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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 annotationBy similarity

Enzyme regulationi

Non-allosteric.UniRule annotationBy similarity

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

    Pathwayi: 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)DescriptionActionsGraphical viewLength
    Binding sitei82Diphosphate; via amide nitrogenUniRule annotation1 Publication1
    Binding sitei146Substrate1 Publication1
    Metal bindingi176Magnesium; catalyticUniRule annotationBy similarity1
    Sitei177Important 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 ATPUniRule annotation1 Publication1
    Sitei203Important for catalytic activity; stabilizes the transition state when the phosphoryl donor is PPiUniRule annotation1 Publication1
    Active sitei206Proton acceptorUniRule annotationBy similarity1
    Binding sitei312SubstrateUniRule annotation1 Publication1

    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 lineageiBacteriaSpirochaetesSpirochaetalesBorreliaceaeBorreliella
    Proteomesi
    • UP000001807 Componenti: Chromosome

    Subcellular locationi

    • Cytoplasm UniRule annotationBy similarity

    GO - Cellular componenti

    Complete GO annotation...

    Keywords - Cellular componenti

    Cytoplasm

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    ChainiPRO_00004289431 – 555Pyrophosphate--fructose 6-phosphate 1-phosphotransferaseAdd BLAST555

    Proteomic databases

    PRIDEiP70826.

    Interactioni

    Subunit structurei

    Homodimer.UniRule annotation2 Publications

    Structurei

    Secondary structure

    1555
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details
    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Helixi5 – 10Combined sources6
    Helixi19 – 22Combined sources4
    Helixi25 – 27Combined sources3
    Beta strandi28 – 32Combined sources5
    Helixi42 – 48Combined sources7
    Turni49 – 54Combined sources6
    Beta strandi58 – 63Combined sources6
    Beta strandi74 – 82Combined sources9
    Helixi87 – 101Combined sources15
    Beta strandi106 – 110Combined sources5
    Turni111 – 114Combined sources4
    Helixi115 – 118Combined sources4
    Beta strandi122 – 125Combined sources4
    Helixi127 – 133Combined sources7
    Turni140 – 142Combined sources3
    Helixi152 – 164Combined sources13
    Beta strandi168 – 175Combined sources8
    Helixi176 – 191Combined sources16
    Beta strandi197 – 204Combined sources8
    Helixi220 – 241Combined sources22
    Beta strandi245 – 250Combined sources6
    Helixi257 – 266Combined sources10
    Beta strandi269 – 271Combined sources3
    Helixi274 – 279Combined sources6
    Helixi284 – 300Combined sources17
    Beta strandi306 – 311Combined sources6
    Helixi314 – 316Combined sources3
    Helixi319 – 334Combined sources16
    Helixi336 – 339Combined sources4
    Helixi344 – 354Combined sources11
    Helixi357 – 364Combined sources8
    Helixi368 – 379Combined sources12
    Helixi394 – 410Combined sources17
    Turni411 – 413Combined sources3
    Beta strandi421 – 427Combined sources7
    Helixi428 – 431Combined sources4
    Helixi437 – 455Combined sources19
    Beta strandi460 – 466Combined sources7
    Helixi472 – 474Combined sources3
    Beta strandi476 – 481Combined sources6
    Helixi482 – 485Combined sources4
    Beta strandi486 – 491Combined sources6
    Beta strandi494 – 499Combined sources6
    Helixi509 – 523Combined sources15
    Beta strandi535 – 537Combined sources3
    Helixi539 – 542Combined sources4
    Helixi547 – 552Combined sources6

    3D structure databases

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

    Family & Domainsi

    Region

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Regioni204 – 206Substrate bindingUniRule annotation1 Publication3
    Regioni243 – 244Substrate binding; shared with dimeric partnerUniRule annotation1 Publication2
    Regioni251 – 253Substrate bindingUniRule annotation1 Publication3
    Regioni428 – 431Substrate bindingUniRule annotation1 Publication4

    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. 1 hit.
    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
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    1KZHX-ray2.55A/B1-553[»]
    2F48X-ray2.11A/B1-553[»]
    ProteinModelPortaliP70826.
    SMRiP70826.
    ModBaseiSearch...
    MobiDBiSearch...

    Proteomic databases

    PRIDEiP70826.

    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. 1 hit.
    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...

    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: November 2, 2016
    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, 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

    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 one 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.