MG1655
W3110
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Gene Report : aceE
PEC Original Annotations
Essentiality
     Class non-essential
     References (PMID)  
     Deletion DE(nadC-aceF)72  ,  DE(aroP-lpd)74  ,  OCR31 (D)  ,  OCR31-4 (D)  ,  OCR31-7 (D)  
Related gene (W3110 PEC)
     Gene Search Search MG1655 PEC by gene name:  aceE
Related strains
     Strains Search Search strains by gene name:  aceE   Search strains by all related name:  aceE aceE1 b0114 ECK0113 JW0110

General information  (Go to Linear View:)
 Gene Name aceE  
 Alternative name aceE1,b0114,ECK0113,JW0110  
 Location, Length 123,017 - 125,680 (  +  ) ;   2.65 min ; 2664 (bp) ,   887 (aa) Go to Linear View
 Product pyruvate dehydrogenase, decarboxylase component E1, thiamin-binding  
 Operon Name pdhR-aceEF-lpd  
 Note pyruvate dehydrogenase (decarboxylase component); GO_process: GO:0016052 - carbohydrate catabolic process; GO_process: GO:0006086 - acetyl-CoA biosynthetic process from pyruvate; GO_process: GO:0006096 - glycolysis; GO_process: GO:0009436 - glyoxylate catabolic process; GO_process: GO:0009061 - anaerobic respiration  
 Function enzyme; Energy metabolism, carbon: Pyruvate dehydrogenase  
 Gene Ontology GO:0000287 ; magnesium ion binding ( aceE )
GO:0003824 ; catalytic activity ( aceE )
GO:0004739 ; pyruvate dehydrogenase (acetyl-transferring) activity ( aceE )
GO:0005515 ; protein binding ( aceE )
GO:0005624 ; membrane fraction ( aceE )
GO:0006096 ; glycolysis ( aceE )
GO:0008152 ; metabolic process ( aceE )
GO:0016491 ; oxidoreductase activity ( aceE )
GO:0046872 ; metal ion binding ( aceE )
 PID 1786304  
 EC number
  (KEGG Pathway)   		1.2.4.1  
Verified Protein Starts (data compiled from literature and appropriate citations are available from EcoGene)
     EcoGene aceE ( EG10024 )  
    Number of removed 1 aa cleaved  
SWISS-PROT  ( Show simple )
  botton Entry name(Acc.no) ODP1_ECOLI ( P06958 ; P78049; Q53382 )
    -  Protein name Pyruvate dehydrogenase E1 component  
    -  Synonyms EC 1.2.4.1  
    -  Gene name Name=aceE; OrderedLocusNames=b0114, z0124, ECs0118;  
    -  Comments
  • FUNCTION: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).
  • CATALYTIC ACTIVITY:Pyruvate + [dihydrolipoyllysine-residue acetyltransferase] lipoyllysine = [dihydrolipoyllysine-residue acetyltransferase] S-acetyldihydrolipoyllysine + CO(2).
  • COFACTOR:Thiamine pyrophosphate and magnesium ions.
  • SUBUNIT:Homodimer.  
    •   botton Entry name(Acc.no) Q8FL43 ( Q8FL43 )
        -  Protein name Pyruvate dehydrogenase E1 component  
        -  Synonyms EC 1.2.4.1  
        -  Gene name Name=aceE; OrderedLocusNames=c0142;  
        -  Comments
  • SIMILARITY:Belongs to the ABC transporter family.  

    •  Linear View (Whole Mode)
    View Location
       110.0  –  135.0 (KBP)

    Homology Analysis
    BLAST
        Bacteria
             GTOP aceE (  homologous genes of other bacterias  )  
        PDB     (database updated : 2007.02.20 )
             PSI-BLAST Chain A, E. Coli Pyruvate Dehydrogenase  
        SWISS-PROT     (database updated : 2007.02.20 )
             BLAST Pyruvate dehydrogenase E1 component  
             PSI-BLAST Pyruvate dehydrogenase E1 component
        nr     (database updated : 2007.02.20 )
             BLAST pyruvate dehydrogenase (decarboxylase component) [Escherichia coli O157:H7 EDL933]  
    Pfam 28.0   (database updated : 2015-05 )
        Pfam
    PROSITE
        PROSITE ASN_GLYCOSYLATION    CAMP_PHOSPHO_SITE    PKC_PHOSPHO_SITE    CK2_PHOSPHO_SITE    TYR_PHOSPHO_SITE    MYRISTYL     

    Other Cross-Reference
        COG COG2609C 
        EcoCyc aceE 

    MMBR References
    J Gen Microbiol. 1980;121(2):277-92.
    Molecular cloning of the pyruvate dehydrogenase complex genes of Escherichia coli.
    Guest JR, Stephens PE. ( 6455499 )
    J Bacteriol. 1983;153(2):588-96.
    Cloning, mapping, and expression of the fumarase gene of Escherichia coli K-12.
    Guest JR, Roberts RE. ( 6296045 )
    J Gen Microbiol. 1983;129(3):671-80.
    Hybrid plasmids containing the pyruvate dehydrogenase complex genes and gene-DNA relationships in the 2 to 3 minute region of the Escherichia coli chromosome.
    Guest JR, Roberts RE, Stephens PE. ( 6308128 )
    J Gen Microbiol. 1981;127:65-79.
    Organization and expression of the pyruvate dehydrogenase complex genes of Escherichia coli K12.
    Guest, J. R., S. T. Cole, and K. Jeyaseelan.
    Biochem J. 1987;245(3):869-74.
    Subgenes expressing single lipoyl domains of the pyruvate dehydrogenase complex of Escherichia coli.
    Miles JS, Guest JR. ( 3117051 )
    Mol Gen Genet. 1985;200(1):145-54.
    Transcription analysis of the sucAB, aceEF and lpd genes of Escherichia coli.
    Spencer ME, Guest JR. ( 3897791 )
    Eur J Biochem. 1983;133:155-162
    The pyruvate dehydrogenase complex of Escherichia coli K-12. Nucleotide sequence encoding the pyruvate dehydrogenase component.
    Stephens, P. E., M. G. Darlison, H. M. Lewis, and J. R. Guest.
    FEMS Microbiol Lett. 1998;159(2):325-9.
    Environmental control of pyruvate dehydrogenase complex expression in Escherichia coli.
    Cassey B, Guest JR, Attwood MM. ( 9503628 )

    Sequences
    Amino acid
    FASTA format 
    0001 MSERFPNDVD PIETRDWLQA IESVIREEGV ERAQYLIDQL LAEARKGGVN VAAGTGISNY INTIPVEEQP 
0071 EYPGNLELER RIRSAIRWNA IMTVLRASKK DLELGGHMAS FQSSATIYDV CFNHFFRARN EQDGGDLVYF 
0141 QGHISPGVYA RAFLEGRLTQ EQLDNFRQEV HGNGLSSYPH PKLMPEFWQF PTVSMGLGPI GAIYQAKFLK 
0211 YLEHRGLKDT SKQTVYAFLG DGEMDEPESK GAITIATREK LDNLVFVINC NLQRLDGPVT GNGKIINELE 
0281 GIFEGAGWNV IKVMWGSRWD ELLRKDTSGK LIQLMNETVD GDYQTFKSKD GAYVREHFFG KYPETAALVA 
0351 DWTDEQIWAL NRGGHDPKKI YAAFKKAQET KGKATVILAH TIKGYGMGDA AEGKNIAHQV KKMNMDGVRH 
0421 IRDRFNVPVS DADIEKLPYI TFPEGSEEHT YLHAQRQKLH GYLPSRQPNF TEKLELPSLQ DFGALLEEQS 
0491 KEISTTIAFV RALNVMLKNK SIKDRLVPII ADEARTFGME GLFRQIGIYS PNGQQYTPQD REQVAYYKED 
0561 EKGQILQEGI NELGAGCSWL AAATSYSTNN LPMIPFYIYY SMFGFQRIGD LCWAAGDQQA RGFLIGGTSG 
0631 RTTLNGEGLQ HEDGHSHIQS LTIPNCISYD PAYAYEVAVI MHDGLERMYG EKQENVYYYI TTLNENYHMP 
0701 AMPEGAEEGI RKGIYKLETI EGSKGKVQLL GSGSILRHVR EAAEILAKDY GVGSDVYSVT SFTELARDGQ 
0771 DCERWNMLHP LETPRVPYIA QVMNDAPAVA STDYMKLFAE QVRTYVPADD YRVLGTDGFG RSDSRENLRH 
0841 HFEVDASYVV VAALGELAKR GEIDKKVVAD AIAKFNIDAD KVNPRLA
    Nucleotide
    FASTA format

    View sequence out neighbor 100bp 
    -100                                             GCAACTAAAC GTAGAACCTG TCTTATTGAG 
-070 CTTTCCGGCG AGAGTTCAAT GGGACAGGTT CCAGAAAACT CAACGTTATT AGATAGATAA GGAATAACCC 
0001 atgtcagaac gtttcccaaa tgacgtggat ccgatcgaaa ctcgcgactg gctccaggcg atcgaatcgg 
0071 tcatccgtga agaaggtgtt gagcgtgctc agtatctgat cgaccaactg cttgctgaag cccgcaaagg 
0141 cggtgtaaac gtagccgcag gcacaggtat cagcaactac atcaacacca tccccgttga agaacaaccg 
0211 gagtatccgg gtaatctgga actggaacgc cgtattcgtt cagctatccg ctggaacgcc atcatgacgg 
0281 tgctgcgtgc gtcgaaaaaa gacctcgaac tgggcggcca tatggcgtcc ttccagtctt ccgcaaccat 
0351 ttatgatgtg tgctttaacc acttcttccg tgcacgcaac gagcaggatg gcggcgacct ggtttacttc 
0421 cagggccaca tctccccggg cgtgtacgct cgtgctttcc tggaaggtcg tctgactcag gagcagctgg 
0491 ataacttccg tcaggaagtt cacggcaatg gcctctcttc ctatccgcac ccgaaactga tgccggaatt 
0561 ctggcagttc ccgaccgtat ctatgggtct gggtccgatt ggtgctattt accaggctaa attcctgaaa 
0631 tatctggaac accgtggcct gaaagatacc tctaaacaaa ccgtttacgc gttcctcggt gacggtgaaa 
0701 tggacgaacc ggaatccaaa ggtgcgatca ccatcgctac ccgtgaaaaa ctggataacc tggtcttcgt 
0771 tatcaactgt aacctgcagc gtcttgacgg cccggtcacc ggtaacggca agatcatcaa cgaactggaa 
0841 ggcatcttcg aaggtgctgg ctggaacgtg atcaaagtga tgtggggtag ccgttgggat gaactgctgc 
0911 gtaaggatac cagcggtaaa ctgatccagc tgatgaacga aaccgttgac ggcgactacc agaccttcaa 
0981 atcgaaagat ggtgcgtacg ttcgtgaaca cttcttcggt aaatatcctg aaaccgcagc actggttgca 
1051 gactggactg acgagcagat ctgggcactg aaccgtggtg gtcacgatcc gaagaaaatc tacgctgcat 
1121 tcaagaaagc gcaggaaacc aaaggcaaag cgacagtaat ccttgctcat accattaaag gttacggcat 
1191 gggcgacgcg gctgaaggta aaaacatcgc gcaccaggtt aagaaaatga acatggacgg tgtgcgtcat 
1261 atccgcgacc gtttcaatgt gccggtgtct gatgcagata tcgaaaaact gccgtacatc accttcccgg 
1331 aaggttctga agagcatacc tatctgcacg ctcagcgtca gaaactgcac ggttatctgc caagccgtca 
1401 gccgaacttc accgagaagc ttgagctgcc gagcctgcaa gacttcggcg cgctgttgga agagcagagc 
1471 aaagagatct ctaccactat cgctttcgtt cgtgctctga acgtgatgct gaagaacaag tcgatcaaag 
1541 atcgtctggt accgatcatc gccgacgaag cgcgtacttt cggtatggaa ggtctgttcc gtcagattgg 
1611 tatttacagc ccgaacggtc agcagtacac cccgcaggac cgcgagcagg ttgcttacta taaagaagac 
1681 gagaaaggtc agattctgca ggaagggatc aacgagctgg gcgcaggttg ttcctggctg gcagcggcga 
1751 cctcttacag caccaacaat ctgccgatga tcccgttcta catctattac tcgatgttcg gcttccagcg 
1821 tattggcgat ctgtgctggg cggctggcga ccagcaagcg cgtggcttcc tgatcggcgg tacttccggt 
1891 cgtaccaccc tgaacggcga aggtctgcag cacgaagatg gtcacagcca cattcagtcg ctgactatcc 
1961 cgaactgtat ctcttacgac ccggcttacg cttacgaagt tgctgtcatc atgcatgacg gtctggagcg 
2031 tatgtacggt gaaaaacaag agaacgttta ctactacatc actacgctga acgaaaacta ccacatgccg 
2101 gcaatgccgg aaggtgctga ggaaggtatc cgtaaaggta tctacaaact cgaaactatt gaaggtagca 
2171 aaggtaaagt tcagctgctc ggctccggtt ctatcctgcg tcacgtccgt gaagcagctg agatcctggc 
2241 gaaagattac ggcgtaggtt ctgacgttta tagcgtgacc tccttcaccg agctggcgcg tgatggtcag 
2311 gattgtgaac gctggaacat gctgcacccg ctggaaactc cgcgcgttcc gtatatcgct caggtgatga 
2381 acgacgctcc ggcagtggca tctaccgact atatgaaact gttcgctgag caggtccgta cttacgtacc 
2451 ggctgacgac taccgcgtac tgggtactga tggcttcggt cgttccgaca gccgtgagaa cctgcgtcac 
2521 cacttcgaag ttgatgcttc ttatgtcgtg gttgcggcgc tgggcgaact ggctaaacgt ggcgaaatcg 
2591 ataagaaagt ggttgctgac gcaatcgcca aattcaacat cgatgcagat aaagttaacc cgcgtctggc 
2661 gtaaGAGGTA AAAGAATAAT GGCTATCGAA ATCAAAGTAC CGGACATCGG GGCTGATGAA GTTGAAATCA 
2731 CCGAGATCCT GGTCAAAGTG GGCGACAAAG TTGA