pfkA:Gene Product(s)

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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[2][3]

6-phosphofructokinase-1; allosteric: activated by MgNDPs, inhibited by PEP; homoterameric[4]

EC number (for enzymes)

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Notes

Function

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<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
SP_KW:GO_REF:0000004

IEA: Inferred from Electronic Annotation

SP_KW:KW-0460

F

Seeded from EcoCyc (v14.0)

complete

GO:0003872

6-phosphofructokinase activity

GOA:hamap
GO_REF:0000020

IEA: Inferred from Electronic Annotation

HAMAP:MF_00339

F

Seeded from EcoCyc (v14.0)

complete

GO:0003872

6-phosphofructokinase activity

GOA:interpro
GO_REF:0000002

IEA: Inferred from Electronic Annotation

InterPro:IPR000023

F

Seeded from EcoCyc (v14.0)

complete

GO:0003872

6-phosphofructokinase activity

GOA:interpro
GO_REF:0000002

IEA: Inferred from Electronic Annotation

InterPro:IPR012828

F

Seeded from EcoCyc (v14.0)

complete

GO:0003872

6-phosphofructokinase activity

GOA:interpro
GO_REF:0000002

IEA: Inferred from Electronic Annotation

InterPro:IPR015912

F

Seeded from EcoCyc (v14.0)

complete

GO:0003872

6-phosphofructokinase activity

GOA:spec
GO_REF:0000003

IEA: Inferred from Electronic Annotation

EC:2.7.1.11

F

Seeded from EcoCyc (v14.0)

complete

GO:0005524

ATP binding

GOA:interpro
GO_REF:0000002

IEA: Inferred from Electronic Annotation

InterPro:IPR012003

F

Seeded from EcoCyc (v14.0)

complete

GO:0005524

ATP binding

GOA:interpro
GO_REF:0000002

IEA: Inferred from Electronic Annotation

InterPro:IPR012828

F

Seeded from EcoCyc (v14.0)

complete

GO:0005524

ATP binding

GOA:spkw
SP_KW:GO_REF:0000004

IEA: Inferred from Electronic Annotation

SP_KW:KW-0067

F

Seeded from EcoCyc (v14.0)

complete

GO:0005945

6-phosphofructokinase complex

GOA:interpro
GO_REF:0000002

IEA: Inferred from Electronic Annotation

InterPro:IPR000023

C

Seeded from EcoCyc (v14.0)

complete

GO:0005945

6-phosphofructokinase complex

GOA:interpro
GO_REF:0000002

IEA: Inferred from Electronic Annotation

InterPro:IPR015912

C

Seeded from EcoCyc (v14.0)

complete

GO:0006002

fructose 6-phosphate metabolic process

GOA:interpro
GO_REF:0000002

IEA: Inferred from Electronic Annotation

InterPro:IPR012003

P

Seeded from EcoCyc (v14.0)

complete

GO:0006002

fructose 6-phosphate metabolic process

GOA:interpro
GO_REF:0000002

IEA: Inferred from Electronic Annotation

InterPro:IPR012828

P

Seeded from EcoCyc (v14.0)

complete

GO:0006096

glycolysis

GOA:hamap
GO_REF:0000020

IEA: Inferred from Electronic Annotation

HAMAP:MF_00339

P

Seeded from EcoCyc (v14.0)

complete

GO:0006096

glycolysis

GOA:interpro
GO_REF:0000002

IEA: Inferred from Electronic Annotation

InterPro:IPR000023

P

Seeded from EcoCyc (v14.0)

complete

GO:0006096

glycolysis

GOA:interpro
GO_REF:0000002

IEA: Inferred from Electronic Annotation

InterPro:IPR012003

P

Seeded from EcoCyc (v14.0)

complete

GO:0006096

glycolysis

GOA:interpro
GO_REF:0000002

IEA: Inferred from Electronic Annotation

InterPro:IPR012828

P

Seeded from EcoCyc (v14.0)

complete

GO:0006096

glycolysis

GOA:interpro
GO_REF:0000002

IEA: Inferred from Electronic Annotation

InterPro:IPR015912

P

Seeded from EcoCyc (v14.0)

complete

GO:0006096

glycolysis

GOA:spkw
SP_KW:GO_REF:0000004

IEA: Inferred from Electronic Annotation

SP_KW:KW-0324

P

Seeded from EcoCyc (v14.0)

complete

GO:0003872

6-phosphofructokinase activity

PMID:125265[5]

IMP: Inferred from Mutant Phenotype

F

complete

GO:0005524

ATP binding

PMID:8202475[6]

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

PMID:6232272[7]

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

PMID:1445885[8]

IDA: Inferred from Direct Assay

F

complete

GO:0032553

ribonucleotide binding

PMID:4229913[9]

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

PMID:4229913[9]

IDA: Inferred from Direct Assay

C

complete

GO:0042802

identical protein binding

PMID:11946283[10]

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

PMID:4299078[11]

IMP: Inferred from Mutant Phenotype

P

pfkA mutants are defective in utilization of glucose and mannitol.

complete

GO:0005488

binding

PMID:17307338[12]

IDA: Inferred from Direct Assay

F

Phosphoenolpyruvate (CHEBI:18021) binding inhibits PfkA activity.

complete

GO:0006096

glycolysis

PMID:15237399[13]

IDA: Inferred from Direct Assay

P

Pathway reconstituted in vitro with purified E. coli enzymes.

complete

GO:0006007

glucose catabolic process

PMID:4299078[11]

IMP: Inferred from Mutant Phenotype

P

pfkA mutants are defective in growth on glucose.

complete

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

PMID:16606699[14]

Experiment(s):EBI-1147000

Protein

tpiA

PMID:16606699[14]

Experiment(s):EBI-1147000, EBI-1147023

Protein

argG

PMID:16606699[14]

Experiment(s):EBI-1147000

Protein

aspS

PMID:16606699[14]

Experiment(s):EBI-1147000

Small Molecule

phosphoenolpyruvate

Inhibitory


</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

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Notes

Structure and Physical Properties

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<protect> Physical Properties See Help:Product_physical_properties for help entering or editing information about the physical properties of this gene product.

Name
Sequence

at EcoCyc

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)


Domains/Motifs/Modification Sites

See Help:Product_domains_motifs for help entering or editing information in this section of EcoliWiki.

Type Residues Description Notes References

Domain

3..278

PF00365 Phosphofructokinase

PMID:19920124[15]

<motif_map/>

Structure
See Help:Product_structure for help entering or editing information in this section of EcoliWiki.

Structures

<beststructure> gene=pfkA taxon=562,83333 </beststructure>

Models

View models at:

</protect>

Structure figures

<protect>

</protect>

Notes

Gene Product Resources

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See Help:Product_resources for help with entering or editing information in this section of EcoliWiki.

Resource type Source Notes/Reference

<protect></protect>

Notes

Accessions in Other Databases

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See Help:Gene_accessions for help with entering information into the Gene Accessions table.

Database Accession Notes

NCBI (Protein) (EcoliWiki Page)

GI:16131754

Escherichia coli str. K-12 substr. MG1655

NCBI (Protein) (EcoliWiki Page)

GeneID:948412

Escherichia coli str. K-12 substr. MG1655

ASAP

ASAP:ABE-0012789

Escherichia coli str. K-12 substr. MG1655

UniProt (EcoliWiki Page)

UniProtKB/Swiss-Prot:P0A796

Escherichia coli str. K-12 substr. MG1655

EcoCyc

EcoCyc:EG10699

Escherichia coli str. K-12 substr. MG1655

EcoGene

EcoGene:EG10699

Escherichia coli str. K-12 substr. MG1655

NCBI (Gene) (EcoliWiki Page)

GeneID:948412

Escherichia coli str. K-12 substr. MG1655

RegulonDB

RegulonDB:ECK120000691

Escherichia coli str. K-12 substr. MG1655

EchoBASE

EchoBASE:EB0693

Escherichia coli str. K-12 substr. MG1655

<protect></protect>

Notes

Links

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References

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

  1. 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. 2.0 2.1 2.2 EcoCyc (release 10.6; 2007) Keseler, IM et al. (2005) Nucleic Acids Res. 33(Database issue):D334-7
  3. EcoCyc (release 11.1; 2007) Keseler, IM et al. (2005) Nucleic Acids Res. 33(Database issue):D334-7
  4. EcoGene: Rudd, KE (2000) EcoGene: a genome sequence database for Escherichia coli K-12. Nucleic Acids Res 28:60-4.
  5. Vinopal, RT et al. (1975) PfkA locus of Escherichia coli. J. Bacteriol. 122 1162-71 PubMed
  6. 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
  7. Martel, A & Garel, JR (1984) Renaturation of the allosteric phosphofructokinase from Escherichia coli. J. Biol. Chem. 259 4917-21 PubMed
  8. Johnson, JL & Reinhart, GD (1992) MgATP and fructose 6-phosphate interactions with phosphofructokinase from Escherichia coli. Biochemistry 31 11510-8 PubMed
  9. 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
  10. Blangy, D (1968) Phosphofructokinase from E. Coli: Evidence for a tetrameric structure of the enzyme. FEBS Lett. 2 109-111 PubMed
  11. 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
  12. Ogawa, T et al. (2007) Inhibitory effect of phosphoenolpyruvate on glycolytic enzymes in Escherichia coli. Res. Microbiol. 158 159-63 PubMed
  13. Itoh, A et al. (2004) Application of capillary electrophoresis-mass spectrometry to synthetic in vitro glycolysis studies. Electrophoresis 25 1996-2002 PubMed
  14. 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
  15. Finn, RD et al. (2010) The Pfam protein families database. Nucleic Acids Res. 38 D211-22 PubMed

Categories

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