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Protein

Pyrophosphate--fructose 6-phosphate 1-phosphotransferase

Gene

pfp

Organism
Nitrosospira multiformis (strain ATCC 25196 / NCIMB 11849 / C 71)
Status
Unreviewed-Annotation score: Annotation score: 4 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 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

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), Glucose-6-phosphate isomerase (pgi)
  3. Pyrophosphate--fructose 6-phosphate 1-phosphotransferase (pfp)
  4. Fructose-bisphosphate aldolase (Nmul_A1561)
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 sitei13Diphosphate; via amide nitrogenUniRule annotation1
Sitei115Important 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
Sitei141Important for catalytic activity; stabilizes the transition state when the phosphoryl donor is PPiUniRule annotation1
Active sitei144Proton acceptorUniRule annotation1
Binding sitei247SubstrateUniRule annotation1

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionKinaseUniRule annotationImported, Transferase
Biological processGlycolysisUniRule annotation
LigandMagnesiumUniRule annotation, Metal-bindingUniRule annotation

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
Ordered Locus Names:Nmul_A0740Imported
ORF Names:SAMN05216403_103113Imported
OrganismiNitrosospira multiformis (strain ATCC 25196 / NCIMB 11849 / C 71)Imported
Taxonomic identifieri323848 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaBetaproteobacteriaNitrosomonadalesNitrosomonadaceaeNitrosospira
Proteomesi
  • UP000002718 Componenti: Chromosome

Subcellular locationi

Q2YB24:
  • Cytoplasm UniRule annotation

GO - Cellular componenti

Keywords - Cellular componenti

CytoplasmUniRule annotation

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Protein-protein interaction databases

STRINGi323848.Nmul_A0740.

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3HNOX-ray2.00A/B/C/D1-419[»]
SMRiQ2YB24.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ2YB24.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini10 – 324PFKInterPro annotationAdd BLAST315

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni142 – 144Substrate bindingUniRule annotation3
Regioni190 – 192Substrate bindingUniRule annotation3
Regioni297 – 300Substrate bindingUniRule annotation4

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiENOG4107R15. Bacteria.
COG0205. LUCA.
HOGENOMiHOG000007357.
KOiK21071.
OMAiAHDIGYF.
OrthoDBiPOG091H01AC.

Family and domain databases

HAMAPiMF_01978. Phosphofructokinase_II_B2. 1 hit.
InterProiView protein in InterPro
IPR022953. ATP_PFK.
IPR000023. Phosphofructokinase_dom.
IPR035966. PKF_sf.
IPR011404. PPi-PFK_XF0274.
PfamiView protein in Pfam
PF00365. PFK. 1 hit.
PIRSFiPIRSF036483. PFK_XF0274. 1 hit.
PRINTSiPR00476. PHFRCTKINASE.
SUPFAMiSSF53784. SSF53784. 1 hit.

Sequencei

Sequence statusi: Complete.

Q2YB24-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAAKNAFYAQ SGGVTAVINA SAAGVIEAAR KQSGKIGRIY AGRNGIIGAL
60 70 80 90 100
TEDLIDTGQE SDAAISALRY TPSGAFGSCR YKLKSLEQNR REYERLIEVF
110 120 130 140 150
KAHDIGYFFY NGGGDSADTC LKVSQLSGTL GYPIQAIHVP KTVDNDLPIT
160 170 180 190 200
DCCPGFGSVA KYIAVSTLEA SFDVASMSAT STKVFVLEVM GRHAGWIAAA
210 220 230 240 250
GGLASSPERE IPVVILFPEI SFDKQKFLAK VDSCVKKFGY CSVVVSEGVK
260 270 280 290 300
GDDGKFLSDQ GVRDAFGHAQ LGGVAPVVAS MVKEGLGLKY HWGVADYLQR
310 320 330 340 350
AARHIASKTD VEQAYAMGQA AVEFAVQGHN SVMPTIERIS ARPYQWKVGM
360 370 380 390 400
AQLSQVANVE KMMPENFITE DGFGITDLCR EYLAPLIEGE DYPPYKDGLP
410
DYVRLKNVAV PKKLSGFTL
Length:419
Mass (Da):45,062
Last modified:December 20, 2005 - v1
Checksum:i903739280B805510
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000103 Genomic DNA. Translation: ABB74047.1.
FNVK01000003 Genomic DNA. Translation: SEF55197.1.
RefSeqiWP_011380097.1. NC_007614.1.

Genome annotation databases

EnsemblBacteriaiABB74047; ABB74047; Nmul_A0740.
KEGGinmu:Nmul_A0740.

Similar proteinsi

Entry informationi

Entry nameiQ2YB24_NITMU
AccessioniPrimary (citable) accession number: Q2YB24
Entry historyiIntegrated into UniProtKB/TrEMBL: December 20, 2005
Last sequence update: December 20, 2005
Last modified: October 25, 2017
This is version 88 of the entry and version 1 of the sequence. See complete history.
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Caution

Lacks conserved residue(s) required for the propagation of feature annotation.UniRule annotation

Keywords - Technical termi

3D-structureCombined sources, Complete proteome, Reference proteomeImported