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P80019 (PFKA_LACDE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 93. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
ATP-dependent 6-phosphofructokinase

Short name=ATP-PFK
Short name=Phosphofructokinase
EC=2.7.1.11
Alternative name(s):
Phosphohexokinase
Gene names
Name:pfkA
OrganismLactobacillus delbrueckii subsp. bulgaricus
Taxonomic identifier1585 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliLactobacillalesLactobacillaceaeLactobacillus

Protein attributes

Sequence length319 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Catalyzes the phosphorylation of D-fructose 6-phosphate to fructose 1,6-bisphosphate by ATP, the first committing step of glycolysis. Ref.2

Catalytic activity

ATP + D-fructose 6-phosphate = ADP + D-fructose 1,6-bisphosphate. HAMAP-Rule MF_00339

Cofactor

Magnesium By similarity. HAMAP-Rule MF_00339

Enzyme regulation

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. Ref.2 Ref.3

Pathway

Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-phosphate and glycerone phosphate from D-glucose: step 3/4. HAMAP-Rule MF_00339

Subunit structure

Homotetramer. Ref.2

Subcellular location

Cytoplasm Ref.2.

Sequence similarities

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

Biophysicochemical properties

Kinetic parameters:

KM=0.2 mM for ATP (at pH 8.2) Ref.2

KM=0.07 mM for ATP (at pH 6.0)

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 dependence:

Optimum pH is 8.2.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 319319ATP-dependent 6-phosphofructokinase HAMAP-Rule MF_00339
PRO_0000111957

Regions

Nucleotide binding72 – 732ATP By similarity
Nucleotide binding102 – 1054ATP By similarity
Region21 – 255Allosteric activator ADP binding; shared with dimeric partner By similarity
Region125 – 1273Substrate binding By similarity
Region169 – 1713Substrate binding By similarity
Region185 – 1873Allosteric activator ADP binding By similarity
Region213 – 2153Allosteric activator ADP binding By similarity
Region249 – 2524Substrate binding By similarity

Sites

Active site1271Proton acceptor By similarity
Metal binding1031Magnesium; catalytic By similarity
Binding site111ATP; via amide nitrogen By similarity
Binding site1541Allosteric activator ADP By similarity
Binding site1621Substrate; shared with dimeric partner By similarity
Binding site2221Substrate By similarity
Binding site2431Substrate; shared with dimeric partner By similarity

Secondary structure

.................................................... 319
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P80019 [UniParc].

Last modified June 1, 1994. Version 2.
Checksum: 555C5FE1D522BC9C

FASTA31934,009
        10         20         30         40         50         60 
MKRIGILTSG GDAPGMNAAV RAVTRVAIAN GLEVFGIRYG FAGLVAGDIF PLESEDVAHL 

        70         80         90        100        110        120 
INVSGTFLYS ARYPEFAEEE GQLAGIEQLK KHGIDAVVVI GGDGSYHGAL QLTRHGFNSI 

       130        140        150        160        170        180 
GLPGTIDNDI PYTDATIGYD TACMTAMDAI DKIRDTASSH HRVFIVNVMG RNCGDIAMRV 

       190        200        210        220        230        240 
GVACGADAIV IPERPYDVEE IANRLKQAQE SGKDHGLVVV AEGVMTADQF MAELKKYGDF 

       250        260        270        280        290        300 
DVRANVLGHM QRGGTPTVSD RVLASKLGSE AVHLLLEGKG GLAVGIENGK VTSHDILDLF 

       310 
DESHRGDYDL LKLNADLSR 

« Hide

References

[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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X71403 Genomic DNA. Translation: CAA50526.1.
PIRS35928. A48663.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1ZXXX-ray1.85A1-319[»]
ProteinModelPortalP80019.
SMRP80019. Positions 1-319.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Enzyme and pathway databases

SABIO-RKP80019.
UniPathwayUPA00109; UER00182.

Family and domain databases

HAMAPMF_00339. Phosphofructokinase_I_B1.
InterProIPR012003. ATP_PFK_prok.
IPR012828. PFKA_ATP.
IPR022953. Phosphofructokinase.
IPR015912. Phosphofructokinase_CS.
IPR000023. Phosphofructokinase_dom.
[Graphical view]
PfamPF00365. PFK. 1 hit.
[Graphical view]
PIRSFPIRSF000532. ATP_PFK_prok. 1 hit.
PRINTSPR00476. PHFRCTKINASE.
SUPFAMSSF53784. SSF53784. 1 hit.
TIGRFAMsTIGR02482. PFKA_ATP. 1 hit.
PROSITEPS00433. PHOSPHOFRUCTOKINASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP80019.

Entry information

Entry namePFKA_LACDE
AccessionPrimary (citable) accession number: P80019
Entry history
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 statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways