AC MF_00186; DC Protein; auto TR HAMAP; MF_00186; -; 1; level=0 XX Names: Glycerol_kin XX ID GLPK DE RecName: Full=Glycerol kinase; DE EC=2.7.1.30; DE AltName: Full=ATP:glycerol 3-phosphotransferase; DE AltName: Full=Glycerokinase; DE Short=GK; GN Name=glpK; XX CC -!- FUNCTION: Key enzyme in the regulation of glycerol uptake and CC metabolism. Catalyzes the phosphorylation of glycerol to yield sn- CC glycerol 3-phosphate. CC -!- CATALYTIC ACTIVITY: CC Reaction=ATP + glycerol = ADP + H(+) + sn-glycerol 3-phosphate; CC Xref=Rhea:RHEA:21644, ChEBI:CHEBI:15378, ChEBI:CHEBI:17754, CC ChEBI:CHEBI:30616, ChEBI:CHEBI:57597, ChEBI:CHEBI:456216; CC EC=2.7.1.30; case CC -!- ACTIVITY REGULATION: Activity of this regulatory enzyme is affected by CC several metabolites. Allosterically and non-competitively inhibited by CC fructose 1,6-bisphosphate (FBP) and unphosphorylated phosphocarrier CC protein EIIA-Glc (III-Glc), an integral component of the bacterial CC phosphotransferase (PTS) system. else case CC -!- ACTIVITY REGULATION: Activated by phosphorylation and inhibited by CC fructose 1,6-bisphosphate (FBP). else case not CC -!- ACTIVITY REGULATION: Inhibited by fructose 1,6-bisphosphate (FBP). end case CC -!- PATHWAY: Polyol metabolism; glycerol degradation via glycerol kinase CC pathway; sn-glycerol 3-phosphate from glycerol: step 1/1. case CC -!- SUBUNIT: Homotetramer and homodimer (in equilibrium). Heterodimer with CC EIIA-Glc. Binds 1 zinc ion per glycerol kinase EIIA-Glc dimer. The zinc CC ion is important for dimerization. else case CC -!- SUBUNIT: Homotetramer and homodimer (in equilibrium). end case case CC -!- PTM: The phosphoenolpyruvate-dependent sugar phosphotransferase system CC (PTS), including enzyme I, and histidine-containing protein (HPr) are CC required for the phosphorylation, which leads to the activation of the CC enzyme. end case CC -!- SIMILARITY: Belongs to the FGGY kinase family. XX DR PROSITE; PS00933; FGGY_KINASES_1; 1; trigger=no DR PROSITE; PS00445; FGGY_KINASES_2; 1; trigger=no DR Pfam; PF02782; FGGY_C; 1; trigger=no DR Pfam; PF00370; FGGY_N; 1; trigger=no DR NCBIfam; TIGR01311; Glycerol_kin; 1; trigger=no XX case KW Allosteric enzyme KW Metal-binding KW Zinc end case KW Glycerol metabolism KW Transferase KW Kinase KW ATP-binding KW Nucleotide-binding case KW Phosphoprotein end case XX GO GO:0005524; F:ATP binding GO GO:0004370; F:glycerol kinase activity GO GO:0006072; P:glycerol-3-phosphate metabolic process XX FT From: GLPK_ECOLI (P0A6F3) case FT BINDING 479 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_note="ligand shared with EIIA-Glc" FT Condition: E FT BINDING 235 FT /ligand="beta-D-fructose 1,6-bisphosphate" FT /ligand_id="ChEBI:CHEBI:32966" FT /ligand_note="allosteric inhibitor" FT Condition: G FT BINDING 237 FT /ligand="beta-D-fructose 1,6-bisphosphate" FT /ligand_id="ChEBI:CHEBI:32966" FT /ligand_note="allosteric inhibitor" FT Condition: R end case FT BINDING 14 FT /ligand="ADP" FT /ligand_id="ChEBI:CHEBI:456216" FT Condition: [TS] FT BINDING 14 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT Condition: [TS] FT BINDING 14 FT /ligand="sn-glycerol 3-phosphate" FT /ligand_id="ChEBI:CHEBI:57597" FT Condition: [TS] FT BINDING 15 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT Condition: [TS] FT BINDING 16 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT Optional; Condition: [ST] FT BINDING 18 FT /ligand="ADP" FT /ligand_id="ChEBI:CHEBI:456216" FT Condition: [RK] FT BINDING 84 FT /ligand="glycerol" FT /ligand_id="ChEBI:CHEBI:17754" FT Condition: R FT BINDING 84 FT /ligand="sn-glycerol 3-phosphate" FT /ligand_id="ChEBI:CHEBI:57597" FT Condition: R FT BINDING 85 FT /ligand="glycerol" FT /ligand_id="ChEBI:CHEBI:17754" FT Condition: E FT BINDING 85 FT /ligand="sn-glycerol 3-phosphate" FT /ligand_id="ChEBI:CHEBI:57597" FT Condition: E FT BINDING 136 FT /ligand="glycerol" FT /ligand_id="ChEBI:CHEBI:17754" FT Condition: Y FT BINDING 136 FT /ligand="sn-glycerol 3-phosphate" FT /ligand_id="ChEBI:CHEBI:57597" FT Condition: Y FT BINDING 246 FT /ligand="glycerol" FT /ligand_id="ChEBI:CHEBI:17754" FT Condition: D FT BINDING 246 FT /ligand="sn-glycerol 3-phosphate" FT /ligand_id="ChEBI:CHEBI:57597" FT Condition: D FT BINDING 247 FT /ligand="glycerol" FT /ligand_id="ChEBI:CHEBI:17754" FT Condition: Q FT BINDING 268 FT /ligand="ADP" FT /ligand_id="ChEBI:CHEBI:456216" FT Condition: T FT BINDING 268 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT Condition: T FT BINDING 311 FT /ligand="ADP" FT /ligand_id="ChEBI:CHEBI:456216" FT Condition: G FT BINDING 311 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT Condition: G FT BINDING 315 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT Condition: Q FT BINDING 412 FT /ligand="ADP" FT /ligand_id="ChEBI:CHEBI:456216" FT Condition: [GA] FT BINDING 412 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT Condition: [GA] FT BINDING 416 FT /ligand="ADP" FT /ligand_id="ChEBI:CHEBI:456216" FT Optional; Condition: N FT From: GLPK_ENTCA (O34153) case FT MOD_RES 232 FT /note="Phosphohistidine; by HPr" FT Group: 1; Condition: H end case XX Size: 490-517; Related: None; Template: P0A6F3; P18157; O34153; O34154; Q9WX53; O66131; O93623; Scope: Bacteria Archaea Fusion: Nter: None Cter: None Duplicate: in CLOTE, LACPL, PSEAE, STRAW, STRCO, SACS2, THEMA Plasmid: in RHIME 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. XX # Revision 1.41 2023/10/16 //