UniProt Accession

 ODB2_MOUSE; P53395; Q3TMF5 

Genbank Protein ID

 L42996; AK165959; CH466532 

Genbank Nucleotide ID

 AAC37681.1; BAE38487.1; EDL12381.1 

Protein Name

 Lipoamide acyltransferase component of branched-chain alpha-keto acid dehydrogenase complex, mitochondrial 

Protein Synonyms/Alias

 Branched-chain alpha-keto acid dehydrogenase complex component E2; BCKAD-E2; BCKADE2; Dihydrolipoamide acetyltransferase component of branched-chain alpha-keto acid dehydrogenase complex; Dihydrolipoamide branched chain transacylase; Dihydrolipoyllysine-residue (2-methylpropanoyl)transferase 

Gene Name

 Dbt 

Gene Synonyms/Alias

  

Created Date

 July 27, 2013 

Organism

 Mus musculus (Mouse) 

NCBI Taxa ID

 10090 

Lysine Modification

Position	Peptide	Type	References
68	QGQVVQFKLSDIGEG	acetylation	[1]
82	GIREVTIKEWYVKEG	acetylation	[1, 2, 3]
119	SRYDGVIKRLYYNLD	acetylation	[1]
133	DDIAYVGKPLIDIET	acetylation	[4]
133	DDIAYVGKPLIDIET	succinylation	[4]
196	SEVVGSGKDGRILKE	acetylation	[1, 2, 4]
196	SEVVGSGKDGRILKE	succinylation	[4]
202	GKDGRILKEDILSFL	acetylation	[1, 5, 6, 7]
211	DILSFLEKQTGAILP	acetylation	[4]
211	DILSFLEKQTGAILP	succinylation	[4]
233	TPPPPQPKDRTFPTP	acetylation	[1, 2]
243	TFPTPIAKPPVFTGK	acetylation	[1]
250	KPPVFTGKDRTEPVT	acetylation	[1, 2, 3]
261	EPVTGFQKAMVKTMS	acetylation	[1, 2, 3, 4]
261	EPVTGFQKAMVKTMS	succinylation	[4]
265	GFQKAMVKTMSAALK	acetylation	[2, 3, 4]
265	GFQKAMVKTMSAALK	succinylation	[4]
289	IDLTQLVKLREELKP	acetylation	[1, 4]
289	IDLTQLVKLREELKP	succinylation	[4]
295	VKLREELKPVALARG	acetylation	[1, 2, 3, 6, 8]
304	VALARGIKLSFMPFF	acetylation	[1, 2]
379	MELNRLQKLGSSGQL	acetylation	[1]
410	SIGGTYAKPVILPPE	acetylation	[4]
410	SIGGTYAKPVILPPE	succinylation	[4]
427	IGALGAIKALPRFDQ	acetylation	[7]
435	ALPRFDQKGDVYKAQ	acetylation	[1, 2, 3, 4]
435	ALPRFDQKGDVYKAQ	succinylation	[4]
440	DQKGDVYKAQIMNVS	acetylation	[1, 2, 3, 4, 6]
440	DQKGDVYKAQIMNVS	succinylation	[4]

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] 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]
 [3] 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]
 [4] 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]
 [5] Mitochondrial acetylome analysis in a mouse model of alcohol-induced liver injury utilizing SIRT3 knockout mice.
 Fritz KS, Galligan JJ, Hirschey MD, Verdin E, Petersen DR.
 J Proteome Res. 2012 Mar 2;11(3):1633-43. [PMID: 22309199]
 [6] Quantitative assessment of the impact of the gut microbiota on lysine epsilon-acetylation of host proteins using gnotobiotic mice.
 Simon GM, Cheng J, Gordon JI.
 Proc Natl Acad Sci U S A. 2012 Jul 10;109(28):11133-8. [PMID: 22733758]
 [7] Quantitative acetylome analysis reveals the roles of SIRT1 in regulating diverse substrates and cellular pathways.
 Chen Y, Zhao W, Yang JS, Cheng Z, Luo H, Lu Z, Tan M, Gu W, Zhao Y.
 Mol Cell Proteomics. 2012 Oct;11(10):1048-62. [PMID: 22826441]
 [8] Proteomic investigations of lysine acetylation identify diverse substrates of mitochondrial deacetylase sirt3.
 Sol EM, Wagner SA, Weinert BT, Kumar A, Kim HS, Deng CX, Choudhary C.
 PLoS One. 2012;7(12):e50545. [PMID: 23236377] 

Functional Description

 The branched-chain alpha-keto dehydrogenase complex catalyzes the overall conversion of alpha-keto acids to acyl-CoA and CO(2). It contains multiple copies of three enzymatic components: branched-chain alpha-keto acid decarboxylase (E1), lipoamide acyltransferase (E2) and lipoamide dehydrogenase (E3). Within this complex, the catalytic function of this enzyme is to accept, and to transfer to coenzyme A, acyl groups that are generated by the branched-chain alpha-keto acid decarboxylase component. 

Sequence Annotation

 DOMAIN 65 138 Lipoyl-binding.
 ACT_SITE 452 452 Potential.
 ACT_SITE 456 456 Potential.
 MOD_RES 105 105 N6-lipoyllysine (By similarity).
 MOD_RES 295 295 N6-acetyllysine (By similarity).  

Keyword

 Acetylation; Acyltransferase; Complete proteome; Lipoyl; Mitochondrion; Reference proteome; Transferase; Transit peptide. 

Sequence Source

 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 

Protein Length

 482 AA 

Protein Sequence

Gene Ontology

 GO:0015630; C:microtubule cytoskeleton; IEA:Compara.
 GO:0042645; C:mitochondrial nucleoid; IEA:Compara.
 GO:0005739; C:mitochondrion; IDA:MGI.
 GO:0048037; F:cofactor binding; IEA:InterPro.
 GO:0043754; F:dihydrolipoyllysine-residue (2-methylpropanoyl)transferase activity; IEA:EC.
 GO:0046949; P:fatty-acyl-CoA biosynthetic process; IEA:InterPro. 

Interpro

 IPR003016; 2-oxoA_DH_lipoyl-BS.
 IPR001078; 2-oxoacid_DH_actylTfrase.
 IPR000089; Biotin_lipoyl.
 IPR023213; CAT-like_dom.
 IPR004167; E3-bd.
 IPR015761; Lip_Acyl_TA.
 IPR011053; Single_hybrid_motif. 

Pfam

 PF00198; 2-oxoacid_dh
 PF00364; Biotin_lipoyl
 PF02817; E3_binding 

SMART

  

PROSITE

 PS50968; BIOTINYL_LIPOYL
 PS00189; LIPOYL 

PRINTS