AC   MF_03186;
DC   Protein; auto
c?   <OC:Eukaryota>
TR   HAMAP; MF_01981; -; 1; level=0
XX
Names: Phosphofructokinase_II_X_euk
XX
ID   PFKA
DE   RecName: Full=ATP-dependent 6-phosphofructokinase;
DE            Short=ATP-PFK;
DE            Short=Phosphofructokinase;
DE            EC=2.7.1.11;
DE   AltName: Full=Phosphohexokinase;
case <OC:Viridiplantae>
GN   Name=PFK;
else case <OC:Kinetoplastea>
GN   Name=pfk;
end case
XX
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;
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC   -!- ACTIVITY REGULATION: Allosterically activated by AMP.
CC   -!- PATHWAY: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-
CC       phosphate and glycerone phosphate from D-glucose: step 3/4.
CC   -!- SUBUNIT: Homotetramer.
case <OC:Kinetoplastea>
CC   -!- SUBCELLULAR LOCATION: Glycosome.
else
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
end case
CC   -!- SIMILARITY: Belongs to the phosphofructokinase type A (PFKA) family.
CC       PPi-dependent PFK group II subfamily. Atypical ATP-dependent clade 'X'
CC       sub-subfamily.
XX
DR   Pfam; PF00365; PFK; 1; trigger=no
DR   PIRSF; PIRSF000534; PPi_PFK_TP0108; 1; trigger=no
DR   PRINTS; PR00476; PHFRCTKINASE; 1; trigger=no
XX
KW   Allosteric enzyme
KW   Kinase
KW   Transferase
KW   Glycolysis
KW   ATP-binding
KW   Nucleotide-binding
KW   Magnesium
KW   Metal-binding
case <OC:Kinetoplastea>
KW   Glycosome
KW   Peroxisome
else
KW   Cytoplasm
end case
XX
GO   GO:0003872; F:6-phosphofructokinase activity
GO   GO:0006096; P:glycolytic process
GO   GO:0005737; C:cytoplasm
XX
FT   From: PFKA_TRYBB (O15648)
FT   SITE            200
FT                   /note="Important for substrate specificity; cannot use PPi
FT                   as phosphoryl donor"
FT   Optional; Condition: G
FT   BINDING         173..174
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT   Condition: [RK]-x
FT   BINDING         198..201
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT   Condition: G-[DENG]-G-[ST]
FT   BINDING         107
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT   Condition: G
FT   BINDING         227..229
FT                   /ligand="substrate"
FT   Condition: T-x-D
FT   BINDING         272..274
FT                   /ligand="substrate"
FT   Condition: M-G-[RH]
FT   BINDING         380..383
FT                   /ligand="substrate"
FT   Condition: [HY]-x(2)-R
FT   ACT_SITE        229
FT                   /note="Proton acceptor"
FT   Condition: D
FT   BINDING         199
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_note="catalytic"
FT   Condition: [DEN]
FT   BINDING         325
FT                   /ligand="substrate"
FT   Condition: E
case <OC:Kinetoplastea>
FT   MOTIF           Cter-2..Cter
FT                   /note="Peroxisomal targeting signal"
FT   Optional; Condition: [AS]-K-[LV]>
end case
XX
Size: 436-537;
Related: MF_01981;
Template: O15648; Q27651; Q9BIC6; Q4E657;
Scope:
 Eukaryota
Fusion:
 Nter: None
 Cter: None
Duplicate: in ARATH
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).
XX
# Revision 1.12 2022/11/19
//