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Protein

Pyrophosphate--fructose 6-phosphate 1-phosphotransferase

Gene

pfp

Organism
Clostridium perfringens (strain SM101 / Type A)
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)
  3. ATP-dependent 6-phosphofructokinase (pfkA), Pyrophosphate--fructose 6-phosphate 1-phosphotransferase (pfp), Phosphofructokinase family protein (CPR_1203)
  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 sitei10 – 101Diphosphate; via amide nitrogenUniRule annotation
Metal bindingi110 – 1101Magnesium; catalyticUniRule annotation
Sitei111 – 1111Important 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
Sitei137 – 1371Important for catalytic activity; stabilizes the transition state when the phosphoryl donor is PPiUniRule annotation
Active sitei140 – 1401Proton acceptorUniRule annotation
Binding sitei241 – 2411SubstrateUniRule 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

BioCyciCPER289380:GI76-1459-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:CPR_1446Imported
OrganismiClostridium perfringens (strain SM101 / Type A)Imported
Taxonomic identifieri289380 [NCBI]
Taxonomic lineageiBacteriaFirmicutesClostridiaClostridialesClostridiaceaeClostridium
ProteomesiUP000001824 Componenti: Chromosome

Subcellular locationi

  • Cytoplasm UniRule annotation

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

CytoplasmUniRule annotation

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Structurei

3D structure databases

ProteinModelPortaliQ0SSZ2.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni138 – 1403Substrate bindingUniRule annotation
Regioni184 – 1863Substrate 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

eggNOGiCOG0205.
HOGENOMiHOG000007357.
KOiK00850.
OMAiKNAFYAQ.
OrthoDBiEOG6PP9HS.

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.

Q0SSZ2-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MNCIIAQSGG PTSVINASVY GLVKANKKLN LYENVYGGLN GIEGILNKKI
60 70 80 90 100
INLSDLDELQ LERFKNSPAS GLGSCRYKLK PLSESEDEYL KLLDILNSLN
110 120 130 140 150
IKAFFYVGGN DSMDTTAKLN AFAKAKNIDI KFFGIPKTID NDLMHTDHTP
160 170 180 190 200
GFGSAAKFIS TAVLETYLDS KVYTNNGIFI IETMGRDTGW LAASGALATI
210 220 230 240 250
NGNKCADLVY LPERAFSVQS FLTDVARIFK EKKHVYIVAS EGLKDENGKF
260 270 280 290 300
LTETAPNDDS FGHAQLGGVG AYLKNLIIQA SITHRVKSLE LNTLQRCSMH
310 320 330 340 350
ASSKIDVNEA VMVGQAALEA SVNSEGGYMV AIRRDSSFPY KSSTFLIEAD
360 370 380 390 400
KIANNIKYFP NEWINEEGNN ITEEGLSYLK PLISDFEDRD SLPLYHSFVL
Length:400
Mass (Da):43,984
Last modified:September 5, 2006 - v1
Checksum:iB1A70B3FF94D2A4B
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000312 Genomic DNA. Translation: ABG86277.1.

Genome annotation databases

EnsemblBacteriaiABG86277; ABG86277; CPR_1446.
KEGGicpr:CPR_1446.
PATRICi19491183. VBICloPer122123_1421.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000312 Genomic DNA. Translation: ABG86277.1.

3D structure databases

ProteinModelPortaliQ0SSZ2.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiABG86277; ABG86277; CPR_1446.
KEGGicpr:CPR_1446.
PATRICi19491183. VBICloPer122123_1421.

Phylogenomic databases

eggNOGiCOG0205.
HOGENOMiHOG000007357.
KOiK00850.
OMAiKNAFYAQ.
OrthoDBiEOG6PP9HS.

Enzyme and pathway databases

UniPathwayiUPA00109; UER00182.
BioCyciCPER289380:GI76-1459-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. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: SM101 / Type AImported.

Entry informationi

Entry nameiQ0SSZ2_CLOPS
AccessioniPrimary (citable) accession number: Q0SSZ2
Entry historyi
Integrated into UniProtKB/TrEMBL: September 5, 2006
Last sequence update: September 5, 2006
Last modified: July 22, 2015
This is version 69 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Keywords - Technical termi

Complete 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.