Dihydrolipoyl dehydrogenase, mitochondrial precursor

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Q6P6R2 (DLDH_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 78. History...

Clusters with 100%, 90%, 50% identity |

Documents (1) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Dihydrolipoyl dehydrogenase, mitochondrial
EC=1.8.1.4

Alternative name(s):
Dihydrolipoamide dehydrogenase

Gene names

Name:

Dld

Organism

Rattus norvegicus (Rat) [Reference proteome]

Taxonomic identifier

10116 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus

Protein attributes

Sequence length	509 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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 component	Mitochondrion
Domain	Redox-active center Transit peptide
Ligand	FAD Flavoprotein NAD
Molecular function	Oxidoreductase
PTM	Acetylation Disulfide bond Phosphoprotein
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	2-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_component	mitochondrial matrix Inferred from electronic annotation. Source: UniProtKB-SubCell mitochondrion Inferred from direct assay PubMed 3571202 PubMed 3753688 PubMed 7487891 PubMed 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_function	NAD binding Inferred from direct assay PubMed 3753688. Source: RGD dihydrolipoyl dehydrogenase activity Inferred from direct assay PubMed 7487891 PubMed 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 key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Transit peptide

1 – 35

Mitochondrion By similarity

Chain

36 – 509

474

Dihydrolipoyl dehydrogenase, mitochondrial

PRO_0000260228

Regions

Nucleotide binding

71 – 80

FAD By similarity

Nucleotide binding

183 – 185

FAD By similarity

Nucleotide binding

220 – 227

NAD By similarity

Nucleotide binding

361 – 364

FAD By similarity

Sites

Active site

487

Proton acceptor By similarity

Binding site

FAD By similarity

Binding site

154

FAD; via amide nitrogen and carbonyl oxygen By similarity

Binding site

243

NAD By similarity

Binding site

278

NAD; via amide nitrogen and carbonyl oxygen By similarity

Binding site

314

NAD; via amide nitrogen By similarity

Binding site

355

FAD By similarity

Amino acid modifications

Modified residue

127

N6-acetyllysine By similarity

Modified residue

143

N6-acetyllysine By similarity

Modified residue

410

N6-acetyllysine By similarity

Modified residue

417

N6-acetyllysine By similarity

Disulfide bond

80 ↔ 85

Redox-active By similarity

Sequences

Sequence

Length

Mass (Da)

Tools

Q6P6R2 [UniParc].

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

509

54,038

        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' referencesShow '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, 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.
IPI	IPI00365545.
RefSeq	NP_955417.1. NM_199385.1.
UniGene	Rn.86962.
3D structure databases
HSSP	HSSP built from PDB template 2F5Z based on UniProtKB P09622.
ProteinModelPortal	Q6P6R2.
SMR	Q6P6R2. Positions 37-509.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q6P6R2. 1 interaction.
MINT	MINT-1775384.
STRING	10116.ENSRNOP00000008980.
PTM databases
PhosphoSite	Q6P6R2.
Proteomic databases
PaxDb	Q6P6R2.
PRIDE	Q6P6R2.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSRNOT00000008980; ENSRNOP00000008980; ENSRNOG00000006364.
GeneID	298942.
KEGG	rno:298942.
UCSC	RGD:735073. rat.
Organism-specific databases
CTD	1738.
RGD	735073. Dld.
Phylogenomic databases
eggNOG	COG1249.
GeneTree	ENSGT00550000074844.
HOGENOM	HOG000276708.
HOVERGEN	HBG002290.
KO	K00382.
OrthoDB	EOG46Q6SC.
Enzyme and pathway databases
SABIO-RK	Q6P6R2.
Gene expression databases
ArrayExpress	Q6P6R2.
Genevestigator	Q6P6R2.
GermOnline	ENSRNOG00000006364. Rattus norvegicus.
Family and domain databases
Gene3D	3.30.390.30. 1 hit.
InterPro	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]
PANTHER	PTHR22912:SF20. PTHR22912:SF20. 1 hit.
Pfam	PF00070. Pyr_redox. 1 hit. PF07992. Pyr_redox_2. 1 hit. PF02852. Pyr_redox_dim. 1 hit. [Graphical view]
PRINTS	PR00368. FADPNR.
SUPFAM	SSF55424. FAD/NAD-linked_reductase_dimer. 1 hit.
TIGRFAMs	TIGR01350. lipoamide_DH. 1 hit.
PROSITE	PS00076. PYRIDINE_REDOX_1. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	644542.

Entry information

Entry name

DLDH_RAT

Accession

Primary (citable) accession number: Q6P6R2

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 28, 2006
Last sequence update:	July 5, 2004
Last modified:	April 3, 2013
This is version 78 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Amino acid modifications

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

PTM databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents