CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-002407
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 
Gene Name
 aceF 
Gene Synonyms/Alias
 b0115; JW0111 
Created Date
 July 27, 2013 
Organism
 Escherichia coli (strain K12) 
NCBI Taxa ID
 83333 
Lysine Modification
Position
Peptide
Type
References
64IKVSVGDKTQTGALIacetylation[1]
91APAQAEEKKEAAPAAacetylation[1]
106APAAAAAKDVNVPDIacetylation[1]
161AGTVKEIKVNVGDKVpupylation[2]
207PAPAAGVKEVNVPDIacetylation[1]
262AGVVKELKVNVGDKVacetylation[1]
268LKVNVGDKVKTGSLIacetylation[1]
302AAPAPAAKAEAPAAAacetylation[1]
313PAAAPAAKAEGKSEFacetylation[1]
317PAAKAEGKSEFAENDacetylation[1]
346EFGVNLAKVKGTGRKacetylation[1]
348GVNLAKVKGTGRKGRacetylation[1]
366EDVQAYVKEAIKRAEacetylation[1, 3]
370AYVKEAIKRAEAAPAacetylation[1]
391PGMLPWPKVDFSKFGacetylation[1]
396WPKVDFSKFGEIEEVacetylation[1, 3, 4, 5]
410VELGRIQKISGANLSacetylation[1, 5]
431PHVTHFDKTDITELEacetylation[1]
442TELEAFRKQQNEEAAacetylation[1]
450QQNEEAAKRKLDVKIacetylation[1, 5]
452NEEAAKRKLDVKITPacetylation[1]
456AKRKLDVKITPVVFIacetylation[1, 5]
492GQRLTLKKYINIGVAacetylation[1]
512GLVVPVFKDVNKKGIacetylation[1]
516PVFKDVNKKGIIELSacetylation[1]
531RELMTISKKARDGKLacetylation[1, 5]
532ELMTISKKARDGKLTacetylation[1]
587MEPVWNGKEFVPRLMacetylation[1, 5]
Reference
 [1] Acetyl-Phosphate Is a Critical Determinant of Lysine Acetylation in E. coli.
 Weinert BT, Iesmantavicius V, Wagner SA, Schölz C, Gummesson B, Beli P, Nyström T, Choudhary C.
 Mol Cell. 2013 Jul 25;51(2):265-72. [PMID: 23830618]
 [2] Reconstitution of the Mycobacterium tuberculosis pupylation pathway in Escherichia coli.
 Cerda-Maira FA, McAllister F, Bode NJ, Burns KE, Gygi SP, Darwin KH.
 EMBO Rep. 2011 Jul 8;12(8):863-70. [PMID: 21738222]
 [3] The diversity of lysine-acetylated proteins in Escherichia coli.
 Yu BJ, Kim JA, Moon JH, Ryu SE, Pan JG.
 J Microbiol Biotechnol. 2008 Sep;18(9):1529-36. [PMID: 18852508]
 [4] Lysine acetylation is a highly abundant and evolutionarily conserved modification in Escherichia coli.
 Zhang J, Sprung R, Pei J, Tan X, Kim S, Zhu H, Liu CF, Grishin NV, Zhao Y.
 Mol Cell Proteomics. 2009 Feb;8(2):215-25. [PMID: 18723842]
 [5] Comprehensive profiling of protein lysine acetylation in Escherichia coli.
 Zhang K, Zheng S, Yang JS, Chen Y, Cheng Z.
 J Proteome Res. 2013 Feb 1;12(2):844-51. [PMID: 23294111] 
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 74 Lipoyl-binding 1.
 DOMAIN 106 177 Lipoyl-binding 2.
 DOMAIN 207 278 Lipoyl-binding 3.
 REGION 317 630 Subunit binding, catalytic.
 REGION 373 389 Hydrophobic.
 REGION 542 567 Hydrophobic.
 ACT_SITE 547 547 Potential.
 ACT_SITE 603 603
 ACT_SITE 607 607 Potential.
 MOD_RES 41 41 N6-lipoyllysine.
 MOD_RES 144 144 N6-lipoyllysine.
 MOD_RES 245 245 N6-lipoyllysine.
 MOD_RES 396 396 N6-acetyllysine.  
Keyword
 3D-structure; Acetylation; Acyltransferase; Complete proteome; Direct protein sequencing; Glycolysis; Lipoyl; Reference proteome; Repeat; Transferase. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 630 AA 
Protein Sequence
MAIEIKVPDI GADEVEITEI LVKVGDKVEA EQSLITVEGD KASMEVPSPQ AGIVKEIKVS 60
VGDKTQTGAL IMIFDSADGA ADAAPAQAEE KKEAAPAAAP AAAAAKDVNV PDIGSDEVEV 120
TEILVKVGDK VEAEQSLITV EGDKASMEVP APFAGTVKEI KVNVGDKVST GSLIMVFEVA 180
GEAGAAAPAA KQEAAPAAAP APAAGVKEVN VPDIGGDEVE VTEVMVKVGD KVAAEQSLIT 240
VEGDKASMEV PAPFAGVVKE LKVNVGDKVK TGSLIMIFEV EGAAPAAAPA KQEAAAPAPA 300
AKAEAPAAAP AAKAEGKSEF AENDAYVHAT PLIRRLAREF GVNLAKVKGT GRKGRILRED 360
VQAYVKEAIK RAEAAPAATG GGIPGMLPWP KVDFSKFGEI EEVELGRIQK ISGANLSRNW 420
VMIPHVTHFD KTDITELEAF RKQQNEEAAK RKLDVKITPV VFIMKAVAAA LEQMPRFNSS 480
LSEDGQRLTL KKYINIGVAV DTPNGLVVPV FKDVNKKGII ELSRELMTIS KKARDGKLTA 540
GEMQGGCFTI SSIGGLGTTH FAPIVNAPEV AILGVSKSAM EPVWNGKEFV PRLMLPISLS 600
FDHRVIDGAD GARFITIINN TLSDIRRLVM 630 
Gene Ontology
 GO:0045254; C:pyruvate dehydrogenase complex; IDA:EcoliWiki.
 GO:0004742; F:dihydrolipoyllysine-residue acetyltransferase activity; IDA:EcoliWiki.
 GO:0031405; F:lipoic acid binding; IDA:EcoliWiki.
 GO:0006086; P:acetyl-CoA biosynthetic process from pyruvate; IMP:EcoliWiki.
 GO:0006096; P:glycolysis; IEA:UniProtKB-KW. 
Interpro
 IPR003016; 2-oxoA_DH_lipoyl-BS.
 IPR001078; 2-oxoacid_DH_actylTfrase.
 IPR006256; AcTrfase_Pyrv_DH_cplx.
 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