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Q6P6R2 (DLDH_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 88. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Dihydrolipoyl dehydrogenase, mitochondrial

EC=1.8.1.4
Alternative name(s):
Dihydrolipoamide dehydrogenase
Gene names
Name:Dld
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Protein attributes

Sequence length509 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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.

Catalytic activity

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

Cofactor

Binds 1 FAD per subunit By similarity.

Subunit structure

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.

Subcellular location

Mitochondrion matrix By similarity.

Post-translational modification

Tyrosine phosphorylated By similarity.

Miscellaneous

The active site is a redox-active disulfide bond.

Sequence similarities

Belongs to the class-I pyridine nucleotide-disulfide oxidoreductase family.

Ontologies

Keywords
   Cellular componentMitochondrion
   DomainRedox-active center
Transit peptide
   LigandFAD
Flavoprotein
NAD
   Molecular functionOxidoreductase
   PTMAcetylation
Disulfide bond
Phosphoprotein
   Technical termComplete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_process2-oxoglutarate metabolic process

Inferred from direct assay PubMed 3571202. Source: RGD

acetyl-CoA biosynthetic process from pyruvate

Inferred from direct assay PubMed 7487891. Source: RGD

aging

Inferred from expression pattern PubMed 18316113. Source: RGD

cell redox homeostasis

Inferred from electronic annotation. Source: InterPro

dihydrolipoamide metabolic process

Inferred from direct assay PubMed 8981046. Source: RGD

lipoate metabolic process

Inferred from direct assay PubMed 8981046. Source: RGD

   Cellular_componentmitochondrial matrix

Inferred from electronic annotation. Source: UniProtKB-SubCell

mitochondrion

Inferred from direct assay PubMed 3571202PubMed 3753688PubMed 7487891PubMed 8981046. Source: RGD

oxoglutarate dehydrogenase complex

Inferred from direct assay PubMed 3571202. Source: RGD

pyruvate dehydrogenase complex

Inferred from direct assay PubMed 7487891. Source: RGD

   Molecular_functionNAD binding

Inferred from direct assay PubMed 3753688. Source: RGD

dihydrolipoyl dehydrogenase activity

Inferred from direct assay PubMed 7487891PubMed 8981046. Source: RGD

flavin adenine dinucleotide binding

Inferred from direct assay PubMed 3753688. Source: RGD

lipoamide binding

Inferred from direct assay PubMed 8981046. Source: RGD

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 3535Mitochondrion By similarity
Chain36 – 509474Dihydrolipoyl dehydrogenase, mitochondrial
PRO_0000260228

Regions

Nucleotide binding71 – 8010FAD By similarity
Nucleotide binding183 – 1853FAD By similarity
Nucleotide binding220 – 2278NAD By similarity
Nucleotide binding361 – 3644FAD By similarity

Sites

Active site4871Proton acceptor By similarity
Binding site891FAD By similarity
Binding site1541FAD; via amide nitrogen and carbonyl oxygen By similarity
Binding site2431NAD By similarity
Binding site2781NAD; via amide nitrogen and carbonyl oxygen By similarity
Binding site3141NAD; via amide nitrogen By similarity
Binding site3551FAD By similarity

Amino acid modifications

Modified residue661N6-acetyllysine; alternate By similarity
Modified residue661N6-succinyllysine; alternate By similarity
Modified residue1041N6-acetyllysine; alternate By similarity
Modified residue1041N6-succinyllysine; alternate By similarity
Modified residue1221N6-acetyllysine; alternate By similarity
Modified residue1221N6-succinyllysine; alternate By similarity
Modified residue1321N6-acetyllysine; alternate By similarity
Modified residue1321N6-succinyllysine; alternate By similarity
Modified residue1431N6-acetyllysine; alternate By similarity
Modified residue1431N6-succinyllysine; alternate By similarity
Modified residue1591N6-succinyllysine By similarity
Modified residue2731N6-succinyllysine By similarity
Modified residue2771N6-succinyllysine By similarity
Modified residue3461N6-acetyllysine By similarity
Modified residue4101N6-acetyllysine; alternate By similarity
Modified residue4101N6-succinyllysine; alternate By similarity
Modified residue4171N6-acetyllysine By similarity
Modified residue4201N6-acetyllysine By similarity
Modified residue4301N6-succinyllysine By similarity
Modified residue5051N6-acetyllysine; alternate By similarity
Modified residue5051N6-succinyllysine; alternate By similarity
Disulfide bond80 ↔ 85Redox-active By similarity

Sequences

Sequence LengthMass (Da)Tools
Q6P6R2 [UniParc].

Last modified July 5, 2004. Version 1.
Checksum: 854802DBFE36573A

FASTA50954,038
        10         20         30         40         50         60 
MQSWSRVYCS LAKKGHFNRL SHGLQGASSV PLRTYSDQPI DADVTVIGSG PGGYVAAIKA 

        70         80         90        100        110        120 
AQLGFKTVCI EKNETLGGTC LNVGCIPSKA LLNNSHYYHL AHGKDFASRG IEIPEVRLNL 

       130        140        150        160        170        180 
EKMMEQKRSA VKALTGGIAH LFKQNKVVHV NGFGKITGKN QVTATTADGS TQVIGTKNIL 

       190        200        210        220        230        240 
IATGSEVTPF PGITIDEDTI VSSTGALSLK KVPEKLVVIG AGVIGVELGS VWQRLGADVT 

       250        260        270        280        290        300 
AVEFLGHVGG IGIDMEISKN FQRILQKQGF KFKLNTKVTG ATKKSDGKID VSVEAASGGK 

       310        320        330        340        350        360 
AEVITCDVLL VCIGRRPFTQ NLGLEELGIE LDPKGRIPVN TRFQTKIPNI FAIGDVVAGP 

       370        380        390        400        410        420 
MLAHKAEDEG IICVEGMAGG AVHIDYNCVP SVIYTHPEVA WVGKSEEQLK EEGVEFKVGK 

       430        440        450        460        470        480 
FPFAANSRAK TNADTDGMVK ILGHKSTDRI LGAHILGPGA GEMVNEAALA LEYGASCEDV 

       490        500 
ARVCHAHPTL SEAFREANLA ASFGKPINF 

« Hide

References

« Hide 'large scale' references
[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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BC062069 mRNA. Translation: AAH62069.1.
RefSeqNP_955417.1. NM_199385.2.
UniGeneRn.86962.

3D structure databases

ProteinModelPortalQ6P6R2.
SMRQ6P6R2. Positions 37-509.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActQ6P6R2. 1 interaction.
MINTMINT-1775384.
STRING10116.ENSRNOP00000008980.

PTM databases

PhosphoSiteQ6P6R2.

Proteomic databases

PaxDbQ6P6R2.
PRIDEQ6P6R2.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSRNOT00000008980; ENSRNOP00000008980; ENSRNOG00000006364.
GeneID298942.
KEGGrno:298942.
UCSCRGD:735073. rat.

Organism-specific databases

CTD1738.
RGD735073. Dld.

Phylogenomic databases

eggNOGCOG1249.
GeneTreeENSGT00550000074844.
HOGENOMHOG000276708.
HOVERGENHBG002290.
KOK00382.
OMARMERGFV.
OrthoDBEOG77126S.
PhylomeDBQ6P6R2.
TreeFamTF300414.

Enzyme and pathway databases

SABIO-RKQ6P6R2.

Gene expression databases

GenevestigatorQ6P6R2.

Family and domain databases

Gene3D3.30.390.30. 1 hit.
InterProIPR016156. 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]
PfamPF00070. Pyr_redox. 1 hit.
PF07992. Pyr_redox_2. 1 hit.
PF02852. Pyr_redox_dim. 1 hit.
[Graphical view]
PRINTSPR00368. FADPNR.
SUPFAMSSF55424. SSF55424. 1 hit.
TIGRFAMsTIGR01350. lipoamide_DH. 1 hit.
PROSITEPS00076. PYRIDINE_REDOX_1. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio644542.
PROQ6P6R2.

Entry information

Entry nameDLDH_RAT
AccessionPrimary (citable) accession number: Q6P6R2
Entry history
Integrated into UniProtKB/Swiss-Prot: November 28, 2006
Last sequence update: July 5, 2004
Last modified: May 14, 2014
This is version 88 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families