CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-005016
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex 
Protein Synonyms/Alias
 Dihydrolipoamide acetyltransferase component of pyruvate dehydrogenase complex; E2; S complex, 48 kDa subunit 
Gene Name
 pdhC 
Gene Synonyms/Alias
 aceC; BSU14600 
Created Date
 July 27, 2013 
Organism
 Bacillus subtilis (strain 168) 
NCBI Taxa ID
 224308 
Lysine Modification
Position
Peptide
Type
References
257VAHRKQFKQVAADQGacetylation[1]
Reference
 [1] The acetylproteome of Gram-positive model bacterium Bacillus subtilis.
 Kim D, Yu BJ, Kim JA, Lee YJ, Choi SG, Kang S, Pan JG.
 Proteomics. 2013 May;13(10-11):1726-36. [PMID: 23468065] 
Functional Description
 The pyruvate dehydrogenase complex catalyzes the overall conversion of pyruvate to acetyl-CoA and CO(2). It contains multiple copies of three enzymatic components: pyruvate dehydrogenase (E1), dihydrolipoamide acetyltransferase (E2) and lipoamide dehydrogenase (E3). 
Sequence Annotation
 DOMAIN 2 76 Lipoyl-binding.
 REGION 140 182 E1/E3 binding.
 ACT_SITE 413 413 Potential.
 MOD_RES 43 43 N6-lipoyllysine.  
Keyword
 Acyltransferase; Complete proteome; Glycolysis; Lipoyl; Reference proteome; Transferase. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 442 AA 
Protein Sequence
MAFEFKLPDI GEGIHEGEIV KWFVKPNDEV DEDDVLAEVQ NDKAVVEIPS PVKGKVLELK 60
VEEGTVATVG QTIITFDAPG YEDLQFKGSD ESDDAKTEAQ VQSTAEAGQD VAKEEQAQEP 120
AKATGAGQQD QAEVDPNKRV IAMPSVRKYA REKGVDIRKV TGSGNNGRVV KEDIDSFVNG 180
GAQEAAPQET AAPQETAAKP AAAPAPEGEF PETREKMSGI RKAIAKAMVN SKHTAPHVTL 240
MDEVDVTNLV AHRKQFKQVA ADQGIKLTYL PYVVKALTSA LKKFPVLNTS IDDKTDEVIQ 300
KHYFNIGIAA DTEKGLLVPV VKNADRKSVF EISDEINGLA TKAREGKLAP AEMKGASCTI 360
TNIGSAGGQW FTPVINHPEV AILGIGRIAE KAIVRDGEIV AAPVLALSLS FDHRMIDGAT 420
AQNALNHIKR LLNDPQLILM EA 442 
Gene Ontology
 GO:0004742; F:dihydrolipoyllysine-residue acetyltransferase activity; IEA:EC.
 GO:0006096; P:glycolysis; IEA:UniProtKB-KW. 
Interpro
 IPR003016; 2-oxoA_DH_lipoyl-BS.
 IPR001078; 2-oxoacid_DH_actylTfrase.
 IPR000089; Biotin_lipoyl.
 IPR023213; CAT-like_dom.
 IPR004167; E3-bd.
 IPR011053; Single_hybrid_motif. 
Pfam
 PF00198; 2-oxoacid_dh
 PF00364; Biotin_lipoyl
 PF02817; E3_binding 
SMART
  
PROSITE
 PS50968; BIOTINYL_LIPOYL
 PS00189; LIPOYL 
PRINTS