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P80019

- PFKA_LACDE

UniProt

P80019 - PFKA_LACDE

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Protein
ATP-dependent 6-phosphofructokinase
Gene
pfkA
Organism
Lactobacillus delbrueckii subsp. bulgaricus
Status
Reviewed - 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.1 Publication

Catalytic activityi

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

Cofactori

Magnesium By similarity.UniRule annotation

Enzyme regulationi

Allosterically activated by ADP and other diphosphonucleosides, and allosterically inhibited by phosphoenolpyruvate. The binding affinities for these effectors are decreased however, and therefore the allosteric effect becomes apparent only at high effector concentrations.2 Publications

Kineticsi

  1. KM=0.2 mM for ATP (at pH 8.2)1 Publication
  2. KM=0.07 mM for ATP (at pH 6.0)
  3. KM=0.3 mM for fructose 6-phosphate (at pH 6.0 and 8.2)

Vmax=90 µmol/min/mg enzyme (at pH 8.2)

pH dependencei

Optimum pH is 8.2.

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei11 – 111ATP; via amide nitrogen By similarity
Metal bindingi103 – 1031Magnesium; catalytic By similarity
Active sitei127 – 1271Proton acceptor By similarity
Binding sitei154 – 1541Allosteric activator ADP By similarity
Binding sitei162 – 1621Substrate; shared with dimeric partner By similarity
Binding sitei222 – 2221Substrate By similarity
Binding sitei243 – 2431Substrate; shared with dimeric partner By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi72 – 732ATP By similarity
Nucleotide bindingi102 – 1054ATP By similarity

GO - Molecular functioni

  1. 6-phosphofructokinase activity Source: UniProtKB-HAMAP
  2. ATP binding Source: UniProtKB-KW
  3. metal ion binding Source: UniProtKB-KW
Complete GO annotation...

GO - Biological processi

  1. fructose 6-phosphate metabolic process Source: InterPro
  2. glycolytic process Source: UniProtKB-HAMAP
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

SABIO-RKP80019.
UniPathwayiUPA00109; UER00182.

Names & Taxonomyi

Protein namesi
Recommended name:
ATP-dependent 6-phosphofructokinase (EC:2.7.1.11)
Short name:
ATP-PFK
Short name:
Phosphofructokinase
Alternative name(s):
Phosphohexokinase
Gene namesi
Name:pfkA
OrganismiLactobacillus delbrueckii subsp. bulgaricus
Taxonomic identifieri1585 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliLactobacillalesLactobacillaceaeLactobacillus

Subcellular locationi

Cytoplasm 1 Publication

GO - Cellular componenti

  1. 6-phosphofructokinase complex Source: InterPro
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 319319ATP-dependent 6-phosphofructokinaseUniRule annotation
PRO_0000111957Add
BLAST

Interactioni

Subunit structurei

Homotetramer.1 Publication

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi3 – 86
Helixi16 – 2813
Turni29 – 313
Beta strandi33 – 375
Helixi40 – 467
Beta strandi49 – 513
Helixi54 – 574
Helixi74 – 763
Helixi79 – 9113
Beta strandi96 – 1016
Helixi103 – 11412
Beta strandi119 – 1257
Helixi139 – 15921
Beta strandi163 – 1686
Helixi175 – 1839
Beta strandi187 – 1904
Helixi198 – 21013
Beta strandi216 – 2216
Turni222 – 2243
Helixi227 – 23610
Beta strandi242 – 2465
Helixi248 – 2525
Helixi258 – 27619
Beta strandi281 – 2877
Beta strandi290 – 2956
Helixi296 – 2994
Helixi309 – 3179

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1ZXXX-ray1.85A1-319[»]
ProteinModelPortaliP80019.
SMRiP80019. Positions 1-319.

Miscellaneous databases

EvolutionaryTraceiP80019.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni21 – 255Allosteric activator ADP binding; shared with dimeric partner By similarity
Regioni125 – 1273Substrate binding By similarity
Regioni169 – 1713Substrate binding By similarity
Regioni185 – 1873Allosteric activator ADP binding By similarity
Regioni213 – 2153Allosteric activator ADP binding By similarity
Regioni249 – 2524Substrate binding By similarity

Sequence similaritiesi

Family and domain databases

HAMAPiMF_00339. Phosphofructokinase_I_B1.
InterProiIPR012003. ATP_PFK_prok.
IPR012828. PFKA_ATP.
IPR022953. Phosphofructokinase.
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.

P80019-1 [UniParc]FASTAAdd to Basket

« Hide

MKRIGILTSG GDAPGMNAAV RAVTRVAIAN GLEVFGIRYG FAGLVAGDIF    50
PLESEDVAHL INVSGTFLYS ARYPEFAEEE GQLAGIEQLK KHGIDAVVVI 100
GGDGSYHGAL QLTRHGFNSI GLPGTIDNDI PYTDATIGYD TACMTAMDAI 150
DKIRDTASSH HRVFIVNVMG RNCGDIAMRV GVACGADAIV IPERPYDVEE 200
IANRLKQAQE SGKDHGLVVV AEGVMTADQF MAELKKYGDF DVRANVLGHM 250
QRGGTPTVSD RVLASKLGSE AVHLLLEGKG GLAVGIENGK VTSHDILDLF 300
DESHRGDYDL LKLNADLSR 319
Length:319
Mass (Da):34,009
Last modified:June 1, 1994 - v2
Checksum:i555C5FE1D522BC9C
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X71403 Genomic DNA. Translation: CAA50526.1.
PIRiA48663. S35928.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X71403 Genomic DNA. Translation: CAA50526.1 .
PIRi A48663. S35928.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1ZXX X-ray 1.85 A 1-319 [» ]
ProteinModelPortali P80019.
SMRi P80019. Positions 1-319.
ModBasei Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Enzyme and pathway databases

UniPathwayi UPA00109 ; UER00182 .
SABIO-RK P80019.

Miscellaneous databases

EvolutionaryTracei P80019.

Family and domain databases

HAMAPi MF_00339. Phosphofructokinase_I_B1.
InterProi IPR012003. ATP_PFK_prok.
IPR012828. PFKA_ATP.
IPR022953. Phosphofructokinase.
IPR015912. Phosphofructokinase_CS.
IPR000023. Phosphofructokinase_dom.
[Graphical view ]
Pfami PF00365. PFK. 1 hit.
[Graphical view ]
PIRSFi PIRSF000532. ATP_PFK_prok. 1 hit.
PRINTSi PR00476. PHFRCTKINASE.
SUPFAMi SSF53784. SSF53784. 1 hit.
TIGRFAMsi TIGR02482. PFKA_ATP. 1 hit.
PROSITEi PS00433. PHOSPHOFRUCTOKINASE. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. "Cloning, sequencing, and expression in Escherichia coli of the gene coding for phosphofructokinase in Lactobacillus bulgaricus."
    Branny P., de la Torre F., Garel J.R.
    J. Bacteriol. 175:5344-5349(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "Purification and properties of the phosphofructokinase from Lactobacillus bulgaricus. A non-allosteric analog of the enzyme from Escherichia coli."
    le Bras G., Deville-Bonne D., Garel J.R.
    Eur. J. Biochem. 198:683-687(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 1-38, FUNCTION, SUBCELLULAR LOCATION, SUBUNIT, BIOPHYSICOCHEMICAL PROPERTIES, ENZYME REGULATION.
    Strain: B107.
  3. "Kinetic and structural characterization of phosphofructokinase from Lactobacillus bulgaricus."
    Paricharttanakul N.M., Ye S., Menefee A.L., Javid-Majd F., Sacchettini J.C., Reinhart G.D.
    Biochemistry 44:15280-15286(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS), ENZYME REGULATION.
    Strain: B107.

Entry informationi

Entry nameiPFKA_LACDE
AccessioniPrimary (citable) accession number: P80019
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 1, 1991
Last sequence update: June 1, 1994
Last modified: July 9, 2014
This is version 93 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Allosteric enzyme, Direct protein sequencing

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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