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HAMAP rule MF_00186

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General rule information [?]

Accession MF_00186
Dates 1-JUN-2001 (Created)
16-OCT-2023 (Last updated, Version 41)
Name Glycerol_kin
Scope(s) Bacteria
Archaea
Template(s) P0A6F3 (GLPK_ECOLI); P18157 (GLPK_BACSU); O34153 (GLPK_ENTCA); O34154 (GLPK_ENTFA); Q9WX53 (GLPK_THEAQ); O66131 (GLPK_THETH); O93623 (GLPK_THEKO); [ Recover all ]
Triggered by HAMAP; MF_00186 (Get profile general information and statistics)

Propagated annotation [?]

Identifier, protein and gene names [?]

Identifier GLPK
Protein name RecName: Full=Glycerol kinase;
                 EC=2.7.1.30;
AltName: Full=ATP:glycerol 3-phosphotransferase;
AltName: Full=Glycerokinase;
                 Short=GK;
Gene name Name=glpK;

Comments [?]

FUNCTIONKey enzyme in the regulation of glycerol uptake and metabolism. Catalyzes the phosphorylation of glycerol to yield sn- glycerol 3-phosphate.
CATALYTIC ACTIVITY Reaction=ATP + glycerol = ADP + H(+) + sn-glycerol 3-phosphate; Xref=Rhea:RHEA:21644, ChEBI:CHEBI:15378, ChEBI:CHEBI:17754, ChEBI:CHEBI:30616, ChEBI:CHEBI:57597, ChEBI:CHEBI:456216; EC=2.7.1.30;
case <OC:Enterobacterales>
ACTIVITY REGULATIONActivity of this regulatory enzyme is affected by several metabolites. Allosterically and non-competitively inhibited by fructose 1,6-bisphosphate (FBP) and unphosphorylated phosphocarrier protein EIIA-Glc (III-Glc), an integral component of the bacterial phosphotransferase (PTS) system.
else case <OC:Bacillota>
ACTIVITY REGULATIONActivated by phosphorylation and inhibited by fructose 1,6-bisphosphate (FBP).
else case not <OC:Archaea>
ACTIVITY REGULATIONInhibited by fructose 1,6-bisphosphate (FBP).
end case
PATHWAYPolyol metabolism; glycerol degradation via glycerol kinase pathway; sn-glycerol 3-phosphate from glycerol: step 1/1.
case <OC:Enterobacterales>
SUBUNITHomotetramer and homodimer (in equilibrium). Heterodimer with EIIA-Glc. Binds 1 zinc ion per glycerol kinase EIIA-Glc dimer. The zinc ion is important for dimerization.
else case <OC:Bacillota>
SUBUNITHomotetramer and homodimer (in equilibrium).
end case
case <FTGroup:1>
PTMThe phosphoenolpyruvate-dependent sugar phosphotransferase system (PTS), including enzyme I, and histidine-containing protein (HPr) are required for the phosphorylation, which leads to the activation of the enzyme.
end case
SIMILARITYBelongs to the FGGY kinase family.

Keywords [?]

case <OC:Enterobacterales>
Allosteric enzyme
Metal-binding
Zinc
end case
Glycerol metabolism
Transferase
Kinase
ATP-binding
Nucleotide-binding
case <FTGroup:1>
Phosphoprotein
end case

Gene Ontology [?]

GO:0005524; Molecular function:ATP binding
GO:0004370; Molecular function:glycerol kinase activity
GO:0006072; Biological process:glycerol-3-phosphate metabolic process

Cross-references [?]

PROSITE PS00933; FGGY_KINASES_1; 1;
PROSITE PS00445; FGGY_KINASES_2; 1;
Pfam PF02782; FGGY_C; 1;
Pfam PF00370; FGGY_N; 1;
NCBIfam TIGR01311; Glycerol_kin; 1;

Features [?]

From: GLPK_ECOLI (P0A6F3)
Key From To Description Tag Condition FTGroup
case <OC:Enterobacterales>
BINDING 479 479 /ligand="Zn(2+)"
/ligand_id="ChEBI:CHEBI:29105"
/ligand_note="ligand shared with EIIA-Glc"		 E
BINDING 235 235 /ligand="beta-D-fructose 1,6-bisphosphate"
/ligand_id="ChEBI:CHEBI:32966"
/ligand_note="allosteric inhibitor"		 G
BINDING 237 237 /ligand="beta-D-fructose 1,6-bisphosphate"
/ligand_id="ChEBI:CHEBI:32966"
/ligand_note="allosteric inhibitor"		 R
end case
BINDING 14 14 /ligand="ADP"
/ligand_id="ChEBI:CHEBI:456216"		 [TS]
BINDING 14 14 /ligand="ATP"
/ligand_id="ChEBI:CHEBI:30616"		 [TS]
BINDING 14 14 /ligand="sn-glycerol 3-phosphate"
/ligand_id="ChEBI:CHEBI:57597"		 [TS]
BINDING 15 15 /ligand="ATP"
/ligand_id="ChEBI:CHEBI:30616"		 [TS]
BINDING 16 16 /ligand="ATP"
/ligand_id="ChEBI:CHEBI:30616"		 [ST]
BINDING 18 18 /ligand="ADP"
/ligand_id="ChEBI:CHEBI:456216"		 [RK]
BINDING 84 84 /ligand="glycerol"
/ligand_id="ChEBI:CHEBI:17754"		 R
BINDING 84 84 /ligand="sn-glycerol 3-phosphate"
/ligand_id="ChEBI:CHEBI:57597"		 R
BINDING 85 85 /ligand="glycerol"
/ligand_id="ChEBI:CHEBI:17754"		 E
BINDING 85 85 /ligand="sn-glycerol 3-phosphate"
/ligand_id="ChEBI:CHEBI:57597"		 E
BINDING 136 136 /ligand="glycerol"
/ligand_id="ChEBI:CHEBI:17754"		 Y
BINDING 136 136 /ligand="sn-glycerol 3-phosphate"
/ligand_id="ChEBI:CHEBI:57597"		 Y
BINDING 246 246 /ligand="glycerol"
/ligand_id="ChEBI:CHEBI:17754"		 D
BINDING 246 246 /ligand="sn-glycerol 3-phosphate"
/ligand_id="ChEBI:CHEBI:57597"		 D
BINDING 247 247 /ligand="glycerol"
/ligand_id="ChEBI:CHEBI:17754"		 Q
BINDING 268 268 /ligand="ADP"
/ligand_id="ChEBI:CHEBI:456216"		 T
BINDING 268 268 /ligand="ATP"
/ligand_id="ChEBI:CHEBI:30616"		 T
BINDING 311 311 /ligand="ADP"
/ligand_id="ChEBI:CHEBI:456216"		 G
BINDING 311 311 /ligand="ATP"
/ligand_id="ChEBI:CHEBI:30616"		 G
BINDING 315 315 /ligand="ATP"
/ligand_id="ChEBI:CHEBI:30616"		 Q
BINDING 412 412 /ligand="ADP"
/ligand_id="ChEBI:CHEBI:456216"		 [GA]
BINDING 412 412 /ligand="ATP"
/ligand_id="ChEBI:CHEBI:30616"		 [GA]
BINDING 416 416 /ligand="ADP"
/ligand_id="ChEBI:CHEBI:456216"		 N
From: GLPK_ENTCA (O34153)
Key From To Description Tag Condition FTGroup
case <OC:Bacilli>
MOD_RES 232 232 /note="Phosphohistidine; by HPr" H 1
end case

Additional information [?]

Size range 490-517 amino acids
Related rules None
Fusion Nter: None Cter: None
Comments Possible wrong start in RHOBA; sequence not included in alignment and not taken into account in size range. There is a possible divergent glpK in ARCFU: AF0866.



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