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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.

Catalytic activityi

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

Cofactori

Enzyme regulationi

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

Pathway:iglycolysis

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)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei12 – 121ATP; via amide nitrogen
Metal bindingi104 – 1041Magnesium; catalyticUniRule annotation1 Publication
Active sitei128 – 1281Proton acceptorUniRule annotation2 Publications
Binding sitei155 – 1551Allosteric activator ADPUniRule annotation1 Publication
Binding sitei163 – 1631Substrate; shared with dimeric partner
Binding sitei212 – 2121Allosteric activator ADPUniRule annotation
Binding sitei223 – 2231Substrate
Binding sitei244 – 2441Substrate; shared with dimeric partner

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi73 – 742ATP
Nucleotide bindingi103 – 1064ATP

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

  • carbohydrate phosphorylation Source: GOC
  • cellular carbohydrate catabolic process Source: EcoliWiki
  • fructose 6-phosphate metabolic process Source: InterPro
  • glucose catabolic process Source: EcoliWiki
  • glycolytic process Source: EcoliWiki
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 lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
ProteomesiUP000000318 Componenti: Chromosome UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG10699. pfkA.

Subcellular locationi

GO - Cellular componenti

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

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi128 – 1281D → S: 18000-fold reduction of catalytic rate. 1 Publication
Mutagenesisi172 – 1721R → S: 3.4-fold reduction in turnover numbers. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 320320ATP-dependent 6-phosphofructokinase isozyme 1PRO_0000111950Add
BLAST

Proteomic databases

PaxDbiP0A796.
PRIDEiP0A796.

2D gel databases

SWISS-2DPAGEP0A796.

Interactioni

Subunit structurei

Homotetramer.UniRule annotation1 Publication

Protein-protein interaction databases

DIPiDIP-35841N.
IntActiP0A796. 7 interactions.
MINTiMINT-1322275.
STRINGi511145.b3916.

Structurei

Secondary structure

1
320
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi4 – 96Combined sources
Helixi17 – 3014Combined sources
Beta strandi34 – 396Combined sources
Helixi41 – 466Combined sources
Beta strandi50 – 534Combined sources
Helixi56 – 583Combined sources
Helixi75 – 784Combined sources
Helixi80 – 9213Combined sources
Beta strandi97 – 1026Combined sources
Helixi104 – 11512Combined sources
Beta strandi120 – 1256Combined sources
Helixi140 – 16122Combined sources
Beta strandi164 – 1696Combined sources
Helixi176 – 1849Combined sources
Beta strandi188 – 1914Combined sources
Helixi199 – 21113Combined sources
Beta strandi217 – 22610Combined sources
Helixi228 – 23912Combined sources
Beta strandi243 – 2475Combined sources
Helixi249 – 2535Combined sources
Helixi259 – 27719Combined sources
Beta strandi282 – 2887Combined sources
Beta strandi291 – 2966Combined sources
Helixi297 – 3037Combined sources
Helixi310 – 31910Combined sources

3D structure databases

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

Miscellaneous databases

EvolutionaryTraceiP0A796.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni22 – 265Allosteric activator ADP binding; shared with dimeric partner
Regioni55 – 606Allosteric activator ADP binding; shared with dimeric partner
Regioni126 – 1283Substrate binding
Regioni170 – 1723Substrate binding
Regioni186 – 1883Allosteric activator ADP binding
Regioni214 – 2163Allosteric activator ADP binding
Regioni250 – 2534Substrate binding

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

eggNOGiCOG0205.
HOGENOMiHOG000248870.
InParanoidiP0A796.
KOiK00850.
OMAiGFGGRCV.
OrthoDBiEOG644ZRM.
PhylomeDBiP0A796.

Family and domain databases

HAMAPiMF_00339. Phosphofructokinase_I_B1.
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)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti74 – 741F → C in CAA26356 (PubMed:3158524).Curated
Sequence conflicti103 – 1042GD → DG in CAA26356 (PubMed:3158524).Curated
Sequence conflicti163 – 1631R → P in CAA26356 (PubMed:3158524).Curated
Sequence conflicti317 – 3193KKL → EKM in CAA26356 (PubMed:3158524).Curated

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_CP010445.1.

Genome annotation databases

EnsemblBacteriaiAAC76898; AAC76898; b3916.
BAE77394; BAE77394; BAE77394.
GeneIDi948412.
KEGGieco: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_CP010445.1.

3D structure databases

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

Protein-protein interaction databases

DIPiDIP-35841N.
IntActiP0A796. 7 interactions.
MINTiMINT-1322275.
STRINGi511145.b3916.

2D gel databases

SWISS-2DPAGEP0A796.

Proteomic databases

PaxDbiP0A796.
PRIDEiP0A796.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC76898; AAC76898; b3916.
BAE77394; BAE77394; BAE77394.
GeneIDi948412.
KEGGieco:b3916.
PATRICi32123343. VBIEscCol129921_4032.

Organism-specific databases

EchoBASEiEB0693.
EcoGeneiEG10699. pfkA.

Phylogenomic databases

eggNOGiCOG0205.
HOGENOMiHOG000248870.
InParanoidiP0A796.
KOiK00850.
OMAiGFGGRCV.
OrthoDBiEOG644ZRM.
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

HAMAPiMF_00339. Phosphofructokinase_I_B1.
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...

Publicationsi

« Hide 'large scale' publications
  1. "Nucleotide sequence and high-level expression of the major Escherichia coli phosphofructokinase."
    Hellinga H.W., Evans P.R.
    Eur. J. Biochem. 149:363-373(1985) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "Mutations in the active site of Escherichia coli phosphofructokinase."
    Hellinga H.W., Evans P.R.
    Nature 327:437-439(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: SEQUENCE REVISION, ACTIVE SITE, MUTAGENESIS OF ASP-128 AND ARG-172.
  3. "Analysis of the Escherichia coli genome. III. DNA sequence of the region from 87.2 to 89.2 minutes."
    Plunkett G. III, Burland V., Daniels D.L., Blattner F.R.
    Nucleic Acids Res. 21:3391-3398(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  5. "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
    Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
    Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  6. "A role of RnlA in the RNase LS activity from Escherichia coli."
    Otsuka Y., Koga M., Iwamoto A., Yonesaki T.
    Genes Genet. Syst. 82:291-299(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 1-8.
    Strain: K12.
  7. "Escherichia coli proteome analysis using the gene-protein database."
    VanBogelen R.A., Abshire K.Z., Moldover B., Olson E.R., Neidhardt F.C.
    Electrophoresis 18:1243-1251(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY 2D-GEL.
  8. "Crystal structure of the complex of phosphofructokinase from Escherichia coli with its reaction products."
    Shirakihara Y., Evans P.R.
    J. Mol. Biol. 204:973-994(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.40 ANGSTROMS) IN COMPLEX WITH MAGNESIUM; ADP; FRUCTOSE 1,6-BISPHOSPHATE AND ALLOSTERIC ACTIVATOR, ACTIVE SITE.
  9. "Crystal structure of unliganded phosphofructokinase from Escherichia coli."
    Rypniewski W.R., Evans P.R.
    J. Mol. Biol. 207:805-821(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS).

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: July 22, 2015
This is version 99 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

External Data

Dasty 3

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 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.