Skip Header

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

P70826

- PFP_BORBU

UniProt

P70826 - PFP_BORBU

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

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

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

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

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
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 lineageiBacteriaSpirochaetesSpirochaetalesSpirochaetaceaeBorreliaBorrelia burgdorferi group
ProteomesiUP000001807: Chromosome

Subcellular locationi

Cytoplasm UniRule annotation

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-KW
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.2 PublicationsUniRule annotation

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.
InterProiIPR013981. PFK_a-hlx.
IPR011183. PfpB_PPi_PFK.
IPR022953. Phosphofructokinase.
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.
PIRi D70102.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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 IPR013981. PFK_a-hlx.
IPR011183. PfpB_PPi_PFK.
IPR022953. Phosphofructokinase.
IPR000023. Phosphofructokinase_dom.
[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

« 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: November 26, 2014
This is version 79 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