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Protein

Pyrophosphate--fructose 6-phosphate 1-phosphotransferase

Gene

pfp

Organism
Amycolatopsis methanolica
Status
Reviewed-Annotation score: 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.UniRule annotation2 Publications

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 annotation1 Publication

Kineticsi

  1. KM=0.84 mM for phosphate1 Publication
  2. KM=0.2 mM for diphosphate1 Publication
  3. KM=0.4 mM for fructose 6-phosphate1 Publication
  4. KM=0.025 mM for fructose 1,6-bisphosphate1 Publication
  1. Vmax=58 µmol/min/mg enzyme for the forward reaction1 Publication
  2. Vmax=59 µmol/min/mg enzyme for the reverse reaction1 Publication

pH dependencei

Optimum pH is 7.5 for both the forward and the reverse reactions.1 Publication

Temperature dependencei

Optimum temperature is 35-46 degrees Celsius.1 Publication

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. no protein annotated in this organism
  3. ATP-dependent 6-phosphofructokinase (pfkA), Pyrophosphate--fructose 6-phosphate 1-phosphotransferase (pfp)
  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 bindingi103 – 1031Magnesium; catalyticUniRule annotation
Sitei104 – 1041Important 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
Sitei124 – 1241Important for catalytic activity; stabilizes the transition state when the phosphoryl donor is PPiUniRule annotation
Active sitei127 – 1271Proton acceptorUniRule annotation
Binding sitei162 – 1621Substrate; shared with dimeric partnerUniRule annotation
Binding sitei221 – 2211SubstrateUniRule annotation
Binding sitei265 – 2651Substrate; shared with dimeric partnerUniRule 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

BRENDAi2.7.1.90. 314.
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
OrganismiAmycolatopsis methanolica
Taxonomic identifieri1814 [NCBI]
Taxonomic lineageiBacteriaActinobacteriaPseudonocardialesPseudonocardiaceaeAmycolatopsis

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 – 341341Pyrophosphate--fructose 6-phosphate 1-phosphotransferasePRO_0000112011Add
BLAST

Expressioni

Inductioni

Present when grown on glucose.1 Publication

Interactioni

Subunit structurei

Homotetramer.1 Publication

Structurei

3D structure databases

ProteinModelPortaliQ59126.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni125 – 1273Substrate bindingUniRule annotation
Regioni169 – 1713Substrate bindingUniRule annotation
Regioni271 – 2744Substrate bindingUniRule annotation

Sequence similaritiesi

Belongs to the phosphofructokinase type A (PFKA) family. Mixed-substrate PFK group III subfamily.UniRule annotation

Family and domain databases

HAMAPiMF_01976. Phosphofructokinase_III.
InterProiIPR022953. ATP_PFK.
IPR012003. ATP_PFK_prok-type.
IPR015912. Phosphofructokinase_CS.
IPR000023. Phosphofructokinase_dom.
IPR012829. Phosphofructokinase_III.
[Graphical view]
PfamiPF00365. PFK. 1 hit.
[Graphical view]
PIRSFiPIRSF000532. ATP_PFK_prok. 1 hit.
PRINTSiPR00476. PHFRCTKINASE.
SUPFAMiSSF53784. SSF53784. 1 hit.
TIGRFAMsiTIGR02483. PFK_mixed. 1 hit.
PROSITEiPS00433. PHOSPHOFRUCTOKINASE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q59126-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MRVGVLTGGG DCPGLNAVIR AVVRKGIEAH GWEIVGFRSG WRGPLTGDSR
60 70 80 90 100
PLGLDDVEEI LIRGGTILGS SRTNPYKEEG GVEKIRAVLA DQGVDALIAI
110 120 130 140 150
GGEDTLGVAK KLTDDGIGVV GVPKTIDNDL AATDYTFGFD TAVHIATEAI
160 170 180 190 200
DRLRTTAESH YRAMVVEVMG RHAGWIALHA GLAGGANVIL VPERPFSVEQ
210 220 230 240 250
VVEWVERRFE KMYAPIIVVA EGAVPEGGAE VLRTGEKDAF GHVQLGGVGT
260 270 280 290 300
WLADEIAERT GKESRAVVLG HTQRGGTPTA YDRVLATRFG LHAVDAVADG
310 320 330 340
DFGTMVALRG TDIVRVKLAE ATAELKTVPP ERYEEAEVFF G
Length:341
Mass (Da):36,229
Last modified:May 16, 2003 - v2
Checksum:i306613246172D36B
GO

Sequence cautioni

The sequence AAB01683.1 differs from that shown. Reason: Erroneous initiation. Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U31277 Genomic DNA. Translation: AAB01683.1. Different initiation.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U31277 Genomic DNA. Translation: AAB01683.1. Different initiation.

3D structure databases

ProteinModelPortaliQ59126.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

UniPathwayiUPA00109; UER00182.
BRENDAi2.7.1.90. 314.

Family and domain databases

HAMAPiMF_01976. Phosphofructokinase_III.
InterProiIPR022953. ATP_PFK.
IPR012003. ATP_PFK_prok-type.
IPR015912. Phosphofructokinase_CS.
IPR000023. Phosphofructokinase_dom.
IPR012829. Phosphofructokinase_III.
[Graphical view]
PfamiPF00365. PFK. 1 hit.
[Graphical view]
PIRSFiPIRSF000532. ATP_PFK_prok. 1 hit.
PRINTSiPR00476. PHFRCTKINASE.
SUPFAMiSSF53784. SSF53784. 1 hit.
TIGRFAMsiTIGR02483. PFK_mixed. 1 hit.
PROSITEiPS00433. PHOSPHOFRUCTOKINASE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "Characterization and phylogeny of the pfp gene of Amycolatopsis methanolica encoding PPi-dependent phosphofructokinase."
    Alves A.M., Meijer W.G., Vrijbloed J.W., Dijkhuizen L.
    J. Bacteriol. 178:149-155(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: DSM 44096 / JCM 8087 / NBRC 15065 / NCIMB 11946.
  2. "Enzymes of glucose and methanol metabolism in the actinomycete Amycolatopsis methanolica."
    Alves A.M., Euverink G.J., Hektor H.J., Hessels G.I., van der Vlag J., Vrijbloed J.W., Hondmann D., Visser J., Dijkhuizen L.
    J. Bacteriol. 176:6827-6835(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 1-40, FUNCTION, CATALYTIC ACTIVITY, SUBUNIT, BIOPHYSICOCHEMICAL PROPERTIES, ENZYME REGULATION.
    Strain: DSM 44096 / JCM 8087 / NBRC 15065 / NCIMB 11946.
  3. "Different physiological roles of ATP- and PP(i)-dependent phosphofructokinase isoenzymes in the methylotrophic actinomycete Amycolatopsis methanolica."
    Alves A.M., Euverink G.J., Santos H., Dijkhuizen L.
    J. Bacteriol. 183:7231-7240(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INDUCTION.
    Strain: DSM 44096 / JCM 8087 / NBRC 15065 / NCIMB 11946.

Entry informationi

Entry nameiPFP_AMYME
AccessioniPrimary (citable) accession number: Q59126
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: May 16, 2003
Last modified: July 6, 2016
This is version 86 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

Direct protein sequencing

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.