2.

Gene expression databases

GenevisibleiQ6P6R2. RN.

Family and domain databases

Gene3Di3.30.390.30. 1 hit.
InterProiIPR016156. FAD/NAD-linked_Rdtase_dimer.
IPR006258. Lipoamide_DH.
IPR004099. Pyr_nucl-diS_OxRdtase_dimer.
IPR023753. Pyr_nucl-diS_OxRdtase_FAD/NAD.
IPR012999. Pyr_OxRdtase_I_AS.
IPR001327. Pyr_OxRdtase_NAD-bd_dom.
[Graphical view]
PfamiPF00070. Pyr_redox. 1 hit.
PF07992. Pyr_redox_2. 1 hit.
PF02852. Pyr_redox_dim. 1 hit.
[Graphical view]
SUPFAMiSSF55424. SSF55424. 1 hit.
TIGRFAMsiTIGR01350. lipoamide_DH. 1 hit.
PROSITEiPS00076. PYRIDINE_REDOX_1. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "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: Prostate.
  2. Lubec G., Afjehi-Sadat L., Kang S.U.
    Submitted (JUL-2007) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 90-104; 289-334; 431-440 AND 483-495, IDENTIFICATION BY MASS SPECTROMETRY.
    Strain: Sprague-Dawley.
    Tissue: Brain and Spinal cord.

Entry informationi

Entry nameiDLDH_RAT
AccessioniPrimary (citable) accession number: Q6P6R2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 28, 2006
Last sequence update: July 5, 2004
Last modified: June 24, 2015
This is version 98 of the entry and version 1 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. 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.