ECOLI:K6PF1

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Species (Taxon ID)	Escherichia coli (strain K12). (taxon:83333)
Gene Name(s)	pfkA
Protein Name(s)	6-phosphofructokinase isozyme 1 6-phosphofructokinase isozyme I Phosphofructokinase 1 Phosphohexokinase 1
External Links
UniProt Identifier	K6PF1_ECOLI
UniProt Accessions	P0A796, P06998, Q2M8L2,
EMBL	X02519, L19201, U00096, AP009048,
PIR	G65197,
RefSeq	AP_003893.1, NP_418351.1,
PDB	1PFK, 2PFK,
IntAct	P0A796,
Pfam	PF00365,

Annotations

Qualifier	GO ID	GO term name	Reference	Evidence Code	with/from	Aspect	Notes	Status
	GO:0005945	6-phosphofructokinase complex		IDA: Inferred from Direct Assay		C	Source: EcoliWiki
	GO:0003872	6-phosphofructokinase activity		IMP: Inferred from Mutant Phenotype		F	Source: EcoliWiki
	GO:0005524	ATP binding		IMP: Inferred from Mutant Phenotype		F	Source: EcoliWiki
	GO:0042802	identical protein binding		IDA: Inferred from Direct Assay		F	Source: EcoliWiki
	GO:0000287	magnesium ion binding		IDA: Inferred from Direct Assay		F	Source: EcoliWiki
	GO:0006002	fructose 6-phosphate metabolic process		IEA: Inferred from Electronic Annotation		P	Source: InterPro
	GO:0006096	glycolysis		IDA: Inferred from Direct Assay		P	Source: EcoliWiki
	GO:0003872	6-phosphofructokinase activity	PMID:4275310^[1]	IMP: Inferred from Mutant Phenotype		F	Table 3. A mutant strain of E. coli that does not contain pfkA is for all practical reasons unable to grow on glucose, while a strain containing pfkA is able to.	complete
	GO:0006096	glycolysis	PMID:4275310^[1]	IMP: Inferred from Mutant Phenotype		P	Table 3. A mutant strain of E. coli that does not contain pfkA is for all practical reasons unable to grow on glucose, while a strain containing pfkA is able to.	complete
	GO:0003872	6-phosphofructokinase activity	PMID:368027^[2]	IMP: Inferred from Mutant Phenotype		F	Table 2. A mutant strain that does not contain pfkA has a significantly lower phosphofructokinase activity than the wild type.	complete
	GO:0000166	nucleotide binding	GO_REF:0000004	IEA: Inferred from Electronic Annotation	SP_KW:KW-0547	F
	GO:0000287	magnesium ion binding	PMID:1445885^[3]	IDA: Inferred from Direct Assay		F
	GO:0003824	catalytic activity	GO_REF:0000004	IEA: Inferred from Electronic Annotation	SP_KW:KW-0021	F
	GO:0003872	6-phosphofructokinase activity	GO_REF:0000002	IEA: Inferred from Electronic Annotation	InterPro:IPR000023	F
	GO:0003872	6-phosphofructokinase activity	GO_REF:0000002	IEA: Inferred from Electronic Annotation	InterPro:IPR012828	F
	GO:0003872	6-phosphofructokinase activity	GO_REF:0000002	IEA: Inferred from Electronic Annotation	InterPro:IPR015912	F
	GO:0003872	6-phosphofructokinase activity	GO_REF:0000003	IEA: Inferred from Electronic Annotation	EC:2.7.1.11	F
	GO:0003872	6-phosphofructokinase activity	PMID:125265^[4]	IMP: Inferred from Mutant Phenotype		F
	GO:0003872	6-phosphofructokinase activity	PMID:4229913^[5]	IDA: Inferred from Direct Assay		F
	GO:0005488	binding	PMID:17307338^[6]	IDA: Inferred from Direct Assay		F
	GO:0005515	protein binding	PMID:15690043^[7]	IPI: Inferred from Physical Interaction	UniProtKB:P0A7I4	F
	GO:0005515	protein binding	PMID:15690043^[7]	IPI: Inferred from Physical Interaction	UniProtKB:P12281	F
	GO:0005515	protein binding	PMID:15690043^[7]	IPI: Inferred from Physical Interaction	UniProtKB:P37440	F
	GO:0005524	ATP binding	GO_REF:0000002	IEA: Inferred from Electronic Annotation	InterPro:IPR012003	F
	GO:0005524	ATP binding	GO_REF:0000002	IEA: Inferred from Electronic Annotation	InterPro:IPR012828	F
	GO:0005524	ATP binding	GO_REF:0000004	IEA: Inferred from Electronic Annotation	SP_KW:KW-0067	F
	GO:0005524	ATP binding	PMID:8202475^[8]	IMP: Inferred from Mutant Phenotype		F
	GO:0005737	cytoplasm	GO_REF:0000004	IEA: Inferred from Electronic Annotation	SP_KW:KW-0963	C
	GO:0005737	cytoplasm	GO_REF:0000023	IEA: Inferred from Electronic Annotation	SP_SL:SL-0086	C
	GO:0005737	cytoplasm	PMID:4229913^[5]	IDA: Inferred from Direct Assay		C
	GO:0005945	6-phosphofructokinase complex	GO_REF:0000002	IEA: Inferred from Electronic Annotation	InterPro:IPR000023	C
	GO:0005945	6-phosphofructokinase complex	GO_REF:0000002	IEA: Inferred from Electronic Annotation	InterPro:IPR015912	C
	GO:0005945	6-phosphofructokinase complex	PMID:6232272^[9]	IDA: Inferred from Direct Assay		C
	GO:0006002	fructose 6-phosphate metabolic process	GO_REF:0000002	IEA: Inferred from Electronic Annotation	InterPro:IPR012003	P
	GO:0006002	fructose 6-phosphate metabolic process	GO_REF:0000002	IEA: Inferred from Electronic Annotation	InterPro:IPR012828	P
	GO:0006007	glucose catabolic process	PMID:4299078^[10]	IMP: Inferred from Mutant Phenotype		P
	GO:0006096	glycolysis	GO_REF:0000002	IEA: Inferred from Electronic Annotation	InterPro:IPR000023	P
	GO:0006096	glycolysis	GO_REF:0000002	IEA: Inferred from Electronic Annotation	InterPro:IPR012003	P
	GO:0006096	glycolysis	GO_REF:0000002	IEA: Inferred from Electronic Annotation	InterPro:IPR012828	P
	GO:0006096	glycolysis	GO_REF:0000002	IEA: Inferred from Electronic Annotation	InterPro:IPR015912	P
	GO:0006096	glycolysis	GO_REF:0000004	IEA: Inferred from Electronic Annotation	SP_KW:KW-0324	P
	GO:0006096	glycolysis	PMID:15237399^[11]	IDA: Inferred from Direct Assay		P
	GO:0006096	glycolysis	PMID:177406^[12]	IMP: Inferred from Mutant Phenotype		P
	GO:0008152	metabolic process	GO_REF:0000004	IEA: Inferred from Electronic Annotation	SP_KW:KW-0021	P
	GO:0008443	phosphofructokinase activity	GO_REF:0000002	IEA: Inferred from Electronic Annotation	InterPro:IPR012003	F
	GO:0016301	kinase activity	GO_REF:0000004	IEA: Inferred from Electronic Annotation	SP_KW:KW-0418	F
	GO:0016310	phosphorylation	GO_REF:0000004	IEA: Inferred from Electronic Annotation	SP_KW:KW-0418	P
	GO:0016740	transferase activity	GO_REF:0000004	IEA: Inferred from Electronic Annotation	SP_KW:KW-0808	F
	GO:0019003	GDP binding	PMID:70226^[13]	IDA: Inferred from Direct Assay		F
	GO:0032553	ribonucleotide binding	PMID:4229913^[5]	IDA: Inferred from Direct Assay		F
	GO:0042802	identical protein binding	PMID:11946283^[14]	IDA: Inferred from Direct Assay		F
	GO:0046872	metal ion binding	GO_REF:0000004	IEA: Inferred from Electronic Annotation	SP_KW:KW-0479	F
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Notes

References

See Help:References for how to manage references in GONUTS.

↑ ^1.0 ^1.1 Vinopal RT & Fraenkel DG (1974) Phenotypic suppression of phosphofructokinase mutations in Escherichia coli by constitutive expression of the glyoxylate shunt. J Bacteriol 118: 1090-100 PubMed GONUTS page
↑ Thomson J et al. (1979) ColE1 hybrid plasmids for Escherichia coli genes of glycolysis and the hexose monophosphate shunt. J Bacteriol 137: 502-6 PubMed GONUTS page
↑ Johnson JL & Reinhart GD (1992) MgATP and fructose 6-phosphate interactions with phosphofructokinase from Escherichia coli. Biochemistry 31: 11510-8 PubMed GONUTS page
↑ Vinopal RT et al. (1975) PfkA locus of Escherichia coli. J Bacteriol 122: 1162-71 PubMed GONUTS page
↑ ^5.0 ^5.1 ^5.2 Blangy D et al. (1968) Kinetics of the allosteric interactions of phosphofructokinase from Escherichia coli. J Mol Biol 31: 13-35 PubMed GONUTS page
↑ Ogawa T et al. (2007) Inhibitory effect of phosphoenolpyruvate on glycolytic enzymes in Escherichia coli. Res Microbiol 158: 159-63 PubMed GONUTS page
↑ ^7.0 ^7.1 ^7.2 Butland G et al. (2005) Interaction network containing conserved and essential protein complexes in Escherichia coli. Nature 433: 531-7 PubMed GONUTS page
↑ Auzat I et al. (1994) The cooperativity and allosteric inhibition of Escherichia coli phosphofructokinase depend on the interaction between threonine-125 and ATP. Proc Natl Acad Sci U S A 91: 5242-6 PubMed GONUTS page
↑ Martel A & Garel JR (1984) Renaturation of the allosteric phosphofructokinase from Escherichia coli. J Biol Chem 259: 4917-21 PubMed GONUTS page
↑ Morrissey AT & Fraenkel DG (1968) Selection of fructose 6-phosphate kinase mutants in Escherichia coli. Biochem Biophys Res Commun 32: 467-73 PubMed GONUTS page
↑ Itoh A et al. (2004) Application of capillary electrophoresis-mass spectrometry to synthetic in vitro glycolysis studies. Electrophoresis 25: 1996-2002 PubMed GONUTS page
↑ Roehl RA & Vinopal RT (1976) Lack of glucose phosphotransferase function in phosphofructokinase mutants of Escherichia coli. J Bacteriol 126: 852-60 PubMed GONUTS page
↑ Kotlarz D & Buc H (1977) Two Escherichia coli fructose-6-phosphate kinases. Preparative purification, oligomeric structure and immunological studies. Biochim Biophys Acta 484: 35-48 PubMed GONUTS page
↑ Blangy D (1968) Phosphofructokinase from E. Coli: Evidence for a tetrameric structure of the enzyme. FEBS Lett 2: 109-111 PubMed GONUTS page

[PMID:4275310-0] 1.0 ^1.1 Vinopal RT & Fraenkel DG (1974) Phenotypic suppression of phosphofructokinase mutations in Escherichia coli by constitutive expression of the glyoxylate shunt. J Bacteriol 118: 1090-100 PubMed GONUTS page

[PMID:368027-1] Thomson J et al. (1979) ColE1 hybrid plasmids for Escherichia coli genes of glycolysis and the hexose monophosphate shunt. J Bacteriol 137: 502-6 PubMed GONUTS page

[PMID:1445885-2] Johnson JL & Reinhart GD (1992) MgATP and fructose 6-phosphate interactions with phosphofructokinase from Escherichia coli. Biochemistry 31: 11510-8 PubMed GONUTS page

[PMID:125265-3] Vinopal RT et al. (1975) PfkA locus of Escherichia coli. J Bacteriol 122: 1162-71 PubMed GONUTS page

[PMID:4229913-4] 5.0 ^5.1 ^5.2 Blangy D et al. (1968) Kinetics of the allosteric interactions of phosphofructokinase from Escherichia coli. J Mol Biol 31: 13-35 PubMed GONUTS page

[PMID:17307338-5] Ogawa T et al. (2007) Inhibitory effect of phosphoenolpyruvate on glycolytic enzymes in Escherichia coli. Res Microbiol 158: 159-63 PubMed GONUTS page

[PMID:15690043-6] 7.0 ^7.1 ^7.2 Butland G et al. (2005) Interaction network containing conserved and essential protein complexes in Escherichia coli. Nature 433: 531-7 PubMed GONUTS page

[PMID:8202475-7] Auzat I et al. (1994) The cooperativity and allosteric inhibition of Escherichia coli phosphofructokinase depend on the interaction between threonine-125 and ATP. Proc Natl Acad Sci U S A 91: 5242-6 PubMed GONUTS page

[PMID:6232272-8] Martel A & Garel JR (1984) Renaturation of the allosteric phosphofructokinase from Escherichia coli. J Biol Chem 259: 4917-21 PubMed GONUTS page

[PMID:4299078-9] Morrissey AT & Fraenkel DG (1968) Selection of fructose 6-phosphate kinase mutants in Escherichia coli. Biochem Biophys Res Commun 32: 467-73 PubMed GONUTS page

[PMID:15237399-10] Itoh A et al. (2004) Application of capillary electrophoresis-mass spectrometry to synthetic in vitro glycolysis studies. Electrophoresis 25: 1996-2002 PubMed GONUTS page

[PMID:177406-11] Roehl RA & Vinopal RT (1976) Lack of glucose phosphotransferase function in phosphofructokinase mutants of Escherichia coli. J Bacteriol 126: 852-60 PubMed GONUTS page

[PMID:70226-12] Kotlarz D & Buc H (1977) Two Escherichia coli fructose-6-phosphate kinases. Preparative purification, oligomeric structure and immunological studies. Biochim Biophys Acta 484: 35-48 PubMed GONUTS page

[PMID:11946283-13] Blangy D (1968) Phosphofructokinase from E. Coli: Evidence for a tetrameric structure of the enzyme. FEBS Lett 2: 109-111 PubMed GONUTS page

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ECOLI:K6PF1

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