HAMAP logo

HAMAP rule MF_03184

Send feedback

General rule information [?]

Accession MF_03184
Dates 16-MAY-2014 (Created)
1-JUN-2023 (Last updated, Version 14)
Name Phosphofructokinase_I_E
Scope(s) Eukaryota
Template(s) P16861 (PFKA1_YEAST); P16862 (PFKA2_YEAST); P90521 (PFKA_DICDI); P17858 (PFKAL_HUMAN); P08237 (PFKAM_HUMAN); P00511 (PFKAM_RABIT); [ Recover all ]
Triggered by HAMAP; MF_03184 (Get profile general information and statistics)

Propagated annotation [?]

Identifier, protein and gene names [?]

Identifier PFKA
Protein name RecName: Full=ATP-dependent 6-phosphofructokinase;
                 Short=ATP-PFK;
                 Short=Phosphofructokinase;
                 EC=2.7.1.11;
AltName: Full=Phosphohexokinase;

Comments [?]

FUNCTIONCatalyzes the phosphorylation of D-fructose 6-phosphate to fructose 1,6-bisphosphate by ATP, the first committing step of glycolysis.
CATALYTIC ACTIVITY Reaction=ATP + beta-D-fructose 6-phosphate = ADP + beta-D-fructose 1,6- bisphosphate + H(+); Xref=Rhea:RHEA:16109, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:32966, ChEBI:CHEBI:57634, ChEBI:CHEBI:456216; EC=2.7.1.11;
COFACTOR Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
ACTIVITY REGULATIONAllosterically activated by ADP, AMP, or fructose 2,6-bisphosphate, and allosterically inhibited by ATP or citrate.
PATHWAYCarbohydrate degradation; glycolysis; D-glyceraldehyde 3- phosphate and glycerone phosphate from D-glucose: step 3/4.
case <OC:Saccharomycetales>
SUBUNITHeterooctamer of 4 alpha and 4 beta chains.
else case <OC:Vertebrata>
SUBUNITHomo- and heterotetramers.
else
SUBUNITHomotetramer.
end case
SUBCELLULAR LOCATIONCytoplasm.
SIMILARITYBelongs to the phosphofructokinase type A (PFKA) family. ATP-dependent PFK group I subfamily. Eukaryotic two domain clade 'E' sub-subfamily.

Keywords [?]

Allosteric enzyme
Cytoplasm
Kinase
Transferase
Glycolysis
ATP-binding
Nucleotide-binding
Magnesium
Metal-binding

Gene Ontology [?]

GO:0003872; Molecular function:6-phosphofructokinase activity
GO:0006096; Biological process:glycolytic process
GO:0005737; Cellular component:cytoplasm

Cross-references [?]

Pfam PF00365; PFK; 2;
PIRSF PIRSF000533; ATP_PFK_euk; 1;
PRINTS PR00476; PHFRCTKINASE; 1;
NCBIfam TIGR02478; 6PF1K_euk; 1;
PROSITE PS00433; PHOSPHOFRUCTOKINASE; 1;

Features [?]

From: PFKA1_YEAST (P16861)
Key From To Description Tag Condition FTGroup
BINDING 278 279 /ligand="ATP"
/ligand_id="ChEBI:CHEBI:30616"		 R-x
BINDING 308 311 /ligand="ATP"
/ligand_id="ChEBI:CHEBI:30616"		 G-[DE]-G-[ST]
REGION Nter 580 /note="N-terminal catalytic PFK domain 1"
BINDING 354 356 /ligand="substrate"
/ligand_note="ligand shared between dimeric partners"
/note="in other chain"		 S-x-D
BINDING 398 400 /ligand="substrate"
/ligand_note="ligand shared between dimeric partners"
/note="in other chain"		 M-G-R
BINDING 488 491 /ligand="substrate"
/ligand_note="ligand shared between dimeric partners"
/note="in other chain"		 H-x(2)-R
REGION 581 594 /note="Interdomain linker"
REGION 595 Cter /note="C-terminal regulatory PFK domain 2"
BINDING 722 726 /ligand="beta-D-fructose 2,6-bisphosphate"
/ligand_id="ChEBI:CHEBI:58579"
/ligand_note="allosteric activator; ligand shared between dimeric partners"
/note="in other chain"		 [TS]-[ILMV]-S-N-N
BINDING 767 769 /ligand="beta-D-fructose 2,6-bisphosphate"
/ligand_id="ChEBI:CHEBI:58579"
/ligand_note="allosteric activator; ligand shared between dimeric partners"
/note="in other chain"		 [MQ]-G-[GA]
BINDING 859 862 /ligand="beta-D-fructose 2,6-bisphosphate"
/ligand_id="ChEBI:CHEBI:58579"
/ligand_note="allosteric activator; ligand shared between dimeric partners"
/note="in other chain"		 H-x-Q-Q
ACT_SITE 356 356 /note="Proton acceptor" D
BINDING 309 309 /ligand="Mg(2+)"
/ligand_id="ChEBI:CHEBI:18420"
/ligand_note="catalytic"		 [DE]
BINDING 215 215 /ligand="ATP"
/ligand_id="ChEBI:CHEBI:30616"		 G
BINDING 391 391 /ligand="substrate"
/ligand_note="ligand shared between dimeric partners"		 R
BINDING 455 455 /ligand="substrate"
/ligand_note="ligand shared between dimeric partners"
/note="in other chain"		 E
BINDING 482 482 /ligand="substrate"
/ligand_note="ligand shared between dimeric partners"		 [RK]
BINDING 665 665 /ligand="beta-D-fructose 2,6-bisphosphate"
/ligand_id="ChEBI:CHEBI:58579"
/ligand_note="allosteric activator; ligand shared between dimeric partners"
/note="in other chain"		 [RK]
BINDING 760 760 /ligand="beta-D-fructose 2,6-bisphosphate"
/ligand_id="ChEBI:CHEBI:58579"
/ligand_note="allosteric activator; ligand shared between dimeric partners"		 R
BINDING 827 827 /ligand="beta-D-fructose 2,6-bisphosphate"
/ligand_id="ChEBI:CHEBI:58579"
/ligand_note="allosteric activator; ligand shared between dimeric partners"
/note="in other chain"		 [ED]
BINDING 853 853 /ligand="beta-D-fructose 2,6-bisphosphate"
/ligand_id="ChEBI:CHEBI:58579"
/ligand_note="allosteric activator; ligand shared between dimeric partners"		 [RK]
BINDING 952 952 /ligand="beta-D-fructose 2,6-bisphosphate"
/ligand_id="ChEBI:CHEBI:58579"
/ligand_note="allosteric activator; ligand shared between dimeric partners"
/note="in other chain"		 R

Additional information [?]

Size range 756-992 amino acids
Related rules None
Fusion Nter: None Cter: 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).



View rule in raw text format (no links)