UniProt Accession

 DHTK1_MOUSE; A2ATU0; Q0VFY3; Q69ZE3; Q8BWT3 

Genbank Protein ID

 AL928924; BC117994; AK173223; AK050057 

Genbank Nucleotide ID

 CAM20352.1; AAI17995.1; BAD32501.1; BAC34055.1 

Protein Name

 Probable 2-oxoglutarate dehydrogenase E1 component DHKTD1, mitochondrial 

Protein Synonyms/Alias

 Dehydrogenase E1 and transketolase domain-containing protein 1 

Gene Name

 Dhtkd1 

Gene Synonyms/Alias

 Kiaa1630 

Created Date

 July 27, 2013 

Organism

 Mus musculus (Mouse) 

NCBI Taxa ID

 10090 

Lysine Modification

Position	Peptide	Type	References
156	RRFEELKKETFTTEE	acetylation	[1]
184	FDHFLATKFATVKRY	acetylation	[2]
184	FDHFLATKFATVKRY	succinylation	[2]
189	ATKFATVKRYGGEGA	acetylation	[2]
189	ATKFATVKRYGGEGA	succinylation	[2]
554	QVHSHLLKMYVQSRM	acetylation	[1]
801	GDSSVDPKNVKTLIF	acetylation	[2]
801	GDSSVDPKNVKTLIF	succinylation	[2]
804	SVDPKNVKTLIFCSG	acetylation	[2]
804	SVDPKNVKTLIFCSG	succinylation	[2]
819	KHFYALLKQRESLGT	acetylation	[2, 3, 4]
819	KHFYALLKQRESLGT	succinylation	[2]
828	RESLGTKKHDFAIIR	acetylation	[5]

Reference

 [1] Label-free quantitative proteomics of the lysine acetylome in mitochondria identifies substrates of SIRT3 in metabolic pathways.
 Rardin MJ, Newman JC, Held JM, Cusack MP, Sorensen DJ, Li B, Schilling B, Mooney SD, Kahn CR, Verdin E, Gibson BW.
 Proc Natl Acad Sci U S A. 2013 Apr 16;110(16):6601-6. [PMID: 23576753]
 [2] SIRT5-Mediated Lysine Desuccinylation Impacts Diverse Metabolic Pathways.
 Park J, Chen Y, Tishkoff DX, Peng C, Tan M, Dai L, Xie Z, Zhang Y, Zwaans BM, Skinner ME, Lombard DB, Zhao Y.
 Mol Cell. 2013 Jun 27;50(6):919-30. [PMID: 23806337]
 [3] Calorie restriction and SIRT3 trigger global reprogramming of the mitochondrial protein acetylome.
 Hebert AS, Dittenhafer-Reed KE, Yu W, Bailey DJ, Selen ES, Boersma MD, Carson JJ, Tonelli M, Balloon AJ, Higbee AJ, Westphall MS, Pagliarini DJ, Prolla TA, Assadi-Porter F, Roy S, Denu JM, Coon JJ.
 Mol Cell. 2013 Jan 10;49(1):186-99. [PMID: 23201123]
 [4] Quantification of mitochondrial acetylation dynamics highlights prominent sites of metabolic regulation.
 Still AJ, Floyd BJ, Hebert AS, Bingman CA, Carson JJ, Gunderson DR, Dolan BK, Grimsrud PA, Dittenhafer-Reed KE, Stapleton DS, Keller MP, Westphall MS, Denu JM, Attie AD, Coon JJ, Pagliarini DJ.
 J Biol Chem. 2013 Jul 17;. [PMID: 23864654]
 [5] Proteomic analysis of lysine acetylation sites in rat tissues reveals organ specificity and subcellular patterns.
 Lundby A, Lage K, Weinert BT, Bekker-Jensen DB, Secher A, Skovgaard T, Kelstrup CD, Dmytriyev A, Choudhary C, Lundby C, Olsen JV.
 Cell Rep. 2012 Aug 30;2(2):419-31. [PMID: 22902405] 

Functional Description

 The 2-oxoglutarate dehydrogenase complex catalyzes the overall conversion of 2-oxoglutarate to succinyl-CoA and CO(2). It contains multiple copies of three enzymatic components: 2- oxoglutarate dehydrogenase (E1), dihydrolipoamide succinyltransferase (E2) and lipoamide dehydrogenase (E3) (By similarity). 

Sequence Annotation

  

Keyword

 Complete proteome; Glycolysis; Mitochondrion; Oxidoreductase; Reference proteome; Thiamine pyrophosphate; Transit peptide. 

Sequence Source

 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 

Protein Length

 921 AA 

Protein Sequence

Gene Ontology

 GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
 GO:0004591; F:oxoglutarate dehydrogenase (succinyl-transferring) activity; IEA:EC.
 GO:0030976; F:thiamine pyrophosphate binding; IEA:InterPro.
 GO:0006096; P:glycolysis; IEA:UniProtKB-KW.
 GO:0006099; P:tricarboxylic acid cycle; IEA:InterPro. 

Interpro

 IPR011603; 2oxoglutarate_DH_E1.
 IPR001017; DH_E1.
 IPR005475; Transketolase-like_Pyr-bd. 

Pfam

 PF00676; E1_dh
 PF02779; Transket_pyr 

SMART

 SM00861; Transket_pyr 

PROSITE

  

PRINTS