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
Pseudoxanthomonas spadix (strain BD-a59)
Status
Unreviewed-Annotation score: Annotation score: 4 out of 5-Protein inferred from homologyi

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 annotation

Catalytic activityi

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

Cofactori

Mg2+UniRule annotation

Enzyme regulationi

Non-allosteric.UniRule annotation

Pathway:iglycolysis

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), Glucose-6-phosphate isomerase (pgi)
  3. Pyrophosphate--fructose 6-phosphate 1-phosphotransferase (pfp)
  4. Fructose-bisphosphate aldolase (DSC_13105)
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 sitei13 – 131Diphosphate; via amide nitrogenUniRule annotation
Metal bindingi111 – 1111Magnesium; catalyticUniRule annotation
Sitei112 – 1121Important 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 annotation
Sitei138 – 1381Important for catalytic activity; stabilizes the transition state when the phosphoryl donor is PPiUniRule annotation
Active sitei141 – 1411Proton acceptorUniRule annotation
Binding sitei244 – 2441SubstrateUniRule annotation

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

KinaseUniRule annotationImported, Transferase

Keywords - Biological processi

GlycolysisUniRule annotation

Keywords - Ligandi

MagnesiumUniRule annotation, Metal-bindingUniRule annotation

Enzyme and pathway databases

BioCyciPSPA1045855:GH5V-2571-MONOMER.
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
Pyrophosphate-dependent 6-phosphofructose-1-kinaseUniRule annotation
Gene namesi
Name:pfpUniRule annotation
Ordered Locus Names:DSC_13660Imported
OrganismiPseudoxanthomonas spadix (strain BD-a59)Imported
Taxonomic identifieri1045855 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaXanthomonadalesXanthomonadaceaePseudoxanthomonas
ProteomesiUP000005870 Componenti: Chromosome

Subcellular locationi

  • Cytoplasm UniRule annotation

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

CytoplasmUniRule annotation

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Protein-protein interaction databases

STRINGi1045855.DSC_13660.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni139 – 1413Substrate bindingUniRule annotation
Regioni187 – 1893Substrate bindingUniRule annotation
Regioni295 – 2984Substrate bindingUniRule annotation

Sequence similaritiesi

Belongs to the phosphofructokinase type A (PFKA) family. PPi-dependent PFK group II subfamily. Clade "B2" sub-subfamily.UniRule annotation

Phylogenomic databases

KOiK00850.
OMAiKNAFYAQ.

Family and domain databases

HAMAPiMF_01978. Phosphofructokinase_II_B2.
InterProiIPR022953. ATP_PFK.
IPR000023. Phosphofructokinase_dom.
IPR011404. PPi-PFK_XF0274.
[Graphical view]
PfamiPF00365. PFK. 1 hit.
[Graphical view]
PIRSFiPIRSF036483. PFK_XF0274. 1 hit.
PRINTSiPR00476. PHFRCTKINASE.
SUPFAMiSSF53784. SSF53784. 1 hit.

Sequencei

Sequence statusi: Complete.

G7UTD0-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MVQSTLLYAQ SGGVTAVINA TASAVISEAR RRKVKVLAAR NGILGALREE
60 70 80 90 100
LIDTSRESIS AIRALAHTPG GAFGSCRVKL KSLEADRDRY ARLLEVFKAH
110 120 130 140 150
NVRWFLYNGG NDSADTAWKV SQLAQAFDYP LTCVGVPKTI DNDLAVTDTC
160 170 180 190 200
PGFGSAAKYT AVSVRECALD VAAMAQTSTK VFVYEAMGRH AGWLAAAAGL
210 220 230 240 250
AGAAADEAPH IILFPERAYD QAAFLAQVDK VVKQVGYCVV VASEGIRNAD
260 270 280 290 300
GTFVADAGGA ADAFGHAQLG GVAASLAGTV KASLGYKVHW ALPDYLQRSA
310 320 330 340 350
RHIASKTDWA QAQAVGKAAV QYALKGMNAV MPVIVRSADA PYRWKIAPAP
360 370 380 390 400
LSKVANHEKT MPASFIRKDG FGITANARKY LAPLIKGEAP LPYGADGLPR
410
YVTLKNVAVK KKLPAWED
Length:418
Mass (Da):44,347
Last modified:January 25, 2012 - v1
Checksum:iEDA7D3432531F15A
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP003093 Genomic DNA. Translation: AER57376.1.
RefSeqiWP_014161549.1. NC_016147.2.

Genome annotation databases

EnsemblBacteriaiAER57376; AER57376; DSC_13660.
KEGGipsd:DSC_13660.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP003093 Genomic DNA. Translation: AER57376.1.
RefSeqiWP_014161549.1. NC_016147.2.

3D structure databases

ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi1045855.DSC_13660.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAER57376; AER57376; DSC_13660.
KEGGipsd:DSC_13660.

Phylogenomic databases

KOiK00850.
OMAiKNAFYAQ.

Enzyme and pathway databases

UniPathwayiUPA00109; UER00182.
BioCyciPSPA1045855:GH5V-2571-MONOMER.

Family and domain databases

HAMAPiMF_01978. Phosphofructokinase_II_B2.
InterProiIPR022953. ATP_PFK.
IPR000023. Phosphofructokinase_dom.
IPR011404. PPi-PFK_XF0274.
[Graphical view]
PfamiPF00365. PFK. 1 hit.
[Graphical view]
PIRSFiPIRSF036483. PFK_XF0274. 1 hit.
PRINTSiPR00476. PHFRCTKINASE.
SUPFAMiSSF53784. SSF53784. 1 hit.
ProtoNetiSearch...

Publicationsi

  1. "Complete Genome Sequence of the BTEX-Degrading Bacterium Pseudoxanthomonas spadix BD-a59."
    Lee S.H., Jin H.M., Lee H.J., Kim J.M., Jeon C.O.
    J. Bacteriol. 194:544-544(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: BD-a59Imported.

Entry informationi

Entry nameiG7UTD0_PSEUP
AccessioniPrimary (citable) accession number: G7UTD0
Entry historyi
Integrated into UniProtKB/TrEMBL: January 25, 2012
Last sequence update: January 25, 2012
Last modified: July 22, 2015
This is version 23 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteomeImported

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.