MG1655
W3110
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Gene Report : aceF
PEC Original Annotations
Essentiality
     Class non-essential
     References (PMID)  
     Deletion DE(aroP-lpd)74  ,  OCR31 (D)  ,  OCR31-4 (D)  ,  OCR31-7 (D)  
Related gene (W3110 PEC)
     Gene Search Search MG1655 PEC by gene name:  aceF
Related strains
     Strains Search Search strains by gene name:  aceF   Search strains by all related name:  aceF aceE2 b0115 ECK0114 JW0111

General information  (Go to Linear View:)
 Gene Name aceF  
 Alternative name aceE2,b0115,ECK0114,JW0111  
 Location, Length 125,695 - 127,587 (  +  ) ;   2.71 min ; 1893 (bp) ,   630 (aa) Go to Linear View
 Product pyruvate dehydrogenase, dihydrolipoyltransacetylase component E2  
 Operon Name pdhR-aceEF-lpd  
 Note pyruvate dehydrogenase (dihydrolipoyltransacetylase 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:0004742 ; dihydrolipoyllysine-residue acetyltransferase activity ( aceF )
GO:0005515 ; protein binding ( aceF )
GO:0005737 ; cytoplasm ( aceF )
GO:0006096 ; glycolysis ( aceF )
GO:0008152 ; metabolic process ( aceF )
GO:0008415 ; acyltransferase activity ( aceF )
GO:0016740 ; transferase activity ( aceF )
GO:0031405 ; lipoic acid binding ( aceF )
GO:0045254 ; pyruvate dehydrogenase complex ( aceF )
 PID 1786305  
 EC number
  (KEGG Pathway)   		2.3.1.12  
Verified Protein Starts (data compiled from literature and appropriate citations are available from EcoGene)
     EcoGene aceF ( EG10025 )  
    Number of removed 1 aa cleaved  
SWISS-PROT  ( Show simple )
  botton Entry name(Acc.no) ODP2_ECOLI ( P06959 )
    -  Protein name Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex  
    -  Synonyms EC 2.3.1.12, E2, Dihydrolipoamide acetyltransferase component of pyruvate dehydrogenase complex  
    -  Gene name Name=aceF; OrderedLocusNames=b0115;  
    -  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:Acetyl-CoA + enzyme N(6)-(dihydrolipoyl)lysine = CoA + enzyme N(6)-(S-acetyldihydrolipoyl)lysine.
  • COFACTOR:Contains 3 covalently bound lipoyl cofactors.
  • SUBUNIT:Forms a 24-polypeptide structural core with octahedral symmetry.
  • SIMILARITY:Belongs to the 2-oxoacid dehydrogenase family.
  • SIMILARITY:Contains 3 lipoyl-binding domains.  
    •   botton Entry name(Acc.no) Q8X966 ( Q8X966 )
        -  Protein name Pyruvate dehydrogenase  
        -  Synonyms Dihydrolipoyltransacetylase component  
        -  Gene name Name=aceF; OrderedLocusNames=z0125;  
        -  Comments
  • SIMILARITY:Belongs to the 2-oxoacid dehydrogenase family.
  • SIMILARITY:Contains 3 lipoyl-binding domains.  

    •  Linear View (Whole Mode)
    View Location
       115.0  –  140.0 (KBP)

    Homology Analysis
    BLAST
        Bacteria
             GTOP aceF (  homologous genes of other bacterias  )  
        PDB     (database updated : 2007.02.20 )
             PSI-BLAST Chain A, Crystal Structure Of A Cubic Core Of The Dihydrolipoamide Acyltransferase (E2b) Component In The Branched-Chain Alpha-Ketoacid Dehydrogenase Complex (Bckdc), Apo Form  
        SWISS-PROT     (database updated : 2007.02.20 )
             BLAST Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex  
             PSI-BLAST DNA-directed RNA polymerase beta chain
        nr     (database updated : 2007.02.20 )
             BLAST pyruvate dehydrogenase [Escherichia coli UTI89]  
    Pfam 28.0   (database updated : 2015-05 )
        Pfam
    PROSITE
        PROSITE ASN_GLYCOSYLATION    PKC_PHOSPHO_SITE    CK2_PHOSPHO_SITE    MYRISTYL    AMIDATION    ATP_GTP_A    LIPOYL     

    Other Cross-Reference
        COG COG0508C 
        EcoCyc aceF 

    MMBR References
    Eur J Biochem. 1983;133:481-489
    The pyruvate dehydrogenase complex of Escherichia coli K12. Nucleotide sequence encoding the dihydrolipoamide acetyltransferase component.
    Guest, J. R., P. E. Stephens, M. G. Darlison, and H. M. Lewis.
    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 )
    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 MAIEIKVPDI GADEVEITEI LVKVGDKVEA EQSLITVEGD KASMEVPSPQ AGIVKEIKVS VGDKTQTGAL 
0071 IMIFDSADGA ADAAPAQAEE KKEAAPAAAP AAAAAKDVNV PDIGSDEVEV TEILVKVGDK VEAEQSLITV 
0141 EGDKASMEVP APFAGTVKEI KVNVGDKVST GSLIMVFEVA GEAGAAAPAA KQEAAPAAAP APAAGVKEVN 
0211 VPDIGGDEVE VTEVMVKVGD KVAAEQSLIT VEGDKASMEV PAPFAGVVKE LKVNVGDKVK TGSLIMIFEV 
0281 EGAAPAAAPA KQEAAAPAPA AKAEAPAAAP AAKAEGKSEF AENDAYVHAT PLIRRLAREF GVNLAKVKGT 
0351 GRKGRILRED VQAYVKEAIK RAEAAPAATG GGIPGMLPWP KVDFSKFGEI EEVELGRIQK ISGANLSRNW 
0421 VMIPHVTHFD KTDITELEAF RKQQNEEAAK RKLDVKITPV VFIMKAVAAA LEQMPRFNSS LSEDGQRLTL 
0491 KKYINIGVAV DTPNGLVVPV FKDVNKKGII ELSRELMTIS KKARDGKLTA GEMQGGCFTI SSIGGLGTTH 
0561 FAPIVNAPEV AILGVSKSAM EPVWNGKEFV PRLMLPISLS FDHRVIDGAD GARFITIINN TLSDIRRLVM
    Nucleotide
    FASTA format

    View sequence out neighbor 100bp 
    -100                                             GTGGCGAAAT CGATAAGAAA GTGGTTGCTG 
-070 ACGCAATCGC CAAATTCAAC ATCGATGCAG ATAAAGTTAA CCCGCGTCTG GCGTAAGAGG TAAAAGAATA 
0001 atggctatcg aaatcaaagt accggacatc ggggctgatg aagttgaaat caccgagatc ctggtcaaag 
0071 tgggcgacaa agttgaagcc gaacagtcgc tgatcaccgt agaaggcgac aaagcctcta tggaagttcc 
0141 gtctccgcag gcgggtatcg ttaaagagat caaagtctct gttggcgata aaacccagac cggcgcactg 
0211 attatgattt tcgattccgc cgacggtgca gcagacgctg cacctgctca ggcagaagag aagaaagaag 
0281 cagctccggc agcagcacca gcggctgcgg cggcaaaaga cgttaacgtt ccggatatcg gcagcgacga 
0351 agttgaagtg accgaaatcc tggtgaaagt tggcgataaa gttgaagctg aacagtcgct gatcaccgta 
0421 gaaggcgaca aggcttctat ggaagttccg gctccgtttg ctggcaccgt gaaagagatc aaagtgaacg 
0491 tgggtgacaa agtgtctacc ggctcgctga ttatggtctt cgaagtcgcg ggtgaagcag gcgcggcagc 
0561 tccggccgct aaacaggaag cagctccggc agcggcccct gcaccagcgg ctggcgtgaa agaagttaac 
0631 gttccggata tcggcggtga cgaagttgaa gtgactgaag tgatggtgaa agtgggcgac aaagttgccg 
0701 ctgaacagtc actgatcacc gtagaaggcg acaaagcttc tatggaagtt ccggcgccgt ttgcaggcgt 
0771 cgtgaaggaa ctgaaagtca acgttggcga taaagtgaaa actggctcgc tgattatgat cttcgaagtt 
0841 gaaggcgcag cgcctgcggc agctcctgcg aaacaggaag cggcagcgcc ggcaccggca gcaaaagctg 
0911 aagccccggc agcagcacca gctgcgaaag cggaaggcaa atctgaattt gctgaaaacg acgcttatgt 
0981 tcacgcgact ccgctgatcc gccgtctggc acgcgagttt ggtgttaacc ttgcgaaagt gaagggcact 
1051 ggccgtaaag gtcgtatcct gcgcgaagac gttcaggctt acgtgaaaga agctatcaaa cgtgcagaag 
1121 cagctccggc agcgactggc ggtggtatcc ctggcatgct gccgtggccg aaggtggact tcagcaagtt 
1191 tggtgaaatc gaagaagtgg aactgggccg catccagaaa atctctggtg cgaacctgag ccgtaactgg 
1261 gtaatgatcc cgcatgttac tcacttcgac aaaaccgata tcaccgagtt ggaagcgttc cgtaaacagc 
1331 agaacgaaga agcggcgaaa cgtaagctgg atgtgaagat caccccggtt gtcttcatca tgaaagccgt 
1401 tgctgcagct cttgagcaga tgcctcgctt caatagttcg ctgtcggaag acggtcagcg tctgaccctg 
1471 aagaaataca tcaacatcgg tgtggcggtg gataccccga acggtctggt tgttccggta ttcaaagacg 
1541 tcaacaagaa aggcatcatc gagctgtctc gcgagctgat gactatttct aagaaagcgc gtgacggtaa 
1611 gctgactgcg ggcgaaatgc agggcggttg cttcaccatc tccagcatcg gcggcctggg tactacccac 
1681 ttcgcgccga ttgtgaacgc gccggaagtg gctatcctcg gcgtttccaa gtccgcgatg gagccggtgt 
1751 ggaatggtaa agagttcgtg ccgcgtctga tgctgccgat ttctctctcc ttcgaccacc gcgtgatcga 
1821 cggtgctgat ggtgcccgtt tcattaccat cattaacaac acgctgtctg acattcgccg tctggtgatg 
1891 taaGTAAAAG AGCCGGCCCA ACGGCCGGCT TTTTTCTGGT AATCTCATGA ATGTATTGAG GTTATTAGCG 
1961 AATAGACAAA TCGGTTGCCG TTTGTTGTTT AAA