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Protein

Pyrophosphate--fructose 6-phosphate 1-phosphotransferase 1

Gene

Pfk1

Organism
Trichomonas vaginalis
Status
Reviewed-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 annotation1 Publication

Catalytic activityi

Diphosphate + D-fructose 6-phosphate = phosphate + D-fructose 1,6-bisphosphate.UniRule annotation1 Publication

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 (TVAG_389760), Glucose-6-phosphate isomerase (TVAG_061930), Glucose-6-phosphate isomerase (GPI)
  3. Pyrophosphate--fructose 6-phosphate 1-phosphotransferase 1 (Pfk1), Pyrophosphate--fructose 6-phosphate 1-phosphotransferase 3 (pfk3), Pyrophosphate--fructose 6-phosphate 1-phosphotransferase 2 (pfk2)
  4. no protein annotated in this organism
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 sitei15 – 151Diphosphate; via amide nitrogenUniRule annotation
Metal bindingi114 – 1141Magnesium; catalyticUniRule annotation
Sitei115 – 1151Important 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
Sitei139 – 1391Important for catalytic activity; stabilizes the transition state when the phosphoryl donor is PPiUniRule annotation
Active sitei142 – 1421Proton acceptorUniRule annotation
Binding sitei247 – 2471SubstrateUniRule annotation

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-phosphotransferase 1UniRule annotation (EC:2.7.1.90UniRule annotation)
Alternative name(s):
6-phosphofructokinase, pyrophosphate dependent 1UniRule annotation
PPi-dependent phosphofructokinase 1UniRule annotation
Short name:
PPi-PFK 1UniRule annotation
Pyrophosphate-dependent 6-phosphofructose-1-kinase 1UniRule annotation
Gene namesi
Name:Pfk1
ORF Names:TVAG_430830
OrganismiTrichomonas vaginalis
Taxonomic identifieri5722 [NCBI]
Taxonomic lineageiEukaryotaParabasaliaTrichomonadidaTrichomonadidaeTrichomonas
Proteomesi
  • UP000001542 Componenti: Unassembled WGS sequence

Organism-specific databases

EuPathDBiTrichDB:TVAG_430830.

Subcellular locationi

  • Cytoplasm UniRule annotation

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 426426Pyrophosphate--fructose 6-phosphate 1-phosphotransferase 1PRO_0000429702Add
BLAST

Interactioni

Subunit structurei

Homotetramer.UniRule annotation1 Publication

Protein-protein interaction databases

STRINGi5722.O61068.

Structurei

3D structure databases

ProteinModelPortaliO61068.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni140 – 1423Substrate bindingUniRule annotation
Regioni186 – 1883Substrate bindingUniRule annotation
Regioni308 – 3114Substrate bindingUniRule annotation

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiKOG2440. Eukaryota.
COG0205. LUCA.
InParanoidiO61068.

Family and domain databases

HAMAPiMF_01979. Phosphofructokinase_II_Short. 1 hit.
InterProiIPR022953. ATP_PFK.
IPR000023. Phosphofructokinase_dom.
IPR011403. PPi-PFK_TM0289.
[Graphical view]
PfamiPF00365. PFK. 1 hit.
[Graphical view]
PIRSFiPIRSF036482. PPi_PFK_TM0289. 1 hit.
PRINTSiPR00476. PHFRCTKINASE.
SUPFAMiSSF53784. SSF53784. 1 hit.

Sequencei

Sequence statusi: Complete.

O61068-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSTEAPVLGI LCGGGPAPGL NGVIAGATLY ALRLGWKVIG FMEGFKYLCT
60 70 80 90 100
GDVDVVKAHT IDLTYDIVSR IHFQGGTIIQ TSRANPRKSP ELQENVRKCL
110 120 130 140 150
RALKVRYFLT IGGDDTASSA VSVASGMNGN EISVISCPKT IDNDLPLPAD
160 170 180 190 200
QSTFGFHTAR SLGMEIIRNL MVDSKSAPRW FLVEAMGRSA GHLALGMAEA
210 220 230 240 250
SGAHLCLIPE EFKQDEIEFE DVVELVEATI LKRLAYGKNY GVCVLAEGLV
260 270 280 290 300
SKMSKKALYK LFGNREPPTD PHGHILLDDA ELARSLSEEL LKRLGNLGIR
310 320 330 340 350
ITPKKIGYEL RCADPVAFDA VYTRELGYGA IDAFLNGHSA ALIVRENGQV
360 370 380 390 400
KPVQFKDLLD PATGRVRTRL VDVTSQSFKV ARVYMWRMSK KDYENKDLVA
410 420
RVAAAGKMTP EAFTEKFAHL TDVVVE
Length:426
Mass (Da):46,535
Last modified:August 1, 1998 - v1
Checksum:iADDEFE53E507B8D2
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti335 – 3351L → KL AA sequence (PubMed:9847416).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF044973 Genomic DNA. Translation: AAD13344.1.
DS113294 Genomic DNA. Translation: EAY12916.1.
RefSeqiXP_001325139.1. XM_001325104.1.

Genome annotation databases

EnsemblProtistsiEAY12916; EAY12916; TVAG_430830.
GeneIDi4770885.
KEGGitva:TVAG_430830.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF044973 Genomic DNA. Translation: AAD13344.1.
DS113294 Genomic DNA. Translation: EAY12916.1.
RefSeqiXP_001325139.1. XM_001325104.1.

3D structure databases

ProteinModelPortaliO61068.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi5722.O61068.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblProtistsiEAY12916; EAY12916; TVAG_430830.
GeneIDi4770885.
KEGGitva:TVAG_430830.

Organism-specific databases

EuPathDBiTrichDB:TVAG_430830.

Phylogenomic databases

eggNOGiKOG2440. Eukaryota.
COG0205. LUCA.
InParanoidiO61068.

Enzyme and pathway databases

UniPathwayiUPA00109; UER00182.

Family and domain databases

HAMAPiMF_01979. Phosphofructokinase_II_Short. 1 hit.
InterProiIPR022953. ATP_PFK.
IPR000023. Phosphofructokinase_dom.
IPR011403. PPi-PFK_TM0289.
[Graphical view]
PfamiPF00365. PFK. 1 hit.
[Graphical view]
PIRSFiPIRSF036482. PPi_PFK_TM0289. 1 hit.
PRINTSiPR00476. PHFRCTKINASE.
SUPFAMiSSF53784. SSF53784. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiPFP1_TRIVA
AccessioniPrimary (citable) accession number: O61068
Secondary accession number(s): A2E3A6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 9, 2014
Last sequence update: August 1, 1998
Last modified: November 11, 2015
This is version 76 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. 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.