ID GLPK_ECO5E Reviewed; 502 AA.
AC B5YZ64;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 25-NOV-2008, sequence version 1.
DT 27-MAR-2024, entry version 78.
DE RecName: Full=Glycerol kinase {ECO:0000255|HAMAP-Rule:MF_00186};
DE EC=2.7.1.30 {ECO:0000255|HAMAP-Rule:MF_00186};
DE AltName: Full=ATP:glycerol 3-phosphotransferase {ECO:0000255|HAMAP-Rule:MF_00186};
DE AltName: Full=Glycerokinase {ECO:0000255|HAMAP-Rule:MF_00186};
DE Short=GK {ECO:0000255|HAMAP-Rule:MF_00186};
GN Name=glpK {ECO:0000255|HAMAP-Rule:MF_00186};
GN OrderedLocusNames=ECH74115_5381;
OS Escherichia coli O157:H7 (strain EC4115 / EHEC).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=444450;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=EC4115 / EHEC;
RX PubMed=22135463; DOI=10.1073/pnas.1107176108;
RA Eppinger M., Mammel M.K., Leclerc J.E., Ravel J., Cebula T.A.;
RT "Genomic anatomy of Escherichia coli O157:H7 outbreaks.";
RL Proc. Natl. Acad. Sci. U.S.A. 108:20142-20147(2011).
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. {ECO:0000255|HAMAP-Rule:MF_00186}.
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; Evidence={ECO:0000255|HAMAP-Rule:MF_00186};
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. {ECO:0000255|HAMAP-Rule:MF_00186}.
CC -!- PATHWAY: Polyol metabolism; glycerol degradation via glycerol kinase
CC pathway; sn-glycerol 3-phosphate from glycerol: step 1/1.
CC {ECO:0000255|HAMAP-Rule:MF_00186}.
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. {ECO:0000255|HAMAP-Rule:MF_00186}.
CC -!- SIMILARITY: Belongs to the FGGY kinase family. {ECO:0000255|HAMAP-
CC Rule:MF_00186}.
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DR EMBL; CP001164; ACI35872.1; -; Genomic_DNA.
DR RefSeq; WP_000136788.1; NC_011353.1.
DR AlphaFoldDB; B5YZ64; -.
DR SMR; B5YZ64; -.
DR GeneID; 75169366; -.
DR KEGG; ecf:ECH74115_5381; -.
DR HOGENOM; CLU_009281_2_3_6; -.
DR UniPathway; UPA00618; UER00672.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004370; F:glycerol kinase activity; ISS:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0019563; P:glycerol catabolic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0006071; P:glycerol metabolic process; ISS:UniProtKB.
DR GO; GO:0006072; P:glycerol-3-phosphate metabolic process; IEA:UniProtKB-UniRule.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd07786; FGGY_EcGK_like; 1.
DR Gene3D; 3.30.420.40; -; 2.
DR HAMAP; MF_00186; Glycerol_kin; 1.
DR InterPro; IPR043129; ATPase_NBD.
DR InterPro; IPR000577; Carb_kinase_FGGY.
DR InterPro; IPR018483; Carb_kinase_FGGY_CS.
DR InterPro; IPR018485; FGGY_C.
DR InterPro; IPR018484; FGGY_N.
DR InterPro; IPR005999; Glycerol_kin.
DR NCBIfam; TIGR01311; glycerol_kin; 1.
DR PANTHER; PTHR10196:SF69; GLYCEROL KINASE; 1.
DR PANTHER; PTHR10196; SUGAR KINASE; 1.
DR Pfam; PF02782; FGGY_C; 1.
DR Pfam; PF00370; FGGY_N; 1.
DR PIRSF; PIRSF000538; GlpK; 1.
DR SUPFAM; SSF53067; Actin-like ATPase domain; 2.
DR PROSITE; PS00933; FGGY_KINASES_1; 1.
DR PROSITE; PS00445; FGGY_KINASES_2; 1.
PE 3: Inferred from homology;
KW Allosteric enzyme; ATP-binding; Glycerol metabolism; Kinase; Metal-binding;
KW Nucleotide-binding; Transferase; Zinc.
FT CHAIN 1..502
FT /note="Glycerol kinase"
FT /id="PRO_1000098729"
FT BINDING 14
FT /ligand="ADP"
FT /ligand_id="ChEBI:CHEBI:456216"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00186"
FT BINDING 14
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00186"
FT BINDING 14
FT /ligand="sn-glycerol 3-phosphate"
FT /ligand_id="ChEBI:CHEBI:57597"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00186"
FT BINDING 15
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00186"
FT BINDING 16
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00186"
FT BINDING 18
FT /ligand="ADP"
FT /ligand_id="ChEBI:CHEBI:456216"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00186"
FT BINDING 84
FT /ligand="glycerol"
FT /ligand_id="ChEBI:CHEBI:17754"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00186"
FT BINDING 84
FT /ligand="sn-glycerol 3-phosphate"
FT /ligand_id="ChEBI:CHEBI:57597"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00186"
FT BINDING 85
FT /ligand="glycerol"
FT /ligand_id="ChEBI:CHEBI:17754"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00186"
FT BINDING 85
FT /ligand="sn-glycerol 3-phosphate"
FT /ligand_id="ChEBI:CHEBI:57597"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00186"
FT BINDING 136
FT /ligand="glycerol"
FT /ligand_id="ChEBI:CHEBI:17754"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00186"
FT BINDING 136
FT /ligand="sn-glycerol 3-phosphate"
FT /ligand_id="ChEBI:CHEBI:57597"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00186"
FT BINDING 246
FT /ligand="glycerol"
FT /ligand_id="ChEBI:CHEBI:17754"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00186"
FT BINDING 246
FT /ligand="sn-glycerol 3-phosphate"
FT /ligand_id="ChEBI:CHEBI:57597"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00186"
FT BINDING 247
FT /ligand="glycerol"
FT /ligand_id="ChEBI:CHEBI:17754"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00186"
FT BINDING 268
FT /ligand="ADP"
FT /ligand_id="ChEBI:CHEBI:456216"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00186"
FT BINDING 268
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00186"
FT BINDING 311
FT /ligand="ADP"
FT /ligand_id="ChEBI:CHEBI:456216"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00186"
FT BINDING 311
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00186"
FT BINDING 315
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00186"
FT BINDING 412
FT /ligand="ADP"
FT /ligand_id="ChEBI:CHEBI:456216"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00186"
FT BINDING 412
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00186"
FT BINDING 416
FT /ligand="ADP"
FT /ligand_id="ChEBI:CHEBI:456216"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00186"
SQ SEQUENCE 502 AA; 56231 MW; 854B61EA4648AB80 CRC64;
MTEKKYIVAL DQGTTSSRAV VMDHDANIIS VSQREFEQIY PKPGWVEHDP MEIWATQSST
LVEVLAKADI SSDQIAAIGI TNQRETTIVW EKETGKPIYN AIVWQCRRTA EICEHLKRDG
LEDYIRSNTG LVIDPYFSGT KVKWILDHVE GSRERARRGE LLFGTVDTWL IWKMTQGRVH
VTDYTNASRT MLFNIHTLDW DDKMLEVLDI PREMLPEVRR SSEVYGQTNI GGKGGTRIPI
SGIAGDQQAA LFGQLCVKEG MAKNTYGTGC FMLMNTGEKA VKSENGLLTT IACGPTGEVN
YALEGAVFMA GASIQWLRDE MKLINDAYDS EYFATKVQNT NGVYVVPAFT GLGAPYWDPY
ARGAIFGLTR GVNANHIIRA TLESIAYQTR DVLEAMQADS GIRLHALRVD GGAVANNFLM
QFQSDILGTR VERPEVREVT ALGAAYLAGL AVGFWQNLDE LQEKAVIERE FRPGIETTER
NYRYAGWKKA VKRAMAWEEH DE
//
