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P00512 (PFKA_GEOSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 122. 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
Synonyms:pfk
OrganismGeobacillus stearothermophilus (Bacillus stearothermophilus)
Taxonomic identifier1422 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliBacillalesBacillaceaeGeobacillus

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.4

Catalytic activity

ATP + D-fructose 6-phosphate = ADP + D-fructose 1,6-bisphosphate. Ref.4

Cofactor

Magnesium By similarity. HAMAP-Rule MF_00339

Enzyme regulation

Allosterically activated by ADP and other diphosphonucleosides, and allosterically inhibited by phosphoenolpyruvate. HAMAP-Rule MF_00339

Pathway

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

Subunit structure

Homotetramer.

Subcellular location

Cytoplasm HAMAP-Rule MF_00339.

Miscellaneous

In the R state the 6-P group of fructose 6-phosphate (F6P) is bound by His-249 from one chain and Arg-162 and Arg-243 from an adjacent chain. In the T state a conformation change moves Arg-162 away from the substrate. Glu-161 takes its place, hence repelling the phosphate of ATP.

The phosphate group of phosphoenolpyruvate appears to bind in the same place as the beta-phosphate group of ADP.

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=0.07 mM for ATP Ref.4

KM=0.033 mM for fructose 6-phosphate

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 319319ATP-dependent 6-phosphofructokinase HAMAP-Rule MF_00339
PRO_0000111935

Regions

Nucleotide binding72 – 732ATP HAMAP-Rule MF_00339
Nucleotide binding102 – 1054ATP HAMAP-Rule MF_00339
Region21 – 255Allosteric activator ADP binding; shared with dimeric partner HAMAP-Rule MF_00339
Region125 – 1273Substrate binding HAMAP-Rule MF_00339
Region169 – 1713Substrate binding HAMAP-Rule MF_00339
Region185 – 1873Allosteric activator ADP binding HAMAP-Rule MF_00339
Region213 – 2153Allosteric activator ADP binding HAMAP-Rule MF_00339
Region249 – 2524Substrate binding HAMAP-Rule MF_00339

Sites

Active site1271Proton acceptor
Metal binding1031Magnesium; catalytic By similarity
Binding site111ATP; via amide nitrogen
Binding site591Allosteric activator ADP; shared with dimeric partner
Binding site1541Allosteric activator ADP
Binding site1621Substrate; shared with dimeric partner
Binding site2111Allosteric activator ADP
Binding site2221Substrate
Binding site2431Substrate; shared with dimeric partner

Experimental info

Sequence conflict121D → N AA sequence Ref.2
Sequence conflict35 – 373Missing AA sequence Ref.2
Sequence conflict431G → V AA sequence Ref.2
Sequence conflict821Q → E AA sequence Ref.2
Sequence conflict951E → Q AA sequence Ref.2
Sequence conflict2251G → L AA sequence Ref.2

Secondary structure

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

Details...

Sequences

Sequence LengthMass (Da)Tools
P00512 [UniParc].

Last modified July 1, 1989. Version 2.
Checksum: EE968D39BA30712B

FASTA31934,119
        10         20         30         40         50         60 
MKRIGVLTSG GDSPGMNAAI RSVVRKAIYH GVEVYGVYHG YAGLIAGNIK KLEVGDVGDI 

        70         80         90        100        110        120 
IHRGGTILYT ARCPEFKTEE GQKKGIEQLK KHGIEGLVVI GGDGSYQGAK KLTEHGFPCV 

       130        140        150        160        170        180 
GVPGTIDNDI PGTDFTIGFD TALNTVIDAI DKIRDTATSH ERTYVIEVMG RHAGDIALWS 

       190        200        210        220        230        240 
GLAGGAETIL IPEADYDMND VIARLKRGHE RGKKHSIIIV AEGVGSGVDF GRQIQEATGF 

       250        260        270        280        290        300 
ETRVTVLGHV QRGGSPTAFD RVLASRLGAR AVELLLEGKG GRCVGIQNNQ LVDHDIAEAL 

       310 
ANKHTIDQRM YALSKELSI 

« Hide

References

[1]"Nucleotide sequence of the phosphofructokinase gene from Bacillus stearothermophilus and comparison with the homologous Escherichia coli gene."
French B.A., Chang S.H.
Gene 54:65-71(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"Phosphofructokinase: complete amino-acid sequence of the enzyme from Bacillus stearothermophilus."
Kolb E., Hudson P.J., Harris J.I.
Eur. J. Biochem. 108:587-597(1980) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE.
[3]"Molecular cloning and nucleotide sequence of the gene for pyruvate kinase of Bacillus stearothermophilus and the production of the enzyme in Escherichia coli. Evidence that the genes for phosphofructokinase and pyruvate kinase constitute an operon."
Sakai H., Ohta T.
Eur. J. Biochem. 211:851-859(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 300-319.
[4]"Kinetic characteristics of phosphofructokinase from Bacillus stearothermophilus: MgATP nonallosterically inhibits the enzyme."
Byrnes M., Zhu X., Younathan E.S., Chang S.H.
Biochemistry 33:3424-3431(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES.
[5]"Structure and control of phosphofructokinase from Bacillus stearothermophilus."
Evans P.R., Hudson P.J.
Nature 279:500-504(1979) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS).
[6]"Phosphofructokinase: structure and control."
Evans P.R., Farrants G.W., Hudson P.J.
Philos. Trans. R. Soc. Lond., B, Biol. Sci. 293:53-62(1981) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) IN COMPLEX WITH MAGNESIUM; ADP AND FRUCTOSE-6-PHOSPHATE.
[7]"Structural basis of the allosteric behaviour of phosphofructokinase."
Schirmer T., Evans P.R.
Nature 343:140-145(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) IN COMPLEX WITH ALLOSTERIC INHIBITOR.
[8]"Reversible ligand-induced dissociation of a tryptophan-shift mutant of phosphofructokinase from Bacillus stearothermophilus."
Riley-Lovingshimer M.R., Ronning D.R., Sacchettini J.C., Reinhart G.D.
Biochemistry 41:12967-12974(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (3.2 ANGSTROMS) IN COMPLEX WITH FRUCTOSE-6-PHOSPHATE.
[9]"Structure of the apo form of Bacillus stearothermophilus phosphofructokinase."
Mosser R., Reddy M.C., Bruning J.B., Sacchettini J.C., Reinhart G.D.
Biochemistry 51:769-775(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.79 ANGSTROMS).
[10]"Redefining the role of the quaternary shift in Bacillus stearothermophilus phosphofructokinase."
Mosser R., Reddy M.C., Bruning J.B., Sacchettini J.C., Reinhart G.D.
Biochemistry 52:5421-5429(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) IN COMPLEX WITH PHOSPHOENOLPYRUVIC ACID.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M15643 Genomic DNA. Translation: AAA22656.1.
D13095 Genomic DNA. Translation: BAA02405.1.
PIRKIBSFF. A27474.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1MTOX-ray3.20A/B/C/D/E/F/G/H1-319[»]
3PFKX-ray2.40A1-319[»]
3U39X-ray2.79A/B/C/D1-319[»]
4I36X-ray2.30A/B/C/D1-319[»]
4I4IX-ray2.49A/B/C/D1-319[»]
4I7EX-ray2.00A/B/C/D1-319[»]
4PFKX-ray2.40A1-319[»]
6PFKX-ray2.60A/B/C/D1-319[»]
ProteinModelPortalP00512.
SMRP00512. Positions 1-319.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Enzyme and pathway databases

SABIO-RKP00512.
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

EvolutionaryTraceP00512.

Entry information

Entry namePFKA_GEOSE
AccessionPrimary (citable) accession number: P00512
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 1, 1989
Last modified: July 9, 2014
This is version 122 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