pfkA:Gene Product(s)
{{#css:Suppresslinks.css}}<css>h1 .editsection { display:none;} h2 .editsection { display:none;}</css>
Quickview | Gene | Gene Product(s) | Expression | Evolution | On One Page |
Nomenclature | Function | Interactions | Localization | Sequence | Domains | Structure | Resources | Accessions | Links | References | Suggestions |
Nomenclature
See Help:Product_nomenclature for help entering or editing information in this section of EcoliWiki.
Standard name |
PfkA |
---|---|
Synonyms |
6-phosphofructokinase I[1], B3916[2][1], PfkA[2][1] , ECK3908, JW3887, b3916 |
Product description |
6-phosphofructokinase-1; allosteric: activated by MgNDPs, inhibited by PEP; homoterameric[4] |
EC number (for enzymes) | |
edit table |
<protect></protect>
Notes
Function
<protect>
Gene Ontology
See Help:Gene_ontology for help entering or editing GO terms and GO annotations in EcoliWiki.
Qualifier | GO ID | GO term name | Reference | Evidence Code | with/from | Aspect | Notes | Status |
---|---|---|---|---|---|---|---|---|
GO:0000287 |
magnesium ion binding |
GOA:spkw |
IEA: Inferred from Electronic Annotation |
F |
Seeded from EcoCyc (v14.0) |
complete | ||
GO:0003872 |
6-phosphofructokinase activity |
GOA:hamap |
IEA: Inferred from Electronic Annotation |
F |
Seeded from EcoCyc (v14.0) |
complete | ||
GO:0003872 |
6-phosphofructokinase activity |
GOA:interpro |
IEA: Inferred from Electronic Annotation |
F |
Seeded from EcoCyc (v14.0) |
complete | ||
GO:0003872 |
6-phosphofructokinase activity |
GOA:interpro |
IEA: Inferred from Electronic Annotation |
F |
Seeded from EcoCyc (v14.0) |
complete | ||
GO:0003872 |
6-phosphofructokinase activity |
GOA:interpro |
IEA: Inferred from Electronic Annotation |
F |
Seeded from EcoCyc (v14.0) |
complete | ||
GO:0003872 |
6-phosphofructokinase activity |
GOA:spec |
IEA: Inferred from Electronic Annotation |
F |
Seeded from EcoCyc (v14.0) |
complete | ||
GO:0005524 |
ATP binding |
GOA:interpro |
IEA: Inferred from Electronic Annotation |
F |
Seeded from EcoCyc (v14.0) |
complete | ||
GO:0005524 |
ATP binding |
GOA:interpro |
IEA: Inferred from Electronic Annotation |
F |
Seeded from EcoCyc (v14.0) |
complete | ||
GO:0005524 |
ATP binding |
GOA:spkw |
IEA: Inferred from Electronic Annotation |
F |
Seeded from EcoCyc (v14.0) |
complete | ||
GO:0005945 |
6-phosphofructokinase complex |
GOA:interpro |
IEA: Inferred from Electronic Annotation |
C |
Seeded from EcoCyc (v14.0) |
complete | ||
GO:0005945 |
6-phosphofructokinase complex |
GOA:interpro |
IEA: Inferred from Electronic Annotation |
C |
Seeded from EcoCyc (v14.0) |
complete | ||
GO:0006002 |
fructose 6-phosphate metabolic process |
GOA:interpro |
IEA: Inferred from Electronic Annotation |
P |
Seeded from EcoCyc (v14.0) |
complete | ||
GO:0006002 |
fructose 6-phosphate metabolic process |
GOA:interpro |
IEA: Inferred from Electronic Annotation |
P |
Seeded from EcoCyc (v14.0) |
complete | ||
GO:0006096 |
glycolysis |
GOA:hamap |
IEA: Inferred from Electronic Annotation |
P |
Seeded from EcoCyc (v14.0) |
complete | ||
GO:0006096 |
glycolysis |
GOA:interpro |
IEA: Inferred from Electronic Annotation |
P |
Seeded from EcoCyc (v14.0) |
complete | ||
GO:0006096 |
glycolysis |
GOA:interpro |
IEA: Inferred from Electronic Annotation |
P |
Seeded from EcoCyc (v14.0) |
complete | ||
GO:0006096 |
glycolysis |
GOA:interpro |
IEA: Inferred from Electronic Annotation |
P |
Seeded from EcoCyc (v14.0) |
complete | ||
GO:0006096 |
glycolysis |
GOA:interpro |
IEA: Inferred from Electronic Annotation |
P |
Seeded from EcoCyc (v14.0) |
complete | ||
GO:0006096 |
glycolysis |
GOA:spkw |
IEA: Inferred from Electronic Annotation |
P |
Seeded from EcoCyc (v14.0) |
complete | ||
GO:0003872 |
6-phosphofructokinase activity |
IMP: Inferred from Mutant Phenotype |
F |
complete | ||||
GO:0005524 |
ATP binding |
IMP: Inferred from Mutant Phenotype |
F |
Mutation of threonine at position 125 to serine in PfkA prevents allosteric activation and PEP-dependent inhibition. |
complete | |||
GO:0005945 |
6-phosphofructokinase complex |
IDA: Inferred from Direct Assay |
C |
Renaturation of purified PfkA after treatment with 7M guanidine hydrochloride resulted in recovery of catalytic activity and allosteric regulation. |
complete | |||
GO:0000287 |
magnesium ion binding |
IDA: Inferred from Direct Assay |
F |
complete | ||||
GO:0032553 |
ribonucleotide binding |
IDA: Inferred from Direct Assay |
F |
Purified phosphofructokinase was assayed in a coupled assay (as described in this paper) for activity in the presence of nucleotide-monophosphates, nucleotide-diphosphates and nucleotide-triphosphates. Activity was increased in the presence of nucleotide-diphosphates, in particular, GDP and ADP. |
complete | |||
GO:0005737 |
cytoplasm |
IDA: Inferred from Direct Assay |
C |
complete | ||||
GO:0042802 |
identical protein binding |
IDA: Inferred from Direct Assay |
F |
Phosphofructokinase was characterized to be a tetramer by sedimentation velocity and equilibrium experiments as well as SDS-PAGE analysis. |
complete | |||
GO:0044275 |
cellular carbohydrate catabolic process |
IMP: Inferred from Mutant Phenotype |
P |
pfkA mutants are defective in utilization of glucose and mannitol. |
complete | |||
GO:0005488 |
binding |
IDA: Inferred from Direct Assay |
F |
Phosphoenolpyruvate (CHEBI:18021) binding inhibits PfkA activity. |
complete | |||
GO:0006096 |
glycolysis |
IDA: Inferred from Direct Assay |
P |
Pathway reconstituted in vitro with purified E. coli enzymes. |
complete | |||
GO:0006007 |
glucose catabolic process |
IMP: Inferred from Mutant Phenotype |
P |
pfkA mutants are defective in growth on glucose. |
complete | |||
edit table |
Interactions See Help:Product_interactions for help entering or editing information about gene product interactions in this section of EcoliWiki.
Partner Type | Partner | Notes | References | Evidence |
---|---|---|---|---|
Protein |
fpr |
Experiment(s):EBI-1147000 | ||
Protein |
tpiA |
Experiment(s):EBI-1147000, EBI-1147023 | ||
Protein |
argG |
Experiment(s):EBI-1147000 | ||
Protein |
aspS |
Experiment(s):EBI-1147000 | ||
Small Molecule |
phosphoenolpyruvate |
Inhibitory |
| |
edit table |
</protect>
Notes
Localization
See Help:Product_localization for how to add or edit information in this section of EcoliWiki.
Compartment | Description | Evidence | Reference/Source | Notes |
---|---|---|---|---|
edit table |
<protect></protect>
Notes
Structure and Physical Properties
<protect>
Physical Properties
See Help:Product_physical_properties for help entering or editing information about the physical properties of this gene product.
Name | |
---|---|
Sequence |
MIKKIGVLTS GGDAPGMNAA IRGVVRSALT EGLEVMGIYD GYLGLYEDRM VQLDRYSVSD MINRGGTFLG SARFPEFRDE NIRAVAIENL KKRGIDALVV IGGDGSYMGA MRLTEMGFPC IGLPGTIDND IKGTDYTIGF FTALSTVVEA IDRLRDTSSS HQRISVVEVM GRYCGDLTLA AAIAGGCEFV VVPEVEFSRE DLVNEIKAGI AKGKKHAIVA ITEHMCDVDE LAHFIEKETG RETRATVLGH IQRGGSPVPY DRILASRMGA YAIDLLLAGY GGRCVGIQNE QLVHHDIIDA IENMKRPFKG DWLDCAKKLY |
Length |
320 |
Mol. Wt |
34.842 kDa |
pI |
5.5 (calculated) |
Extinction coefficient |
21,890 - 22,640 (calc based on 11 Y, 1 W, and 6 C residues) |
edit table |
Domains/Motifs/Modification Sites
See Help:Product_domains_motifs for help entering or editing information in this section of EcoliWiki.
|
<motif_map/> |
Structure
| </protect>
Structure figures<protect> | ||||||
Notes
Gene Product Resources
See Help:Product_resources for help with entering or editing information in this section of EcoliWiki.
Resource type | Source | Notes/Reference |
---|---|---|
edit table |
<protect></protect>
Notes
Accessions in Other Databases
See Help:Gene_accessions for help with entering information into the Gene Accessions table.
Database | Accession | Notes |
---|---|---|
Escherichia coli str. K-12 substr. MG1655 | ||
Escherichia coli str. K-12 substr. MG1655 | ||
Escherichia coli str. K-12 substr. MG1655 | ||
Escherichia coli str. K-12 substr. MG1655 | ||
Escherichia coli str. K-12 substr. MG1655 | ||
Escherichia coli str. K-12 substr. MG1655 | ||
Escherichia coli str. K-12 substr. MG1655 | ||
Escherichia coli str. K-12 substr. MG1655 | ||
Escherichia coli str. K-12 substr. MG1655 | ||
edit table |
<protect></protect>
Notes
Links
Name | URL | Comments |
---|---|---|
edit table |
References
See Help:References for how to manage references in EcoliWiki.
- ↑ 1.0 1.1 1.2 1.3 Riley, M. et al. (2006) Nucleic Acids Res 34:1-6 (corrected supplemental data from B. Wanner)
- ↑ 2.0 2.1 2.2 EcoCyc (release 10.6; 2007) Keseler, IM et al. (2005) Nucleic Acids Res. 33(Database issue):D334-7
- ↑ EcoCyc (release 11.1; 2007) Keseler, IM et al. (2005) Nucleic Acids Res. 33(Database issue):D334-7
- ↑ EcoGene: Rudd, KE (2000) EcoGene: a genome sequence database for Escherichia coli K-12. Nucleic Acids Res 28:60-4.
- ↑ Vinopal, RT et al. (1975) PfkA locus of Escherichia coli. J. Bacteriol. 122 1162-71 PubMed
- ↑ 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
- ↑ Martel, A & Garel, JR (1984) Renaturation of the allosteric phosphofructokinase from Escherichia coli. J. Biol. Chem. 259 4917-21 PubMed
- ↑ Johnson, JL & Reinhart, GD (1992) MgATP and fructose 6-phosphate interactions with phosphofructokinase from Escherichia coli. Biochemistry 31 11510-8 PubMed
- ↑ 9.0 9.1 Blangy, D et al. (1968) Kinetics of the allosteric interactions of phosphofructokinase from Escherichia coli. J. Mol. Biol. 31 13-35 PubMed
- ↑ Blangy, D (1968) Phosphofructokinase from E. Coli: Evidence for a tetrameric structure of the enzyme. FEBS Lett. 2 109-111 PubMed
- ↑ 11.0 11.1 Morrissey, AT & Fraenkel, DG (1968) Selection of fructose 6-phosphate kinase mutants in Escherichia coli. Biochem. Biophys. Res. Commun. 32 467-73 PubMed
- ↑ Ogawa, T et al. (2007) Inhibitory effect of phosphoenolpyruvate on glycolytic enzymes in Escherichia coli. Res. Microbiol. 158 159-63 PubMed
- ↑ Itoh, A et al. (2004) Application of capillary electrophoresis-mass spectrometry to synthetic in vitro glycolysis studies. Electrophoresis 25 1996-2002 PubMed
- ↑ 14.0 14.1 14.2 14.3 Arifuzzaman, M et al. (2006) Large-scale identification of protein-protein interaction of Escherichia coli K-12. Genome Res. 16 686-91 PubMed
- ↑ Finn, RD et al. (2010) The Pfam protein families database. Nucleic Acids Res. 38 D211-22 PubMed
Categories
- GO:0000287 ! magnesium ion binding
- GO:0003872 ! 6-phosphofructokinase activity
- GO:0005524 ! ATP binding
- GO:0005945 ! 6-phosphofructokinase complex
- GO:0006002 ! fructose 6-phosphate metabolic process
- GO:0006096 ! glycolytic process
- GO:0032553 ! ribonucleotide binding
- GO:0005737 ! cytoplasm
- GO:0042802 ! identical protein binding
- GO:0044275 ! cellular carbohydrate catabolic process
- GO:0005488 ! binding
- GO:0006007 ! glucose catabolic process
- Proteins