Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Pyrophosphate--fructose 6-phosphate 1-phosphotransferase

Gene

pfp

Organism
Borrelia burgdorferi (strain ATCC 35210 / B31 / CIP 102532 / DSM 4680)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.UniRule annotation1 Publication

Catalytic activityi

Diphosphate + D-fructose 6-phosphate = phosphate + D-fructose 1,6-bisphosphate.UniRule annotation1 Publication

Cofactori

Mg2+UniRule annotation

Enzyme regulationi

Non-allosteric.UniRule annotation

Kineticsi

  1. KM=15 µM for diphosphate1 Publication
  2. KM=109 µM for D-fructose 6-phosphate1 Publication

    pH dependencei

    Optimum pH is 6.4-7.2.1 Publication

    Pathway: glycolysis

    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. Pyrophosphate--fructose 6-phosphate 1-phosphotransferase (pfp), ATP-dependent 6-phosphofructokinase (pfkA)
    4. Fructose-bisphosphate aldolase (fba)
    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 sitei82 – 821Diphosphate; via amide nitrogen
    Binding sitei146 – 1461SubstrateUniRule annotation1 Publication
    Metal bindingi176 – 1761Magnesium; catalyticUniRule annotation
    Sitei177 – 1771Important 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
    Sitei203 – 2031Important for catalytic activity; stabilizes the transition state when the phosphoryl donor is PPi
    Active sitei206 – 2061Proton acceptorUniRule annotation
    Binding sitei312 – 3121SubstrateUniRule annotation1 Publication

    GO - Molecular functioni

    GO - Biological processi

    Complete GO annotation...

    Keywords - Molecular functioni

    Kinase, Transferase

    Keywords - Biological processi

    Glycolysis

    Keywords - Ligandi

    Magnesium, Metal-binding

    Enzyme and pathway databases

    UniPathwayiUPA00109; UER00182.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Pyrophosphate--fructose 6-phosphate 1-phosphotransferaseUniRule annotation (EC:2.7.1.90UniRule annotation)
    Alternative name(s):
    6-phosphofructokinase, pyrophosphate dependentUniRule annotation
    PPi-dependent phosphofructokinaseUniRule annotation
    Short name:
    PPi-PFKUniRule annotation
    Pyrophosphate-dependent 6-phosphofructose-1-kinaseUniRule annotation
    Gene namesi
    Name:pfpUniRule annotation
    Synonyms:PFK2, pfpB
    Ordered Locus Names:BB_0020
    OrganismiBorrelia burgdorferi (strain ATCC 35210 / B31 / CIP 102532 / DSM 4680)
    Taxonomic identifieri224326 [NCBI]
    Taxonomic lineageiBacteriaSpirochaetesSpirochaetalesBorreliaceaeBorreliaBorrelia burgdorferi group
    ProteomesiUP000001807 Componenti: Chromosome

    Subcellular locationi

    • Cytoplasm UniRule annotation

    GO - Cellular componenti

    Complete GO annotation...

    Keywords - Cellular componenti

    Cytoplasm

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 555555Pyrophosphate--fructose 6-phosphate 1-phosphotransferasePRO_0000428943Add
    BLAST

    Interactioni

    Subunit structurei

    Homodimer.UniRule annotation2 Publications

    Structurei

    Secondary structure

    1
    555
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi5 – 106Combined sources
    Helixi19 – 224Combined sources
    Helixi25 – 273Combined sources
    Beta strandi28 – 325Combined sources
    Helixi42 – 487Combined sources
    Turni49 – 546Combined sources
    Beta strandi58 – 636Combined sources
    Beta strandi74 – 829Combined sources
    Helixi87 – 10115Combined sources
    Beta strandi106 – 1105Combined sources
    Turni111 – 1144Combined sources
    Helixi115 – 1184Combined sources
    Beta strandi122 – 1254Combined sources
    Helixi127 – 1337Combined sources
    Turni140 – 1423Combined sources
    Helixi152 – 16413Combined sources
    Beta strandi168 – 1758Combined sources
    Helixi176 – 19116Combined sources
    Beta strandi197 – 2048Combined sources
    Helixi220 – 24122Combined sources
    Beta strandi245 – 2506Combined sources
    Helixi257 – 26610Combined sources
    Beta strandi269 – 2713Combined sources
    Helixi274 – 2796Combined sources
    Helixi284 – 30017Combined sources
    Beta strandi306 – 3116Combined sources
    Helixi314 – 3163Combined sources
    Helixi319 – 33416Combined sources
    Helixi336 – 3394Combined sources
    Helixi344 – 35411Combined sources
    Helixi357 – 3648Combined sources
    Helixi368 – 37912Combined sources
    Helixi394 – 41017Combined sources
    Turni411 – 4133Combined sources
    Beta strandi421 – 4277Combined sources
    Helixi428 – 4314Combined sources
    Helixi437 – 45519Combined sources
    Beta strandi460 – 4667Combined sources
    Helixi472 – 4743Combined sources
    Beta strandi476 – 4816Combined sources
    Helixi482 – 4854Combined sources
    Beta strandi486 – 4916Combined sources
    Beta strandi494 – 4996Combined sources
    Helixi509 – 52315Combined sources
    Beta strandi535 – 5373Combined sources
    Helixi539 – 5424Combined sources
    Helixi547 – 5526Combined sources

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1KZHX-ray2.55A/B1-553[»]
    2F48X-ray2.11A/B1-553[»]
    ProteinModelPortaliP70826.
    SMRiP70826. Positions 4-553.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni203 – 2064Substrate binding
    Regioni204 – 2063Substrate bindingUniRule annotation
    Regioni243 – 2442Substrate binding; shared with dimeric partner
    Regioni251 – 2533Substrate binding
    Regioni428 – 4314Substrate binding

    Sequence similaritiesi

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

    Family and domain databases

    Gene3Di1.10.10.480. 1 hit.
    HAMAPiMF_01980. Phosphofructokinase_II_Long.
    InterProiIPR022953. ATP_PFK.
    IPR013981. PFK_a-hlx.
    IPR011183. PfpB_PPi_PFK.
    IPR000023. Phosphofructokinase_dom.
    [Graphical view]
    PfamiPF00365. PFK. 1 hit.
    [Graphical view]
    PIRSFiPIRSF005677. PPi_PFK_PfpB. 1 hit.
    PRINTSiPR00476. PHFRCTKINASE.
    SUPFAMiSSF53784. SSF53784. 1 hit.
    TIGRFAMsiTIGR02477. PFKA_PPi. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    P70826-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MNTSLFKQER QKYIPKLPNI LKKDFNNISL VYGENTEAIQ DRQALKEFFK
    60 70 80 90 100
    NTYGLPIISF TEGESSLSFS KALNIGIILS GGPAPGGHNV ISGVFDAIKK
    110 120 130 140 150
    FNPNSKLFGF KGGPLGLLEN DKIELTESLI NSYRNTGGFD IVSSGRTKIE
    160 170 180 190 200
    TEEHYNKALF VAKENNLNAI IIIGGDDSNT NAAILAEYFK KNGENIQVIG
    210 220 230 240 250
    VPKTIDADLR NDHIEISFGF DSATKIYSEL IGNLCRDAMS TKKYWHFVKL
    260 270 280 290 300
    MGRSASHVAL ECALKTHPNI CIVSEEVLAK KKTLSEIIDE MVSVILKRSL
    310 320 330 340 350
    NGDNFGVVIV PEGLIEFIPE VKSLMLELCD IFDKNEGEFK GLNIEKMKEI
    360 370 380 390 400
    FVAKLSDYMK GVYLSLPLFI QFELIKSILE RDPHGNFNVS RVPTEKLFIE
    410 420 430 440 450
    MIQSRLNDMK KRGEYKGSFT PVDHFFGYEG RSAFPSNFDS DYCYSLGYNA
    460 470 480 490 500
    VVLILNGLTG YMSCIKNLNL KPTDWIAGGV PLTMLMNMEE RYGEKKPVIK
    510 520 530 540 550
    KALVDLEGRP FKEFVKNRDK WALNNLYLYP GPVQYFGSSE IVDEITETLK

    LELLK
    Length:555
    Mass (Da):62,443
    Last modified:November 1, 1998 - v2
    Checksum:i0FEAC1077DA6127F
    GO

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AJ224475 Genomic DNA. Translation: CAA11968.1.
    AE000783 Genomic DNA. No translation available.
    PIRiD70102.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AJ224475 Genomic DNA. Translation: CAA11968.1.
    AE000783 Genomic DNA. No translation available.
    PIRiD70102.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1KZHX-ray2.55A/B1-553[»]
    2F48X-ray2.11A/B1-553[»]
    ProteinModelPortaliP70826.
    SMRiP70826. Positions 4-553.
    ModBaseiSearch...
    MobiDBiSearch...

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Enzyme and pathway databases

    UniPathwayiUPA00109; UER00182.

    Family and domain databases

    Gene3Di1.10.10.480. 1 hit.
    HAMAPiMF_01980. Phosphofructokinase_II_Long.
    InterProiIPR022953. ATP_PFK.
    IPR013981. PFK_a-hlx.
    IPR011183. PfpB_PPi_PFK.
    IPR000023. Phosphofructokinase_dom.
    [Graphical view]
    PfamiPF00365. PFK. 1 hit.
    [Graphical view]
    PIRSFiPIRSF005677. PPi_PFK_PfpB. 1 hit.
    PRINTSiPR00476. PHFRCTKINASE.
    SUPFAMiSSF53784. SSF53784. 1 hit.
    TIGRFAMsiTIGR02477. PFKA_PPi. 1 hit.
    ProtoNetiSearch...

    Publicationsi

    « Hide 'large scale' publications
    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. 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.

    Entry informationi

    Entry nameiPFP_BORBU
    AccessioniPrimary (citable) accession number: P70826
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 14, 2014
    Last sequence update: November 1, 1998
    Last modified: June 24, 2015
    This is version 84 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, Complete proteome, Reference proteome

    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

    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.