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P70826

- PFP_BORBU

UniProt

P70826 - PFP_BORBU

Protein

Pyrophosphate--fructose 6-phosphate 1-phosphotransferase

Gene

pfp

Organism
Borrelia burgdorferi (strain ATCC 35210 / B31 / CIP 102532 / DSM 4680)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 77 (01 Oct 2014)
      Sequence version 2 (01 Nov 1998)
      Previous versions | rss
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    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.1 PublicationUniRule annotation

    Catalytic activityi

    Diphosphate + D-fructose 6-phosphate = phosphate + D-fructose 1,6-bisphosphate.1 PublicationUniRule annotation

    Cofactori

    Magnesium.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

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei82 – 821Diphosphate; via amide nitrogen
    Binding sitei146 – 1461Substrate1 PublicationUniRule annotation
    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 – 3121Substrate1 PublicationUniRule annotation

    GO - Molecular functioni

    1. 6-phosphofructokinase activity Source: InterPro
    2. ATP binding Source: InterPro
    3. diphosphate-fructose-6-phosphate 1-phosphotransferase activity Source: UniProtKB-EC
    4. metal ion binding Source: UniProtKB-KW

    GO - Biological processi

    1. fructose 6-phosphate metabolic process Source: InterPro
    2. glycolytic process Source: UniProtKB-UniPathway

    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 lineageiBacteriaSpirochaetesSpirochaetalesSpirochaetaceaeBorreliaBorrelia burgdorferi group
    ProteomesiUP000001807: Chromosome

    Subcellular locationi

    Cytoplasm UniRule annotation

    GO - Cellular componenti

    1. 6-phosphofructokinase complex Source: InterPro

    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.2 PublicationsUniRule annotation

    Structurei

    Secondary structure

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

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    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.
    InterProiIPR011183. PfpB_PPi_PFK.
    IPR022953. Phosphofructokinase.
    IPR000023. Phosphofructokinase_dom.
    IPR013981. PPi-dep_PFK_a-hlx.
    [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

    MNTSLFKQER QKYIPKLPNI LKKDFNNISL VYGENTEAIQ DRQALKEFFK    50
    NTYGLPIISF TEGESSLSFS KALNIGIILS GGPAPGGHNV ISGVFDAIKK 100
    FNPNSKLFGF KGGPLGLLEN DKIELTESLI NSYRNTGGFD IVSSGRTKIE 150
    TEEHYNKALF VAKENNLNAI IIIGGDDSNT NAAILAEYFK KNGENIQVIG 200
    VPKTIDADLR NDHIEISFGF DSATKIYSEL IGNLCRDAMS TKKYWHFVKL 250
    MGRSASHVAL ECALKTHPNI CIVSEEVLAK KKTLSEIIDE MVSVILKRSL 300
    NGDNFGVVIV PEGLIEFIPE VKSLMLELCD IFDKNEGEFK GLNIEKMKEI 350
    FVAKLSDYMK GVYLSLPLFI QFELIKSILE RDPHGNFNVS RVPTEKLFIE 400
    MIQSRLNDMK KRGEYKGSFT PVDHFFGYEG RSAFPSNFDS DYCYSLGYNA 450
    VVLILNGLTG YMSCIKNLNL KPTDWIAGGV PLTMLMNMEE RYGEKKPVIK 500
    KALVDLEGRP FKEFVKNRDK WALNNLYLYP GPVQYFGSSE IVDEITETLK 550
    LELLK 555
    Length:555
    Mass (Da):62,443
    Last modified:November 1, 1998 - v2
    Checksum:i0FEAC1077DA6127F
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AJ224475 Genomic DNA. Translation: CAA11968.1.
    AE000783 Genomic DNA. No translation available.
    PIRiD70102.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AJ224475 Genomic DNA. Translation: CAA11968.1 .
    AE000783 Genomic DNA. No translation available.
    PIRi D70102.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1KZH X-ray 2.55 A/B 1-553 [» ]
    2F48 X-ray 2.11 A/B 1-553 [» ]
    ProteinModelPortali P70826.
    SMRi P70826. Positions 4-553.
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Enzyme and pathway databases

    UniPathwayi UPA00109 ; UER00182 .

    Family and domain databases

    Gene3Di 1.10.10.480. 1 hit.
    HAMAPi MF_01980. Phosphofructokinase_II_Long.
    InterProi IPR011183. PfpB_PPi_PFK.
    IPR022953. Phosphofructokinase.
    IPR000023. Phosphofructokinase_dom.
    IPR013981. PPi-dep_PFK_a-hlx.
    [Graphical view ]
    Pfami PF00365. PFK. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF005677. PPi_PFK_PfpB. 1 hit.
    PRINTSi PR00476. PHFRCTKINASE.
    SUPFAMi SSF53784. SSF53784. 1 hit.
    TIGRFAMsi TIGR02477. PFKA_PPi. 1 hit.
    ProtoNeti Search...

    Publicationsi

    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: October 1, 2014
    This is version 77 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