AC   MF_03185;
DC   Protein; auto
c?   <OC:Eukaryota>
TR   HAMAP; MF_01980; -; 1; level=0
XX
Names: Phosphofructokinase_II_Long_euk
XX
case <OC:Viridiplantae> and not (<FT:1> or <FT:2>)
ID   PFPA
DE   RecName: Full=Pyrophosphate--fructose 6-phosphate 1-phosphotransferase subunit alpha;
DE            Short=PFP;
DE   AltName: Full=6-phosphofructokinase, pyrophosphate dependent;
DE   AltName: Full=PPi-PFK;
DE   AltName: Full=Pyrophosphate-dependent 6-phosphofructose-1-kinase;
GN   Name=PFP-ALPHA;
else case (<OC:Viridiplantae>) and <FT:1>
ID   PFPB
DE   RecName: Full=Pyrophosphate--fructose 6-phosphate 1-phosphotransferase subunit beta;
DE            Short=PFP;
DE            EC=2.7.1.90;
DE   AltName: Full=6-phosphofructokinase, pyrophosphate dependent;
DE   AltName: Full=PPi-PFK;
DE   AltName: Full=Pyrophosphate-dependent 6-phosphofructose-1-kinase;
GN   Name=PFP-BETA;
else case <FT:1>
ID   PFP
DE   RecName: Full=Pyrophosphate--fructose 6-phosphate 1-phosphotransferase;
DE            EC=2.7.1.90;
DE   AltName: Full=6-phosphofructokinase, pyrophosphate dependent;
DE   AltName: Full=PPi-dependent phosphofructokinase;
DE            Short=PPi-PFK;
DE   AltName: Full=Pyrophosphate-dependent 6-phosphofructose-1-kinase;
else case <FT:2>
ID   PFKA
DE   RecName: Full=Probable ATP-dependent 6-phosphofructokinase;
DE            Short=ATP-PFK;
DE            Short=Phosphofructokinase;
DE            EC=2.7.1.11;
DE   AltName: Full=Phosphohexokinase;
else
ID   PFKA
DE   RecName: Full=6-phosphofructokinase;
DE            EC=2.7.1.-;
end case
XX
case <OC:Viridiplantae> and not (<FT:1> or <FT:2>)
CC   -!- FUNCTION: Regulatory subunit of pyrophosphate--fructose 6-phosphate 1-
CC       phosphotransferase.
else case <OC:Viridiplantae> and <FT:1>
CC   -!- FUNCTION: Catalytic subunit of pyrophosphate--fructose 6-phosphate 1-
CC       phosphotransferase. Catalyzes the phosphorylation of D-fructose 6-
CC       phosphate, the first committing step of glycolysis. Uses inorganic
CC       phosphate (PPi) as phosphoryl donor instead of ATP like common ATP-
CC       dependent phosphofructokinases (ATP-PFKs), which renders the reaction
CC       reversible, and can thus function both in glycolysis and
CC       gluconeogenesis.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=beta-D-fructose 6-phosphate + diphosphate = beta-D-fructose
CC         1,6-bisphosphate + H(+) + phosphate; Xref=Rhea:RHEA:13613,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:32966, ChEBI:CHEBI:33019,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:57634; EC=2.7.1.90;
else case <FT:1>
CC   -!- FUNCTION: Catalyzes the phosphorylation of D-fructose 6-phosphate, the
CC       first committing step of glycolysis. Uses inorganic phosphate (PPi) as
CC       phosphoryl donor instead of ATP like common ATP-dependent
CC       phosphofructokinases (ATP-PFKs), which renders the reaction reversible,
CC       and can thus function both in glycolysis and gluconeogenesis.
CC       Consistently, PPi-PFK can replace the enzymes of both the forward (ATP-
CC       PFK) and reverse (fructose-bisphosphatase (FBPase)) reactions.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=beta-D-fructose 6-phosphate + diphosphate = beta-D-fructose
CC         1,6-bisphosphate + H(+) + phosphate; Xref=Rhea:RHEA:13613,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:32966, ChEBI:CHEBI:33019,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:57634; EC=2.7.1.90;
CC   -!- ACTIVITY REGULATION: Non-allosteric.
else case <FT:2>
CC   -!- FUNCTION: Catalyzes the phosphorylation of D-fructose 6-phosphate to
CC       fructose 1,6-bisphosphate by ATP, the first committing step of
CC       glycolysis.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + beta-D-fructose 6-phosphate = ADP + beta-D-fructose 1,6-
CC         bisphosphate + H(+); Xref=Rhea:RHEA:16109, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:32966, ChEBI:CHEBI:57634,
CC         ChEBI:CHEBI:456216; EC=2.7.1.11;
else
CC   -!- FUNCTION: Catalyzes the phosphorylation of D-fructose 6-phosphate to
CC       fructose 1,6-bisphosphate, the first committing step of glycolysis.
end case
case <OC:Viridiplantae>
CC   -!- ACTIVITY REGULATION: Allosterically activated by fructose 2,6-
CC       bisphosphate.
end case
case <FT:1> or <FT:2>
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
end case
CC   -!- PATHWAY: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-
CC       phosphate and glycerone phosphate from D-glucose: step 3/4.
case (<OC:Viridiplantae> or <OC:Apicomplexa>)
CC   -!- SUBUNIT: Tetramer of two alpha (regulatory) and two beta (catalytic)
CC       chains.
else
CC   -!- SUBUNIT: Homodimer or monomer.
end case
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- SIMILARITY: Belongs to the phosphofructokinase type A (PFKA) family.
CC       PPi-dependent PFK group II subfamily. Clade 'Long' sub-subfamily.
XX
DR   Pfam; PF00365; PFK; 1; trigger=no
DR   PIRSF; PIRSF005677; PPi_PFK_PfpB; 1; trigger=no
DR   PRINTS; PR00476; PHFRCTKINASE; 1; trigger=no
DR   NCBIfam; TIGR02477; PFKA_PPi; 1; trigger=no
XX
case <OC:Viridiplantae>
KW   Allosteric enzyme
end case
KW   Cytoplasm
KW   Kinase
KW   Transferase
KW   Glycolysis
KW   Magnesium
KW   Metal-binding
case <FT:2>
KW   ATP-binding
KW   Nucleotide-binding
end case
XX
GO   GO:0003872; F:6-phosphofructokinase activity
GO   GO:0006096; P:glycolytic process
GO   GO:0005737; C:cytoplasm
XX
FT   From: PFP_ENTH1 (C4LZC2)
FT   SITE            175
FT                   /note="Important for catalytic activity and substrate
FT                   specificity; stabilizes the transition state when the
FT                   phosphoryl donor is PPi; prevents ATP from binding by
FT                   mimicking the alpha-phosphate group of ATP"
FT   Optional; Condition: [DN]
FT   SITE            175
FT                   /note="Important for substrate specificity; cannot use PPi
FT                   as phosphoryl donor"
FT   Optional; Condition: G
case <FT:1>
FT   BINDING         80
FT                   /ligand="diphosphate"
FT                   /ligand_id="ChEBI:CHEBI:33019"
FT   Condition: G
FT   SITE            201
FT                   /note="Important for catalytic activity; stabilizes the
FT                   transition state when the phosphoryl donor is PPi"
FT   Condition: K
else case <FT:2>
FT   BINDING         144..145
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT   Condition: [RK]-x
FT   BINDING         173..176
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT   Condition: G-[DE]-G-[ST]
FT   BINDING         80
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT   Condition: G
end case
case <FT:1> or <FT:2>
FT   BINDING         202..204
FT                   /ligand="substrate"
FT   Condition: T-x-D
FT   BINDING         241..242
FT                   /ligand="substrate"
FT                   /ligand_note="ligand shared between dimeric partners"
FT   Optional; Condition: K-Y
FT   BINDING         249..251
FT                   /ligand="substrate"
FT   Condition: M-G-[RH]
FT   BINDING         420..423
FT                   /ligand="substrate"
FT   Condition: [HY]-x(2)-R
FT   ACT_SITE        204
FT                   /note="Proton acceptor"
FT   Condition: D
FT   BINDING         174
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_note="catalytic"
FT   Condition: [DE]
FT   BINDING         310
FT                   /ligand="substrate"
FT   Condition: E
end case
XX
Size: 544-1426;
Related: MF_01980;
Template: C4LZC2; P70826;
Scope:
 Eukaryota
Fusion:
 Nter: None
 Cter: None
Duplicate: in ARATH, PLAKH, PLAVS, PLAYO, RICCO, SOLTU
Plasmid: None
Comments: Classification of type A phosphofructokinases into subfamilies
 was done according to Mueller at al.(2001) (PubMed:11673446) and
 Bapteste et al.(2003) (PubMed:14585511).
 Phosphoryl donor specificity (ATP or PPi) seems to be determined by
 a single residue, Asp or Gly-175 (PFP_ENTH1 numbering) according to
 Chi et al.(2000) (PubMeed:11001940), Moore et al.(2002) (PubMed:12015149),
 and Bapteste et al.(2003) (PubMed:14585511) and references therein.
XX
# Revision 1.13 2023/06/01
//