CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-003890
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
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
 BCATE2 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
295VKLREELKPIAFARGacetylation[1, 2, 3]
440NQKGEVYKAQIMNVSacetylation[3, 4, 5]
Reference
 [1] Lysine acetylation targets protein complexes and co-regulates major cellular functions.
 Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M.
 Science. 2009 Aug 14;325(5942):834-40. [PMID: 19608861]
 [2] Proteomic investigations reveal a role for RNA processing factor THRAP3 in the DNA damage response.
 Beli P, Lukashchuk N, Wagner SA, Weinert BT, Olsen JV, Baskcomb L, Mann M, Jackson SP, Choudhary C.
 Mol Cell. 2012 Apr 27;46(2):212-25. [PMID: 22424773]
 [3] Integrated proteomic analysis of post-translational modifications by serial enrichment.
 Mertins P, Qiao JW, Patel J, Udeshi ND, Clauser KR, Mani DR, Burgess MW, Gillette MA, Jaffe JD, Carr SA.
 Nat Methods. 2013 Jul;10(7):634-7. [PMID: 23749302]
 [4] Regulation of cellular metabolism by protein lysine acetylation.
 Zhao S, Xu W, Jiang W, Yu W, Lin Y, Zhang T, Yao J, Zhou L, Zeng Y, Li H, Li Y, Shi J, An W, Hancock SM, He F, Qin L, Chin J, Yang P, Chen X, Lei Q, Xiong Y, Guan KL.
 Science. 2010 Feb 19;327(5968):1000-4. [PMID: 20167786]
 [5] 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.  
Keyword
 3D-structure; Acetylation; Acyltransferase; Complete proteome; Direct protein sequencing; Disease mutation; Lipoyl; Maple syrup urine disease; Mitochondrion; Reference proteome; Transferase; Transit peptide. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 482 AA 
Protein Sequence
MAAVRMLRTW SRNAGKLICV RYFQTCGNVH VLKPNYVCFF GYPSFKYSHP HHFLKTTAAL 60
RGQVVQFKLS DIGEGIREVT VKEWYVKEGD TVSQFDSICE VQSDKASVTI TSRYDGVIKK 120
LYYNLDDIAY VGKPLVDIET EALKDSEEDV VETPAVSHDE HTHQEIKGRK TLATPAVRRL 180
AMENNIKLSE VVGSGKDGRI LKEDILNYLE KQTGAILPPS PKVEIMPPPP KPKDMTVPIL 240
VSKPPVFTGK DKTEPIKGFQ KAMVKTMSAA LKIPHFGYCD EIDLTELVKL REELKPIAFA 300
RGIKLSFMPF FLKAASLGLL QFPILNASVD ENCQNITYKA SHNIGIAMDT EQGLIVPNVK 360
NVQICSIFDI ATELNRLQKL GSVGQLSTTD LTGGTFTLSN IGSIGGTFAK PVIMPPEVAI 420
GALGSIKAIP RFNQKGEVYK AQIMNVSWSA DHRVIDGATM SRFSNLWKSY LENPAFMLLD 480
LK 482 
Gene Ontology
 GO:0015630; C:microtubule cytoskeleton; IDA:HPA.
 GO:0005947; C:mitochondrial alpha-ketoglutarate dehydrogenase complex; TAS:ProtInc.
 GO:0042645; C:mitochondrial nucleoid; IDA:BHF-UCL.
 GO:0048037; F:cofactor binding; IEA:InterPro.
 GO:0043754; F:dihydrolipoyllysine-residue (2-methylpropanoyl)transferase activity; IEA:EC.
 GO:0009083; P:branched-chain amino acid catabolic process; TAS:Reactome.
 GO:0034641; P:cellular nitrogen compound metabolic process; TAS:Reactome.
 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