RegulonDB RegulonDB 11.1: Gene Form
   

pck gene in Escherichia coli K-12 genome


Gene local context to scale (view description)

yhgE pck envZ ompR CRP DcuR DcuR CRP Cra terminator anti-terminator TSS_4000 TSS_4000 TSS_3999 (cluster) TSS_3999 (cluster) pckp pckp yhgEp6 yhgEp6 yhgEp9 yhgEp9 yhgEp7 yhgEp7

Gene      
Name: pck    Texpresso search in the literature
Synonym(s): ECK3390, EG10688, b3403, pckA
Genome position(nucleotides): 3532818 --> 3534440
Strand: forward
Sequence: Get nucleotide sequence FastaFormat
GC content %:  
 53.6
External database links:  
ASAP:
 ABE-0011106
CGSC:
 422
ECHOBASE:
 EB0682
ECOLIHUB:
 pck
ECOO157CYC:
 PCKA
OU-MICROARRAY:
 b3403
STRING:
 511145.b3403
COLOMBOS: pck


Product      
Name: phosphoenolpyruvate carboxykinase (ATP)
Synonym(s): Pck, PckA
Sequence: Get amino acid sequence Fasta Format
Cellular location: cytosol
Molecular weight: 59.643
Isoelectric point: 5.397
Motif(s):
 
Type Positions Sequence Comment
22 -> 491 DIVYNPSYDLLYQEELDPSLTGYERGVLTNLGAVAVDTGIFTGRSPKDKYIVRDDTTRDTFWWADKGKGKNDNKPLSPETWQHLKGLVTRQLSGKRLFVVDAFCGANPDTRLSVRFITEVAWQAHFVKNMFIRPSDEELAGFKPDFIVMNGAKCTNPQWKEQGLNSENFVAFNLTERMQLIGGTWYGGEMKKGMFSMMNYLLPLKGIASMHCSANVGEKGDVAVFFGLSGTGKTTLSTDPKRRLIGDDEHGWDDDGVFNFEGGCYAKTIKLSKEAEPEIYNAIRRDALLENVTVREDGTIDFDDGSKTENTRVSYPIYHIDNIVKPVSKAGHATKVIFLTADAFGVLPPVSRLTADQTQYHFLSGFTAKLAGTERGITEPTPTFSACFGAAFLSLHPTQYAEVLVKRMQAAGAQAYLVNTGWNGTGKRISIKDTRAIIDAILNGSLDNAETFTLPMFNLAIPTELPGVDT
65 -> 65 R UniProt: Slightly lower catalytic efficiency compared to wild-type and the affinity binding for OAA is 330-fold higher than for wild-type..
67 -> 72 PKDKYI UniProt: In Ref. 1; AAA24301..
192 -> 194 AFN UniProt: In Ref. 1; AA sequence..
197 -> 203 ERMQLIG UniProt: In Ref. 1; AA sequence..

 
Classification:
Multifun Terms (GenProtEC)  
  1 - metabolism --> 1.7 - central intermediary metabolism
Gene Ontology Terms (GO)  
cellular_component GO:0005737 - cytoplasm
GO:0005829 - cytosol
molecular_function GO:0003824 - catalytic activity
GO:0016829 - lyase activity
GO:0046872 - metal ion binding
GO:0016831 - carboxy-lyase activity
GO:0000166 - nucleotide binding
GO:0005524 - ATP binding
GO:0017076 - purine nucleotide binding
GO:0004611 - phosphoenolpyruvate carboxykinase activity
GO:0004612 - phosphoenolpyruvate carboxykinase (ATP) activity
GO:0000287 - magnesium ion binding
GO:0005509 - calcium ion binding
biological_process GO:0008152 - metabolic process
GO:0006094 - gluconeogenesis
Note(s): Note(s): ...[more].
Reference(s): [1] Bazaes S., et al., 1995
[2] Bazaes S., et al., 1997
[3] Bazaes S., et al., 1993
[4] Bustos P., et al., 1996
[5] Encinas MV., et al., 1998
[6] Encinas MV., et al., 2002
[7] Encinas MV., et al., 1995
[8] Goldie AH., et al., 1981
[9] Hou SY., et al., 1995
[10] Lee B., et al., 1999
[11] Medina V., et al., 1990
[12] Tari LW., et al., 1997
External database links:  
ALPHAFOLD:
 P22259
ECOCYC:
 PEPCARBOXYKIN-MONOMER
ECOLIWIKI:
 b3403
INTERPRO:
 IPR001272
INTERPRO:
 IPR013035
INTERPRO:
 IPR015994
INTERPRO:
 IPR008210
MODBASE:
 P22259
PANTHER:
 PTHR30031
PDB:
 6ASI
PDB:
 6ASM
PDB:
 6ASN
PDB:
 6AT2
PDB:
 6AT3
PDB:
 6AT4
PDB:
 6COM
PDB:
 6CRT
PDB:
 6V2L
PDB:
 6V2M
PDB:
 6V2N
PDB:
 2PY7
PDB:
 2PXZ
PDB:
 2OLR
PDB:
 2OLQ
PDB:
 1OS1
PDB:
 1OEN
PDB:
 1K3D
PDB:
 1K3C
PDB:
 1AQ2
PDB:
 1AYL
PFAM:
 PF01293
PRIDE:
 P22259
PRODB:
 PRO_000023498
PROSITE:
 PS00532
REFSEQ:
 NP_417862
SMR:
 P22259
UNIPROT:
 P22259


Operon      
Name: pck         
Operon arrangement:
Transcription unit        Promoter
pck


Transcriptional Regulation      
Display Regulation             
Activated by: CRP, Cra, DcuR
Repressed by: CRP


RNA cis-regulatory element    
Attenuation: Transcriptional


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 yhgEp7 3532485 reverse nd [COMP-AINF] [13]
  promoter yhgEp9 3532538 reverse nd [COMP-AINF] [13]
  promoter yhgEp6 3532588 reverse nd [COMP-AINF] [13]
  promoter TSS_3999 (cluster) 3532790 forward nd [RS-EPT-CBR] [14]
  promoter TSS_4000 3532798 forward nd [RS-EPT-CBR] [14]


Evidence    

 [COMP-AINF] Inferred computationally without human oversight

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


Reference(s)    

 [1] Bazaes S., Goldie H., Cardemil E., Jabalquinto AM., 1995, Identification of reactive lysines in phosphoenolpyruvate carboxykinases from Escherichia coli and Saccharomyces cerevisiae., FEBS Lett 360(2):207-10

 [2] Bazaes S., Montecinos L., Krautwurst H., Goldie H., Cardemil E., Jabalquinto AM., 1997, Identification of reactive conserved histidines in phosphoenolpyruvate carboxykinases from Escherichia coli and Saccharomyces cerevisiae., Biochim Biophys Acta 1337(2):166-74

 [3] Bazaes S., Silva R., Goldie H., Cardemil E., Jabalquinto AM., 1993, Reactivity of cysteinyl, arginyl, and lysyl residues of Escherichia coli phosphoenolpyruvate carboxykinase against group-specific chemical reagents., J Protein Chem 12(5):571-7

 [4] Bustos P., Gajardo MI., Gomez C., Goldie H., Cardemil E., Jabalquinto AM., 1996, Woodward's reagent K reacts with histidine and cysteine residues in Escherichia coli and Saccharomyces cerevisiae phosphoenolpyruvate carboxykinases., J Protein Chem 15(5):467-72

 [5] Encinas MV., Evangelio JA., Andreu JM., Goldie H., Cardemil E., 1998, Stability of Escherichia coli phosphoenolpyruvate carboxykinase against urea-induced unfolding and ligand effects., Eur J Biochem 255(2):439-45

 [6] Encinas MV., Gonzalez-Nilo FD., Goldie H., Cardemil E., 2002, Ligand interactions and protein conformational changes of phosphopyridoxyl-labeled Escherichia coli phosphoenolpyruvate carboxykinase determined by fluorescence spectroscopy., Eur J Biochem 269(20):4960-8

 [7] Encinas MV., Olsen LR., Diaz JF., Andreu JM., Goldie H., Cardemil E., 1995, Circular dichroism and Fourier transform infrared spectroscopic studies on the secondary structure of Saccharomyces cerevisiae and Escherichia coli phospho enolpyruvate carboxykinases., Biochim Biophys Acta 1252(1):23-7

 [8] Goldie AH., Sanwal BD., 1981, Temperature-sensitive mutation affecting synthesis of phosphoenolpyruvate carboxykinase in Escherichia coli., J Bacteriol 148(2):720-3

 [9] Hou SY., Chao YP., Liao JC., 1995, A mutant phosphoenolpyruvate carboxykinase in Escherichia coli conferring oxaloacetate decarboxylase activity., J Bacteriol 177(6):1620-3

 [10] Lee B., Yen J., Yang L., Liao JC., 1999, Incorporating qualitative knowledge in enzyme kinetic models using fuzzy logic., Biotechnol Bioeng 62(6):722-9

 [11] Medina V., Pontarollo R., Glaeske D., Tabel H., Goldie H., 1990, Sequence of the pckA gene of Escherichia coli K-12: relevance to genetic and allosteric regulation and homology of E. coli phosphoenolpyruvate carboxykinase with the enzymes from Trypanosoma brucei and Saccharomyces cerevisiae., J Bacteriol 172(12):7151-6

 [12] Tari LW., Matte A., Goldie H., Delbaere LT., 1997, Mg(2+)-Mn2+ clusters in enzyme-catalyzed phosphoryl-transfer reactions., Nat Struct Biol 4(12):990-4

 [13] Huerta AM., Collado-Vides J., 2003, Sigma70 promoters in Escherichia coli: specific transcription in dense regions of overlapping promoter-like signals., J Mol Biol 333(2):261-78

 [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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