CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-003542
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Pyruvate dehydrogenase E1 component 
Protein Synonyms/Alias
 PDH E1 component 
Gene Name
 aceE 
Gene Synonyms/Alias
 b0114; JW0110 
Created Date
 July 27, 2013 
Organism
 Escherichia coli (strain K12) 
NCBI Taxa ID
 83333 
Lysine Modification
Position
Peptide
Type
References
210IYQAKFLKYLEHRGLacetylation[1]
222RGLKDTSKQTVYAFLacetylation[1, 2]
250ITIATREKLDNLVFVacetylation[1]
305RWDELLRKDTSGKLIacetylation[1, 2]
310LRKDTSGKLIQLMNEacetylation[1]
327DGDYQTFKSKDGAYVacetylation[1, 2]
329DYQTFKSKDGAYVREacetylation[1, 2]
368NRGGHDPKKIYAAFKacetylation[1]
375KKIYAAFKKAQETKGacetylation[1]
383KAQETKGKATVILAHacetylation[1]
393VILAHTIKGYGMGDAacetylation[1, 2]
404MGDAAEGKNIAHQVKacetylation[1, 2]
411KNIAHQVKKMNMDGVacetylation[1, 2]
412NIAHQVKKMNMDGVRacetylation[1, 2]
436VSDADIEKLPYITFPacetylation[1]
458YLHAQRQKLHGYLPSacetylation[1, 2]
473RQPNFTEKLELPSLQacetylation[1]
508RALNVMLKNKSIKDRacetylation[1, 2]
510LNVMLKNKSIKDRLVacetylation[1]
558REQVAYYKEDEKGQIacetylation[1]
682LERMYGEKQENVYYYacetylation[1]
716GIRKGIYKLETIEGSacetylation[1, 3]
724LETIEGSKGKVQLLGacetylation[1]
748EAAEILAKDYGVGSDacetylation[1]
865AKRGEIDKKVVADAIacetylation[1]
866KRGEIDKKVVADAIAacetylation[1, 2]
874VVADAIAKFNIDADKacetylation[1]
881KFNIDADKVNPRLA*acetylation[1]
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] 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]
 [3] 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] 
Functional Description
 Component of the pyruvate dehydrogenase (PDH) complex, that catalyzes the overall conversion of pyruvate to acetyl-CoA and CO(2). 
Sequence Annotation
 METAL 231 231 Magnesium.
 METAL 261 261 Magnesium.
 METAL 263 263 Magnesium; via carbonyl oxygen.
 MOD_RES 716 716 N6-acetyllysine.  
Keyword
 3D-structure; Acetylation; Complete proteome; Direct protein sequencing; Glycolysis; Magnesium; Metal-binding; Oxidoreductase; Pyruvate; Reference proteome; Thiamine pyrophosphate. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 887 AA 
Protein Sequence
MSERFPNDVD PIETRDWLQA IESVIREEGV ERAQYLIDQL LAEARKGGVN VAAGTGISNY 60
INTIPVEEQP EYPGNLELER RIRSAIRWNA IMTVLRASKK DLELGGHMAS FQSSATIYDV 120
CFNHFFRARN EQDGGDLVYF QGHISPGVYA RAFLEGRLTQ EQLDNFRQEV HGNGLSSYPH 180
PKLMPEFWQF PTVSMGLGPI GAIYQAKFLK YLEHRGLKDT SKQTVYAFLG DGEMDEPESK 240
GAITIATREK LDNLVFVINC NLQRLDGPVT GNGKIINELE GIFEGAGWNV IKVMWGSRWD 300
ELLRKDTSGK LIQLMNETVD GDYQTFKSKD GAYVREHFFG KYPETAALVA DWTDEQIWAL 360
NRGGHDPKKI YAAFKKAQET KGKATVILAH TIKGYGMGDA AEGKNIAHQV KKMNMDGVRH 420
IRDRFNVPVS DADIEKLPYI TFPEGSEEHT YLHAQRQKLH GYLPSRQPNF TEKLELPSLQ 480
DFGALLEEQS KEISTTIAFV RALNVMLKNK SIKDRLVPII ADEARTFGME GLFRQIGIYS 540
PNGQQYTPQD REQVAYYKED EKGQILQEGI NELGAGCSWL AAATSYSTNN LPMIPFYIYY 600
SMFGFQRIGD LCWAAGDQQA RGFLIGGTSG RTTLNGEGLQ HEDGHSHIQS LTIPNCISYD 660
PAYAYEVAVI MHDGLERMYG EKQENVYYYI TTLNENYHMP AMPEGAEEGI RKGIYKLETI 720
EGSKGKVQLL GSGSILRHVR EAAEILAKDY GVGSDVYSVT SFTELARDGQ DCERWNMLHP 780
LETPRVPYIA QVMNDAPAVA STDYMKLFAE QVRTYVPADD YRVLGTDGFG RSDSRENLRH 840
HFEVDASYVV VAALGELAKR GEIDKKVVAD AIAKFNIDAD KVNPRLA 887 
Gene Ontology
 GO:0005829; C:cytosol; IDA:UniProtKB.
 GO:0016020; C:membrane; IDA:UniProtKB.
 GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
 GO:0004739; F:pyruvate dehydrogenase (acetyl-transferring) activity; IEA:EC.
 GO:0004738; F:pyruvate dehydrogenase activity; IGI:EcoliWiki.
 GO:0006096; P:glycolysis; IEA:UniProtKB-KW. 
Interpro
 IPR004660; 2-oxoA_DH_E1.
 IPR009014; Transketo_C/Pyr-ferredox_oxred.
 IPR015941; Transketolase-like_C.
 IPR005474; Transketolase_N. 
Pfam
 PF00456; Transketolase_N 
SMART
  
PROSITE
  
PRINTS