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Protein

ATP-dependent 6-phosphofructokinase isozyme 1

Gene

pfkA

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the phosphorylation of D-fructose 6-phosphate to fructose 1,6-bisphosphate by ATP, the first committing step of glycolysis.UniRule annotation

Catalytic activityi

ATP + D-fructose 6-phosphate = ADP + D-fructose 1,6-bisphosphate.UniRule annotation

Cofactori

Mg2+UniRule annotation1 Publication

Enzyme regulationi

Allosterically activated by ADP and other diphosphonucleosides, and allosterically inhibited by phosphoenolpyruvate.UniRule annotation

Pathwayi: glycolysis

This protein is involved in step 3 of the subpathway that synthesizes D-glyceraldehyde 3-phosphate and glycerone phosphate from D-glucose.UniRule annotation
Proteins known to be involved in the 4 steps of the subpathway in this organism are:
  1. no protein annotated in this organism
  2. Glucose-6-phosphate isomerase (pgi)
  3. ATP-dependent 6-phosphofructokinase isozyme 2 (pfkB), ATP-dependent 6-phosphofructokinase isozyme 1 (pfkA)
  4. Fructose-bisphosphate aldolase class 2 (fbaA)
This subpathway is part of the pathway glycolysis, which is itself part of Carbohydrate degradation.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes D-glyceraldehyde 3-phosphate and glycerone phosphate from D-glucose, the pathway glycolysis and in Carbohydrate degradation.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei12ATP; via amide nitrogenUniRule annotation1 Publication1
Metal bindingi104Magnesium; catalyticUniRule annotation1 Publication1
Active sitei128Proton acceptorUniRule annotation2 Publications1
Binding sitei155Allosteric activator ADPUniRule annotation1 Publication1
Binding sitei163Substrate; shared with dimeric partnerUniRule annotation1 Publication1
Binding sitei212Allosteric activator ADPUniRule annotationBy similarity1
Binding sitei223SubstrateUniRule annotation1 Publication1
Binding sitei244Substrate; shared with dimeric partnerUniRule annotation1 Publication1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi73 – 74ATPUniRule annotation1 Publication2
Nucleotide bindingi103 – 106ATPUniRule annotation1 Publication4

GO - Molecular functioni

  • 6-phosphofructokinase activity Source: EcoCyc
  • ATP binding Source: EcoliWiki
  • GDP binding Source: EcoCyc
  • identical protein binding Source: EcoliWiki
  • magnesium ion binding Source: EcoliWiki
  • ribonucleotide binding Source: EcoliWiki

GO - Biological processi

  • cellular carbohydrate catabolic process Source: EcoliWiki
  • fructose 6-phosphate metabolic process Source: InterPro
  • glucose catabolic process Source: EcoliWiki
  • glycolytic process Source: EcoliWiki
  • protein homotetramerization Source: EcoCyc
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Transferase

Keywords - Biological processi

Glycolysis

Keywords - Ligandi

ATP-binding, Magnesium, Metal-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciEcoCyc:6PFK-1-MONOMER.
ECOL316407:JW3887-MONOMER.
MetaCyc:6PFK-1-MONOMER.
BRENDAi2.7.1.11. 2026.
SABIO-RKP0A796.
UniPathwayiUPA00109; UER00182.

Names & Taxonomyi

Protein namesi
Recommended name:
ATP-dependent 6-phosphofructokinase isozyme 1UniRule annotation (EC:2.7.1.11UniRule annotation)
Short name:
ATP-PFK 1UniRule annotation
Short name:
Phosphofructokinase 1UniRule annotation
Alternative name(s):
6-phosphofructokinase isozyme I
Phosphohexokinase 1UniRule annotation
Gene namesi
Name:pfkAUniRule annotation
Ordered Locus Names:b3916, JW3887
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG10699. pfkA.

Subcellular locationi

  • Cytoplasm UniRule annotation1 Publication

GO - Cellular componenti

  • 6-phosphofructokinase complex Source: EcoliWiki
  • cytoplasm Source: EcoliWiki
  • cytosol Source: EcoCyc
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi128D → S: 18000-fold reduction of catalytic rate. 1 Publication1
Mutagenesisi172R → S: 3.4-fold reduction in turnover numbers. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001119501 – 320ATP-dependent 6-phosphofructokinase isozyme 1Add BLAST320

Proteomic databases

EPDiP0A796.
PaxDbiP0A796.
PRIDEiP0A796.

2D gel databases

SWISS-2DPAGEP0A796.

Interactioni

Subunit structurei

Homotetramer.UniRule annotation1 Publication

GO - Molecular functioni

  • identical protein binding Source: EcoliWiki

Protein-protein interaction databases

BioGridi4261224. 4 interactors.
DIPiDIP-35841N.
IntActiP0A796. 7 interactors.
MINTiMINT-1322275.
STRINGi511145.b3916.

Structurei

Secondary structure

1320
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi4 – 9Combined sources6
Helixi17 – 30Combined sources14
Beta strandi34 – 39Combined sources6
Helixi41 – 46Combined sources6
Beta strandi50 – 53Combined sources4
Helixi56 – 58Combined sources3
Helixi75 – 78Combined sources4
Helixi80 – 92Combined sources13
Beta strandi97 – 102Combined sources6
Helixi104 – 115Combined sources12
Beta strandi120 – 125Combined sources6
Helixi140 – 161Combined sources22
Beta strandi164 – 169Combined sources6
Helixi176 – 184Combined sources9
Beta strandi188 – 191Combined sources4
Helixi199 – 211Combined sources13
Beta strandi217 – 226Combined sources10
Helixi228 – 239Combined sources12
Beta strandi243 – 247Combined sources5
Helixi249 – 253Combined sources5
Helixi259 – 277Combined sources19
Beta strandi282 – 288Combined sources7
Beta strandi291 – 296Combined sources6
Helixi297 – 303Combined sources7
Helixi310 – 319Combined sources10

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1PFKX-ray2.40A/B1-320[»]
2PFKX-ray2.40A/B/C/D1-320[»]
ProteinModelPortaliP0A796.
SMRiP0A796.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP0A796.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni22 – 26Allosteric activator ADP binding; shared with dimeric partnerUniRule annotation1 Publication5
Regioni55 – 60Allosteric activator ADP binding; shared with dimeric partnerUniRule annotation1 Publication6
Regioni126 – 128Substrate bindingUniRule annotation1 Publication3
Regioni170 – 172Substrate bindingUniRule annotationBy similarity3
Regioni186 – 188Allosteric activator ADP bindingUniRule annotation1 Publication3
Regioni214 – 216Allosteric activator ADP bindingUniRule annotation1 Publication3
Regioni250 – 253Substrate bindingUniRule annotation1 Publication4

Sequence similaritiesi

Belongs to the phosphofructokinase type A (PFKA) family. ATP-dependent PFK group I subfamily. Prokaryotic clade "B1" sub-subfamily.UniRule annotation

Phylogenomic databases

eggNOGiENOG4105CTQ. Bacteria.
COG0205. LUCA.
HOGENOMiHOG000248870.
InParanoidiP0A796.
KOiK00850.
OMAiAIITICE.
PhylomeDBiP0A796.

Family and domain databases

CDDicd00763. Bacterial_PFK. 1 hit.
HAMAPiMF_00339. Phosphofructokinase_I_B1. 1 hit.
InterProiIPR022953. ATP_PFK.
IPR012003. ATP_PFK_prok-type.
IPR012828. PFKA_ATP_prok.
IPR015912. Phosphofructokinase_CS.
IPR000023. Phosphofructokinase_dom.
[Graphical view]
PfamiPF00365. PFK. 1 hit.
[Graphical view]
PIRSFiPIRSF000532. ATP_PFK_prok. 1 hit.
PRINTSiPR00476. PHFRCTKINASE.
SUPFAMiSSF53784. SSF53784. 1 hit.
TIGRFAMsiTIGR02482. PFKA_ATP. 1 hit.
PROSITEiPS00433. PHOSPHOFRUCTOKINASE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P0A796-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MIKKIGVLTS GGDAPGMNAA IRGVVRSALT EGLEVMGIYD GYLGLYEDRM
60 70 80 90 100
VQLDRYSVSD MINRGGTFLG SARFPEFRDE NIRAVAIENL KKRGIDALVV
110 120 130 140 150
IGGDGSYMGA MRLTEMGFPC IGLPGTIDND IKGTDYTIGF FTALSTVVEA
160 170 180 190 200
IDRLRDTSSS HQRISVVEVM GRYCGDLTLA AAIAGGCEFV VVPEVEFSRE
210 220 230 240 250
DLVNEIKAGI AKGKKHAIVA ITEHMCDVDE LAHFIEKETG RETRATVLGH
260 270 280 290 300
IQRGGSPVPY DRILASRMGA YAIDLLLAGY GGRCVGIQNE QLVHHDIIDA
310 320
IENMKRPFKG DWLDCAKKLY
Length:320
Mass (Da):34,842
Last modified:June 7, 2005 - v1
Checksum:iD03D79F6A5536A41
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti74F → C in CAA26356 (PubMed:3158524).Curated1
Sequence conflicti103 – 104GD → DG in CAA26356 (PubMed:3158524).Curated2
Sequence conflicti163R → P in CAA26356 (PubMed:3158524).Curated1
Sequence conflicti317 – 319KKL → EKM in CAA26356 (PubMed:3158524).Curated3

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X02519 Genomic DNA. Translation: CAA26356.1.
L19201 Genomic DNA. Translation: AAB03048.1.
U00096 Genomic DNA. Translation: AAC76898.1.
AP009048 Genomic DNA. Translation: BAE77394.1.
PIRiG65197. KIECFA.
RefSeqiNP_418351.1. NC_000913.3.
WP_000591795.1. NZ_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAC76898; AAC76898; b3916.
BAE77394; BAE77394; BAE77394.
GeneIDi948412.
KEGGiecj:JW3887.
eco:b3916.
PATRICi32123343. VBIEscCol129921_4032.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X02519 Genomic DNA. Translation: CAA26356.1.
L19201 Genomic DNA. Translation: AAB03048.1.
U00096 Genomic DNA. Translation: AAC76898.1.
AP009048 Genomic DNA. Translation: BAE77394.1.
PIRiG65197. KIECFA.
RefSeqiNP_418351.1. NC_000913.3.
WP_000591795.1. NZ_LN832404.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1PFKX-ray2.40A/B1-320[»]
2PFKX-ray2.40A/B/C/D1-320[»]
ProteinModelPortaliP0A796.
SMRiP0A796.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4261224. 4 interactors.
DIPiDIP-35841N.
IntActiP0A796. 7 interactors.
MINTiMINT-1322275.
STRINGi511145.b3916.

2D gel databases

SWISS-2DPAGEP0A796.

Proteomic databases

EPDiP0A796.
PaxDbiP0A796.
PRIDEiP0A796.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC76898; AAC76898; b3916.
BAE77394; BAE77394; BAE77394.
GeneIDi948412.
KEGGiecj:JW3887.
eco:b3916.
PATRICi32123343. VBIEscCol129921_4032.

Organism-specific databases

EchoBASEiEB0693.
EcoGeneiEG10699. pfkA.

Phylogenomic databases

eggNOGiENOG4105CTQ. Bacteria.
COG0205. LUCA.
HOGENOMiHOG000248870.
InParanoidiP0A796.
KOiK00850.
OMAiAIITICE.
PhylomeDBiP0A796.

Enzyme and pathway databases

UniPathwayiUPA00109; UER00182.
BioCyciEcoCyc:6PFK-1-MONOMER.
ECOL316407:JW3887-MONOMER.
MetaCyc:6PFK-1-MONOMER.
BRENDAi2.7.1.11. 2026.
SABIO-RKP0A796.

Miscellaneous databases

EvolutionaryTraceiP0A796.
PROiP0A796.

Family and domain databases

CDDicd00763. Bacterial_PFK. 1 hit.
HAMAPiMF_00339. Phosphofructokinase_I_B1. 1 hit.
InterProiIPR022953. ATP_PFK.
IPR012003. ATP_PFK_prok-type.
IPR012828. PFKA_ATP_prok.
IPR015912. Phosphofructokinase_CS.
IPR000023. Phosphofructokinase_dom.
[Graphical view]
PfamiPF00365. PFK. 1 hit.
[Graphical view]
PIRSFiPIRSF000532. ATP_PFK_prok. 1 hit.
PRINTSiPR00476. PHFRCTKINASE.
SUPFAMiSSF53784. SSF53784. 1 hit.
TIGRFAMsiTIGR02482. PFKA_ATP. 1 hit.
PROSITEiPS00433. PHOSPHOFRUCTOKINASE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiPFKA_ECOLI
AccessioniPrimary (citable) accession number: P0A796
Secondary accession number(s): P06998, Q2M8L2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1988
Last sequence update: June 7, 2005
Last modified: November 30, 2016
This is version 109 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Allosteric enzyme, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.