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P70826 (PFP_BORBU) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 76. 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:
Pyrophosphate--fructose 6-phosphate 1-phosphotransferase

EC=2.7.1.90
Alternative name(s):
6-phosphofructokinase, pyrophosphate dependent
PPi-dependent phosphofructokinase
Short name=PPi-PFK
Pyrophosphate-dependent 6-phosphofructose-1-kinase
Gene names
Name:pfp
Synonyms:PFK2, pfpB
Ordered Locus Names:BB_0020
OrganismBorrelia burgdorferi (strain ATCC 35210 / B31 / CIP 102532 / DSM 4680) [Reference proteome] [HAMAP]
Taxonomic identifier224326 [NCBI]
Taxonomic lineageBacteriaSpirochaetesSpirochaetalesSpirochaetaceaeBorreliaBorrelia burgdorferi group

Protein attributes

Sequence length555 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Catalyzes the phosphorylation of D-fructose 6-phosphate, the first committing step of glycolysis. Uses inorganic phosphate (PPi) as phosphoryl donor instead of ATP like common ATP-dependent phosphofructokinases (ATP-PFKs), which renders the reaction reversible, and can thus function both in glycolysis and gluconeogenesis. Consistently, PPi-PFK can replace the enzymes of both the forward (ATP-PFK) and reverse (fructose-bisphosphatase (FBPase)) reactions. Ref.3

Catalytic activity

Diphosphate + D-fructose 6-phosphate = phosphate + D-fructose 1,6-bisphosphate. Ref.3

Cofactor

Magnesium By similarity. HAMAP-Rule MF_01980

Enzyme regulation

Non-allosteric By similarity. HAMAP-Rule MF_01980

Pathway

Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-phosphate and glycerone phosphate from D-glucose: step 3/4. HAMAP-Rule MF_01980

Subunit structure

Homodimer. Ref.3

Subcellular location

Cytoplasm By similarity HAMAP-Rule MF_01980.

Sequence similarities

Belongs to the phosphofructokinase type A (PFKA) family. PPi-dependent PFK group II subfamily. Clade "Long" sub-subfamily.

Biophysicochemical properties

Kinetic parameters:

KM=15 µM for diphosphate Ref.3

KM=109 µM for D-fructose 6-phosphate

pH dependence:

Optimum pH is 6.4-7.2.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 555555Pyrophosphate--fructose 6-phosphate 1-phosphotransferase HAMAP-Rule MF_01980
PRO_0000428943

Regions

Region203 – 2064Substrate binding HAMAP-Rule MF_01980
Region204 – 2063Substrate binding By similarity
Region243 – 2442Substrate binding; shared with dimeric partner HAMAP-Rule MF_01980
Region251 – 2533Substrate binding HAMAP-Rule MF_01980
Region428 – 4314Substrate binding HAMAP-Rule MF_01980

Sites

Active site2061Proton acceptor By similarity
Metal binding1761Magnesium; catalytic By similarity
Binding site821Diphosphate; via amide nitrogen
Binding site1461Substrate
Binding site3121Substrate
Site1771Important for catalytic activity and substrate specificity; stabilizes the transition state when the phosphoryl donor is PPi; prevents ATP from binding by mimicking the alpha-phosphate group of ATP
Site2031Important for catalytic activity; stabilizes the transition state when the phosphoryl donor is PPi

Secondary structure

...................................................................................... 555
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P70826 [UniParc].

Last modified November 1, 1998. Version 2.
Checksum: 0FEAC1077DA6127F

FASTA55562,443
        10         20         30         40         50         60 
MNTSLFKQER QKYIPKLPNI LKKDFNNISL VYGENTEAIQ DRQALKEFFK NTYGLPIISF 

        70         80         90        100        110        120 
TEGESSLSFS KALNIGIILS GGPAPGGHNV ISGVFDAIKK FNPNSKLFGF KGGPLGLLEN 

       130        140        150        160        170        180 
DKIELTESLI NSYRNTGGFD IVSSGRTKIE TEEHYNKALF VAKENNLNAI IIIGGDDSNT 

       190        200        210        220        230        240 
NAAILAEYFK KNGENIQVIG VPKTIDADLR NDHIEISFGF DSATKIYSEL IGNLCRDAMS 

       250        260        270        280        290        300 
TKKYWHFVKL MGRSASHVAL ECALKTHPNI CIVSEEVLAK KKTLSEIIDE MVSVILKRSL 

       310        320        330        340        350        360 
NGDNFGVVIV PEGLIEFIPE VKSLMLELCD IFDKNEGEFK GLNIEKMKEI FVAKLSDYMK 

       370        380        390        400        410        420 
GVYLSLPLFI QFELIKSILE RDPHGNFNVS RVPTEKLFIE MIQSRLNDMK KRGEYKGSFT 

       430        440        450        460        470        480 
PVDHFFGYEG RSAFPSNFDS DYCYSLGYNA VVLILNGLTG YMSCIKNLNL KPTDWIAGGV 

       490        500        510        520        530        540 
PLTMLMNMEE RYGEKKPVIK KALVDLEGRP FKEFVKNRDK WALNNLYLYP GPVQYFGSSE 

       550 
IVDEITETLK LELLK 

« Hide

References

« Hide 'large scale' references
[1]"Homologues of helicase genes priA and ruvAB of Borrelia burgdorferi, the Lyme borreliosis agent."
Boursaux-Eude C., Margarita D., Belfaiza J., Old I.G., Saint-Girons I.
Res. Microbiol. 149:235-245(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: HB19.
[2]"Genomic sequence of a Lyme disease spirochaete, Borrelia burgdorferi."
Fraser C.M., Casjens S., Huang W.M., Sutton G.G., Clayton R.A., Lathigra R., White O., Ketchum K.A., Dodson R.J., Hickey E.K., Gwinn M.L., Dougherty B.A., Tomb J.-F., Fleischmann R.D., Richardson D.L., Peterson J.D., Kerlavage A.R., Quackenbush J. expand/collapse author list , Salzberg S.L., Hanson M., van Vugt R., Palmer N., Adams M.D., Gocayne J.D., Weidman J.F., Utterback T.R., Watthey L., McDonald L.A., Artiach P., Bowman C., Garland S.A., Fujii C., Cotton M.D., Horst K., Roberts K.M., Hatch B., Smith H.O., Venter J.C.
Nature 390:580-586(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 35210 / B31 / CIP 102532 / DSM 4680.
[3]"Expression, characterization, and crystallization of the pyrophosphate-dependent phosphofructo-1-kinase of Borrelia burgdorferi."
Deng Z., Roberts D., Wang X., Kemp R.G.
Arch. Biochem. Biophys. 371:326-331(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT.
[4]"The structure of a pyrophosphate-dependent phosphofructokinase from the Lyme disease spirochete Borrelia burgdorferi."
Moore S.A., Ronimus R.S., Roberson R.S., Morgan H.W.
Structure 10:659-671(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.55 ANGSTROMS) OF 1-553.
[5]"Crystal structure of a novel fructose 1,6-bisphosphate and AlF(3) containing pyrophosphate-dependent phosphofructo-1-kinase complex from Borrelia burgdorferi."
Wang M., Grum-Tokars V.
Submitted (NOV-2005) to the PDB data bank
Cited for: X-RAY CRYSTALLOGRAPHY (2.11 ANGSTROMS) OF 1-553 IN COMPLEX WITH SUBSTRATE.
Strain: ATCC 35210 / B31 / CIP 102532 / DSM 4680.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AJ224475 Genomic DNA. Translation: CAA11968.1.
AE000783 Genomic DNA. No translation available.
PIRD70102.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1KZHX-ray2.55A/B1-553[»]
2F48X-ray2.11A/B1-553[»]
ProteinModelPortalP70826.
SMRP70826. Positions 4-553.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Enzyme and pathway databases

UniPathwayUPA00109; UER00182.

Family and domain databases

Gene3D1.10.10.480. 1 hit.
HAMAPMF_01980. Phosphofructokinase_II_Long.
InterProIPR011183. PfpB_PPi_PFK.
IPR022953. Phosphofructokinase.
IPR000023. Phosphofructokinase_dom.
IPR013981. PPi-dep_PFK_a-hlx.
[Graphical view]
PfamPF00365. PFK. 1 hit.
[Graphical view]
PIRSFPIRSF005677. PPi_PFK_PfpB. 1 hit.
PRINTSPR00476. PHFRCTKINASE.
SUPFAMSSF53784. SSF53784. 1 hit.
TIGRFAMsTIGR02477. PFKA_PPi. 1 hit.
ProtoNetSearch...

Entry information

Entry namePFP_BORBU
AccessionPrimary (citable) accession number: P70826
Entry history
Integrated into UniProtKB/Swiss-Prot: May 14, 2014
Last sequence update: November 1, 1998
Last modified: July 9, 2014
This is version 76 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