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Q6P6R2

- DLDH_RAT

UniProt

Q6P6R2 - DLDH_RAT

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Protein

Dihydrolipoyl dehydrogenase, mitochondrial

Gene

Dld

Organism
Rattus norvegicus (Rat)
Status
Reviewed - 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

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

  1. dihydrolipoyl dehydrogenase activity Source: RGD
  2. flavin adenine dinucleotide binding Source: RGD
  3. lipoamide binding Source: RGD
  4. NAD binding Source: RGD

GO - Biological processi

  1. 2-oxoglutarate metabolic process Source: RGD
  2. acetyl-CoA biosynthetic process from pyruvate Source: RGD
  3. aging Source: RGD
  4. cell redox homeostasis Source: InterPro
  5. dihydrolipoamide metabolic process Source: RGD
  6. lipoate metabolic process Source: RGD
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

FAD, Flavoprotein, NAD

Enzyme and pathway databases

ReactomeiREACT_203088. Pyruvate metabolism.
REACT_216424. Citric acid cycle (TCA cycle).
REACT_220761. Lysine catabolism.
REACT_221218. Branched-chain amino acid 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: Chromosome 6

Organism-specific databases

RGDi735073. Dld.

Subcellular locationi

Mitochondrion matrix By similarity

GO - Cellular componenti

  1. mitochondrion Source: RGD
  2. oxoglutarate dehydrogenase complex Source: RGD
  3. 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

GenevestigatoriQ6P6R2.

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.
OMAiRMERGFV.
OrthoDBiEOG77126S.
PhylomeDBiQ6P6R2.
TreeFamiTF300414.

Family and domain databases

Gene3Di3.30.390.30. 1 hit.
InterProiIPR016156. FAD/NAD-linked_Rdtase_dimer.
IPR013027. FAD_pyr_nucl-diS_OxRdtase.
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]
PRINTSiPR00368. FADPNR.
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:
EMBL
GenBank
DDBJ
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:
EMBL
GenBank
DDBJ
Links Updated
BC062069 mRNA. Translation: AAH62069.1 .
RefSeqi NP_955417.1. NM_199385.2.
UniGenei Rn.86962.

3D structure databases

ProteinModelPortali Q6P6R2.
SMRi Q6P6R2. Positions 37-509.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

IntActi Q6P6R2. 1 interaction.
MINTi MINT-1775384.
STRINGi 10116.ENSRNOP00000008980.

PTM databases

PhosphoSitei Q6P6R2.

Proteomic databases

PaxDbi Q6P6R2.
PRIDEi Q6P6R2.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSRNOT00000008980 ; ENSRNOP00000008980 ; ENSRNOG00000006364 .
GeneIDi 298942.
KEGGi rno:298942.
UCSCi RGD:735073. rat.

Organism-specific databases

CTDi 1738.
RGDi 735073. Dld.

Phylogenomic databases

eggNOGi COG1249.
GeneTreei ENSGT00550000074844.
HOGENOMi HOG000276708.
HOVERGENi HBG002290.
InParanoidi Q6P6R2.
KOi K00382.
OMAi RMERGFV.
OrthoDBi EOG77126S.
PhylomeDBi Q6P6R2.
TreeFami TF300414.

Enzyme and pathway databases

Reactomei REACT_203088. Pyruvate metabolism.
REACT_216424. Citric acid cycle (TCA cycle).
REACT_220761. Lysine catabolism.
REACT_221218. Branched-chain amino acid catabolism.
SABIO-RK Q6P6R2.

Miscellaneous databases

NextBioi 644542.
PROi Q6P6R2.

Gene expression databases

Genevestigatori Q6P6R2.

Family and domain databases

Gene3Di 3.30.390.30. 1 hit.
InterProi IPR016156. FAD/NAD-linked_Rdtase_dimer.
IPR013027. FAD_pyr_nucl-diS_OxRdtase.
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 ]
Pfami PF00070. Pyr_redox. 1 hit.
PF07992. Pyr_redox_2. 1 hit.
PF02852. Pyr_redox_dim. 1 hit.
[Graphical view ]
PRINTSi PR00368. FADPNR.
SUPFAMi SSF55424. SSF55424. 1 hit.
TIGRFAMsi TIGR01350. lipoamide_DH. 1 hit.
PROSITEi PS00076. PYRIDINE_REDOX_1. 1 hit.
[Graphical view ]
ProtoNeti Search...

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: October 29, 2014
This is version 91 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