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ECOLI:K6PF1

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Species (Taxon ID) Escherichia coli (strain K12). (83333)
Gene Name(s) pfkA
Protein Name(s) 6-phosphofructokinase isozyme 1

6-phosphofructokinase isozyme I Phosphofructokinase 1 Phosphohexokinase 1

External Links
UniProt P0A796
EMBL X02519
L19201
U00096
AP009048
PIR G65197
RefSeq NP_418351.1
YP_491535.1
PDB 1PFK
2PFK
PDBsum 1PFK
2PFK
ProteinModelPortal P0A796
SMR P0A796
DIP DIP-35841N
IntAct P0A796
MINT MINT-1322275
STRING 511145.b3916
SWISS-2DPAGE P0A796
PaxDb P0A796
PRIDE P0A796
EnsemblBacteria AAC76898
BAE77394
GeneID 12932230
948412
KEGG ecj:Y75_p3271
eco:b3916
PATRIC 32123343
EchoBASE EB0693
EcoGene EG10699
eggNOG COG0205
HOGENOM HOG000248870
KO K00850
OMA GFGGRCV
OrthoDB EOG644ZRM
PhylomeDB P0A796
BioCyc EcoCyc:6PFK-1-MONOMER
ECOL316407:JW3887-MONOMER
MetaCyc:6PFK-1-MONOMER
SABIO-RK P0A796
UniPathway UPA00109
EvolutionaryTrace P0A796
PRO PR:P0A796
Genevestigator P0A796
GO GO:0005945
GO:0005737
GO:0003872
GO:0005524
GO:0019003
GO:0042802
GO:0000287
GO:0032553
GO:0046835
GO:0044275
GO:0006002
GO:0006007
GO:0006096
HAMAP MF_00339
InterPro IPR012003
IPR012828
IPR022953
IPR015912
IPR000023
Pfam PF00365
PIRSF PIRSF000532
PRINTS PR00476
SUPFAM SSF53784
TIGRFAMs TIGR02482
PROSITE PS00433

Annotations

Qualifier GO ID GO term name Reference ECO ID ECO term name with/from Aspect Extension Notes Status
GO:0003872

6-phosphofructokinase activity

PMID:4275310[1]

ECO:0000315

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]

ECO:0000315

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]

ECO:0000315

F

Table 2. A mutant strain that does not contain pfkA has a significantly lower phosphofructokinase activity than the wild type.

complete

enables

GO:0070095

fructose-6-phosphate binding

PMID:21873635[3]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

PANTHER:PTN000344216
PomBase:SPBC16H5.02
RGD:3311
RGD:61893
RGD:68419
UniProtKB:P17858

F

Seeded From UniProt

complete

involved_in

GO:0061621

canonical glycolysis

PMID:21873635[3]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

MGI:MGI:97548
PANTHER:PTN000344216

P

Seeded From UniProt

complete

involved_in

GO:0051289

protein homotetramerization

PMID:21873635[3]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

EcoGene:EG10699
PANTHER:PTN000344216
RGD:3311
RGD:61893
RGD:68419

P

Seeded From UniProt

complete

enables

GO:0048029

monosaccharide binding

PMID:21873635[3]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

PANTHER:PTN000344216
RGD:3311

F

Seeded From UniProt

complete

enables

GO:0042802

identical protein binding

PMID:21873635[3]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

EcoGene:EG10699
MGI:MGI:97548
PANTHER:PTN000344216
UniProtKB:P08237
UniProtKB:P17858
UniProtKB:Q01813

F

Seeded From UniProt

complete

involved_in

GO:0030388

fructose 1,6-bisphosphate metabolic process

PMID:21873635[3]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

PANTHER:PTN000344216
PomBase:SPBC16H5.02
RGD:3311
RGD:61893
RGD:68419
UniProtKB:P17858

P

Seeded From UniProt

complete

enables

GO:0016208

AMP binding

PMID:21873635[3]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

PANTHER:PTN000344216
RGD:68419

F

Seeded From UniProt

complete

involved_in

GO:0006007

glucose catabolic process

PMID:21873635[3]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

EcoGene:EG10699
PANTHER:PTN000344216
dictyBase:DDB_G0274111

P

Seeded From UniProt

complete

involved_in

GO:0006002

fructose 6-phosphate metabolic process

PMID:21873635[3]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

MGI:MGI:97547
PANTHER:PTN000344216
PomBase:SPBC16H5.02
RGD:3311
RGD:61893
RGD:68419
UniProtKB:P08237
UniProtKB:P17858
dictyBase:DDB_G0274111

P

Seeded From UniProt

complete

part_of

GO:0005945

6-phosphofructokinase complex

PMID:21873635[3]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

EcoGene:EG10699
PANTHER:PTN000344216
PomBase:SPBC16H5.02
SGD:S000003472
SGD:S000004818
UniProtKB:P08237
UniProtKB:P17858
dictyBase:DDB_G0274111

C

Seeded From UniProt

complete

enables

GO:0005524

ATP binding

PMID:21873635[3]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

EcoGene:EG10699
PANTHER:PTN000344216
PomBase:SPBC16H5.02
RGD:3311
RGD:61893
RGD:68419
UniProtKB:P08237
UniProtKB:P17858

F

Seeded From UniProt

complete

enables

GO:0003872

6-phosphofructokinase activity

PMID:21873635[3]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

EcoGene:EG10699
FB:FBgn0003071
MGI:MGI:97548
PANTHER:PTN000344216
PomBase:SPBC16H5.02
RGD:61893
RGD:68419
UniProtKB:P08237
UniProtKB:Q01813
dictyBase:DDB_G0274111

F

Seeded From UniProt

complete

involved_in

GO:0044275

cellular carbohydrate catabolic process

PMID:4299078[4]

ECO:0000315

mutant phenotype evidence used in manual assertion

P

Seeded From UniProt

complete

enables

GO:0042802

identical protein binding

PMID:11946283[5]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

enables

GO:0032553

ribonucleotide binding

PMID:4229913[6]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

involved_in

GO:0006096

glycolytic process

PMID:15237399[7]

ECO:0000314

direct assay evidence used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:0006007

glucose catabolic process

PMID:4299078[4]

ECO:0000315

mutant phenotype evidence used in manual assertion

P

Seeded From UniProt

complete

part_of

GO:0005945

6-phosphofructokinase complex

PMID:6232272[8]

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

part_of

GO:0005737

cytoplasm

PMID:4229913[6]

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

enables

GO:0005524

ATP binding

PMID:8202475[9]

ECO:0000315

mutant phenotype evidence used in manual assertion

F

Seeded From UniProt

complete

enables

GO:0003872

6-phosphofructokinase activity

PMID:125265[10]

ECO:0000315

mutant phenotype evidence used in manual assertion

F

Seeded From UniProt

complete

enables

GO:0000287

magnesium ion binding

PMID:1445885[11]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

involved_in

GO:0051289

protein homotetramerization

PMID:11946283[5]

ECO:0000353

physical interaction evidence used in manual assertion

UniProtKB:P0A796

P

Seeded From UniProt

complete

enables

GO:0019003

GDP binding

PMID:70226[12]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

involved_in

GO:0006096

glycolytic process

PMID:177406[13]

ECO:0000315

mutant phenotype evidence used in manual assertion

P

Seeded From UniProt

complete

part_of

GO:0005829

cytosol

PMID:18304323[14]

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

part_of

GO:0005829

cytosol

PMID:15911532[15]

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

enables

GO:0003872

6-phosphofructokinase activity

PMID:4229913[6]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

involved_in

GO:0046835

carbohydrate phosphorylation

GO_REF:0000108

ECO:0000366

evidence based on logical inference from automatic annotation used in automatic assertion

GO:0008443

P

Seeded From UniProt

complete

enables

GO:0003872

6-phosphofructokinase activity

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR000023
InterPro:IPR012828
InterPro:IPR015912
InterPro:IPR022953
InterPro:IPR035966

F

Seeded From UniProt

complete

enables

GO:0005524

ATP binding

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR012003
InterPro:IPR012828

F

Seeded From UniProt

complete

involved_in

GO:0006002

fructose 6-phosphate metabolic process

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR012003
InterPro:IPR012828
InterPro:IPR022953

P

Seeded From UniProt

complete

involved_in

GO:0006096

glycolytic process

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR000023
InterPro:IPR012003
InterPro:IPR012828
InterPro:IPR015912
InterPro:IPR022953
InterPro:IPR035966

P

Seeded From UniProt

complete

enables

GO:0008443

phosphofructokinase activity

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR012003

F

Seeded From UniProt

complete

enables

GO:0003872

6-phosphofructokinase activity

GO_REF:0000003

ECO:0000501

evidence used in automatic assertion

EC:2.7.1.11

F

Seeded From UniProt

complete

part_of

GO:0005737

cytoplasm

GO_REF:0000104

ECO:0000256

match to sequence model evidence used in automatic assertion

UniRule:UR000084084

C

Seeded From UniProt

complete

involved_in

GO:0006096

glycolytic process

GO_REF:0000104

ECO:0000256

match to sequence model evidence used in automatic assertion

UniRule:UR000084084

P

Seeded From UniProt

complete

enables

GO:0003872

6-phosphofructokinase activity

GO_REF:0000104

ECO:0000256

match to sequence model evidence used in automatic assertion

UniRule:UR000084084

F

Seeded From UniProt

complete

involved_in

GO:0008152

metabolic process

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0021

P

Seeded From UniProt

complete

enables

GO:0003824

catalytic activity

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0021

F

Seeded From UniProt

complete

part_of

GO:0005737

cytoplasm

GO_REF:0000037
GO_REF:0000039

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0963
UniProtKB-SubCell:SL-0086

C

Seeded From UniProt

complete

enables

GO:0000166

nucleotide binding

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0547

F

Seeded From UniProt

complete

enables

GO:0016301

kinase activity

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0418

F

Seeded From UniProt

complete

involved_in

GO:0006096

glycolytic process

GO_REF:0000037
GO_REF:0000041

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0324
UniPathway:UPA00109

P

Seeded From UniProt

complete

enables

GO:0046872

metal ion binding

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0479

F

Seeded From UniProt

complete

involved_in

GO:0016310

phosphorylation

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0418

P

Seeded From UniProt

complete

enables

GO:0016740

transferase activity

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0808

F

Seeded From UniProt

complete

enables

GO:0005524

ATP binding

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0067

F

Seeded From UniProt

complete

edit table

Notes

References

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

  1. ↑ 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
  2. ↑ 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
  3. ↑ 3.00 3.01 3.02 3.03 3.04 3.05 3.06 3.07 3.08 3.09 3.10 3.11 Gaudet, P et al. (2011) Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium. Brief. Bioinformatics 12 449-62 PubMed GONUTS page
  4. ↑ 4.0 4.1 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
  5. ↑ 5.0 5.1 Blangy, D (1968) Phosphofructokinase from E. Coli: Evidence for a tetrameric structure of the enzyme. FEBS Lett. 2 109-111 PubMed GONUTS page
  6. ↑ 6.0 6.1 6.2 Blangy, D et al. (1968) Kinetics of the allosteric interactions of phosphofructokinase from Escherichia coli. J. Mol. Biol. 31 13-35 PubMed GONUTS page
  7. ↑ Itoh, A et al. (2004) Application of capillary electrophoresis-mass spectrometry to synthetic in vitro glycolysis studies. Electrophoresis 25 1996-2002 PubMed GONUTS page
  8. ↑ Martel, A & Garel, JR (1984) Renaturation of the allosteric phosphofructokinase from Escherichia coli. J. Biol. Chem. 259 4917-21 PubMed GONUTS page
  9. ↑ 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
  10. ↑ Vinopal, RT et al. (1975) PfkA locus of Escherichia coli. J. Bacteriol. 122 1162-71 PubMed GONUTS page
  11. ↑ Johnson, JL & Reinhart, GD (1992) MgATP and fructose 6-phosphate interactions with phosphofructokinase from Escherichia coli. Biochemistry 31 11510-8 PubMed GONUTS page
  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
  13. ↑ Roehl, RA & Vinopal, RT (1976) Lack of glucose phosphotransferase function in phosphofructokinase mutants of Escherichia coli. J. Bacteriol. 126 852-60 PubMed GONUTS page
  14. ↑ Ishihama, Y et al. (2008) Protein abundance profiling of the Escherichia coli cytosol. BMC Genomics 9 102 PubMed GONUTS page
  15. ↑ Lopez-Campistrous, A et al. (2005) Localization, annotation, and comparison of the Escherichia coli K-12 proteome under two states of growth. Mol. Cell Proteomics 4 1205-9 PubMed GONUTS page
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