RegulonDB RegulonDB 10.9: Gene Form
   

aceF gene in Escherichia coli K-12 genome


Gene local context to scale (view description)

aceE aceF lpd ArcA CRP ArcA Fis TSS_253 TSS_253 TSS_252 TSS_252 TSS_251 TSS_251 TSS_250 TSS_250 TSS_249 TSS_249 TSS_248 TSS_248 lpdAp lpdAp TSS_247 TSS_247 TSS_246 TSS_246 TSS_245 TSS_245 TSS_244 TSS_244 TSS_243 TSS_243 TSS_242 (cluster) TSS_242 (cluster) TSS_241 TSS_241

Gene      
Name: aceF    Texpresso search in the literature
Synonym(s): ECK0114, EG10025, b0115
Genome position(nucleotides): 125695 --> 127587 Genome Browser
Strand: forward
Sequence: Get nucleotide sequence FastaFormat
GC content %:  
54.68
External database links:  
ASAP:
ABE-0000400
CGSC:
26530
ECHOBASE:
EB0024
ECOLIHUB:
aceF
MIM:
248600
OU-MICROARRAY:
b0115
STRING:
511145.b0115
COLOMBOS: aceF


Product      
Name: pyruvate dehydrogenase, E2 subunit
Synonym(s): AceF, dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex
Sequence: Get amino acid sequence Fasta Format
Cellular location: cytosol
Molecular weight: 66.096
Isoelectric point: 4.813
Motif(s):
 
Type Positions Sequence
206 -> 279 VKEVNVPDIGGDEVEVTEVMVKVGDKVAAEQSLITVEGDKASMEVPAPFAGVVKELKVNVGDKVKTGSLIMIFE
105 -> 178 AKDVNVPDIGSDEVEVTEILVKVGDKVEAEQSLITVEGDKASMEVPAPFAGTVKEIKVNVGDKVSTGSLIMVFE
207 -> 277 KEVNVPDIGGDEVEVTEVMVKVGDKVAAEQSLITVEGDKASMEVPAPFAGVVKELKVNVGDKVKTGSLIMI
327 -> 362 VHATPLIRRLAREFGVNLAKVKGTGRKGRILREDVQ
2 -> 75 AIEIKVPDIGADEVEITEILVKVGDKVEAEQSLITVEGDKASMEVPSPQAGIVKEIKVSVGDKTQTGALIMIFD

 

Classification:
Multifun Terms (GenProtEC)  
  1 - metabolism --> 1.1 - carbon utilization --> 1.1.1 - carbon compounds
  1 - metabolism --> 1.3 - energy metabolism, carbon --> 1.3.3 - pyruvate dehydrogenase
  1 - metabolism --> 1.7 - central intermediary metabolism --> 1.7.21 - glyoxylate degradation
Gene Ontology Terms (GO)  
cellular_component GO:0005737 - cytoplasm
GO:0045254 - pyruvate dehydrogenase complex
molecular_function GO:0005515 - protein binding
GO:0016740 - transferase activity
GO:0016407 - acetyltransferase activity
GO:0016746 - transferase activity, transferring acyl groups
GO:0004742 - dihydrolipoyllysine-residue acetyltransferase activity
GO:0030523 - dihydrolipoamide S-acyltransferase activity
GO:0031405 - lipoic acid binding
biological_process GO:0006086 - acetyl-CoA biosynthetic process from pyruvate
GO:0006090 - pyruvate metabolic process
GO:0006096 - glycolytic process
GO:0055114 - oxidation-reduction process
Note(s): Note(s): ...[more].
Reference(s): [1] Adamson SR., et al., 1986
[2] Akiyama SK., et al., 1980
[3] CaJacob CA., et al., 1985
[4] Danson MJ., et al., 1981
[5] Guest JR., et al., 1985
[6] Guest JR., et al., 1983
[7] Hackert ML., et al., 1983
[8] Harrison JP., et al., 1990
[9] Langley D., et al., 1977
[10] Miles JS., et al., 1987
[11] Nemeria N., et al., 2002
[12] Wei W., et al., 2003
[13] Yang YS., et al., 1986
External database links:  
DIP:
DIP-9040N
ECOCYC:
E2P-MONOMER
ECOLIWIKI:
b0115
INTERPRO:
IPR023213
INTERPRO:
IPR036625
INTERPRO:
IPR006256
INTERPRO:
IPR011053
INTERPRO:
IPR000089
INTERPRO:
IPR001078
INTERPRO:
IPR003016
INTERPRO:
IPR004167
MODBASE:
P06959
PANTHER:
PTHR43178:SF2
PDB:
2K7V
PDB:
1QJO
PFAM:
PF00198
PFAM:
PF02817
PFAM:
PF00364
PRIDE:
P06959
PRODB:
PRO_000022039
PROSITE:
PS51826
PROSITE:
PS00189
PROSITE:
PS50968
REFSEQ:
NP_414657
SMR:
P06959
SWISSMODEL:
P06959
UNIPROT:
P06959


Operon      
Name: pdhR-aceEF-lpd         
Operon arrangement:
Transcription unit        Promoter
pdhR-aceEF-lpdA
pdhR-aceEF-lpdA
aceEF
aceEF
lpdA


Transcriptional Regulation      
Display Regulation             
Activated by: CRP, FNR
Repressed by: NsrR, FNR, Cra, ArcA, PdhR, BtsR
Growth Conditions:

[1] 

C: Escherichia coli| multicopy plasmid pGS623 (pdhR-lpd) mutant| L broth| OD650 of 0.2
E: Escherichia coli| multicopy plasmid pGS623 (pdhR-lpd) mutant| L broth| glucose 10 mM| OD650 of 0.2

[2] 

C: Escherichia coli| multicopy plasmid pGS623 (pdhR-lpd) mutant| L broth| OD650 of 0.2
E: Escherichia coli| multicopy plasmid pGS623 (pdhR-lpd) mutant| L broth| pyruvate 40 mM| OD650 of 0.2



Elements in the selected gene context region unrelated to any object in RegulonDB      

  Type Name Post Left Post Right Strand Notes Evidence (Confirmed, Strong, Weak) References
  promoter TSS_241 123388 forward nd [RS-EPT-CBR] [14]
  promoter TSS_242 (cluster) 123471 forward For this promoter, there
Read more >
[RS-EPT-CBR] [14]
  promoter TSS_243 124973 forward nd [RS-EPT-CBR] [14]
  promoter TSS_244 125226 forward nd [RS-EPT-CBR] [14]
  promoter TSS_245 125425 forward nd [RS-EPT-CBR] [14]
  promoter TSS_246 127432 forward nd [RS-EPT-CBR] [14]
  promoter TSS_247 127436 forward nd [RS-EPT-CBR] [14]
  promoter TSS_248 127896 forward nd [RS-EPT-CBR] [14]
  promoter TSS_249 127898 forward nd [RS-EPT-CBR] [14]
  promoter TSS_250 127900 forward nd [RS-EPT-CBR] [14]
  promoter TSS_251 127907 forward nd [RS-EPT-CBR] [14]
  promoter TSS_252 127929 forward nd [RS-EPT-CBR] [14]
  promoter TSS_253 127953 forward nd [RS-EPT-CBR] [14]


Evidence    

 [RS-EPT-CBR] RNA-seq using two enrichment strategies for primary transcripts and consistent biological replicates



Reference(s)    

 [1] Adamson SR., Holmes CF., Stevenson KJ., 1986, Acetylatable lipoic acid residues interact directly with lipoamide dehydrogenase in the pyruvate dehydrogenase multienzyme complex of Escherichia coli., Biochem Cell Biol 64(3):250-5

 [2] Akiyama SK., Hammes GG., 1980, Elementary steps in the reaction mechanism of the pyruvate dehydrogenase multienzyme complex from Escherichia coli: kinetics of acetylation and deacetylation., Biochemistry 19(18):4208-13

 [3] CaJacob CA., Gavino GR., Frey PA., 1985, Pyruvate dehydrogenase complex of Escherichia coli. Thiamin pyrophosphate and NADH-dependent hydrolysis of acetyl-CoA., J Biol Chem 260(27):14610-15

 [4] Danson MJ., Hale G., Perham RN., 1981, The role of lipoic acid residues in the pyruvate dehydrogenase multienzyme complex of Escherichia coli., Biochem J 199(3):505-11

 [5] Guest JR., Lewis HM., Graham LD., Packman LC., Perham RN., 1985, Genetic reconstruction and functional analysis of the repeating lipoyl domains in the pyruvate dehydrogenase multienzyme complex of Escherichia coli., J Mol Biol 185(4):743-54

 [6] Guest JR., Roberts RE., Stephens PE., 1983, Hybrid plasmids containing the pyruvate dehydrogenase complex genes and gene-DNA relationships in the 2 to 3 minute region of the Escherichia coli chromosome., J Gen Microbiol 129 (Pt 3):671-80

 [7] Hackert ML., Oliver RM., Reed LJ., 1983, A computer model analysis of the active-site coupling mechanism in the pyruvate dehydrogenase multienzyme complex of Escherichia coli., Proc Natl Acad Sci U S A 80(10):2907-11

 [8] Harrison JP., Morrison IE., Cherry RJ., 1990, Rotational diffusion studies of the lipoyl domain of 2-oxoacid dehydrogenase multienzyme complexes., Biochemistry 29(23):5596-604

 [9] Langley D., Guest JR., 1977, Biochemical genetics of the alpha-keto acid dehydrogenase complexes of Escherichia coli K12: isolation and biochemical properties of deletion mutants., J Gen Microbiol 99(2):263-76

 [10] Miles JS., Guest JR., Radford SE., Perham RN., 1987, A mutant pyruvate dehydrogenase complex of Escherichia coli deleted in the (alanine + proline)-rich region of the acetyltransferase component., Biochim Biophys Acta 913(2):117-21

 [11] Nemeria N., Arjunan P., Brunskill A., Sheibani F., Wei W., Yan Y., Zhang S., Jordan F., Furey W., 2002, Histidine 407, a phantom residue in the E1 subunit of the Escherichia coli pyruvate dehydrogenase complex, activates reductive acetylation of lipoamide on the E2 subunit. An explanation for conservation of active sites between the E1 subunit and transketolase., Biochemistry 41(52):15459-67

 [12] Wei W., Li H., Nemeria N., Jordan F., 2003, Expression and purification of the dihydrolipoamide acetyltransferase and dihydrolipoamide dehydrogenase subunits of the Escherichia coli pyruvate dehydrogenase multienzyme complex: a mass spectrometric assay for reductive acetylation of dihydrolipoamide acetyltransferase., Protein Expr Purif 28(1):140-50

 [13] Yang YS., Frey PA., 1986, Dihydrolipoyl transacetylase of Escherichia coli. Formation of 8-S-acetyldihydrolipoamide., Biochemistry 25(25):8173-8

 [14] Salgado H, Peralta-Gil M, Gama-Castro S, Santos-Zavaleta A, Muñiz-Rascado L, García-Sotelo JS, Weiss V, Solano-Lira H, Martínez-Flores I, Medina-Rivera A, Salgado-Osorio G, Alquicira-Hernández S, Alquicira-Hernández K, López-Fuentes A, Porrón-Sotelo L, Huerta AM, Bonavides-Martínez C, Balderas-Martínez YI, Pannier L, Olvera M, Labastida A, Jiménez-Jacinto V, Vega-Alvarado L, Del Moral-Chávez V, Hernández-Alvarez A, Morett E, Collado-Vides J., 2012, RegulonDB v8.0: omics data sets, evolutionary conservation, regulatory phrases, cross-validated gold standards and more., Nucleic Acids Res.


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