ID GLPK_ENTCA Reviewed; 506 AA.
AC O34153;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 24-JAN-2024, entry version 119.
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};
OS Enterococcus casseliflavus (Enterococcus flavescens).
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Enterococcaceae;
OC Enterococcus.
OX NCBI_TaxID=37734;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, PHOSPHORYLATION AT HIS-232,
RP MUTAGENESIS OF HIS-232, AND ACTIVITY REGULATION.
RC STRAIN=ATCC 12755 / DSM 4841 / NCFB 2725 / 491;
RX PubMed=9162046; DOI=10.1074/jbc.272.22.14166;
RA Charrier V., Buckley E., Parsonage D., Galinier A., Darbon E., Jaquinod M.,
RA Forest E., Deutscher J., Claiborne A.;
RT "Cloning and sequencing of two enterococcal glpK genes and regulation of
RT the encoded glycerol kinases by phosphoenolpyruvate-dependent,
RT phosphotransferase system-catalyzed phosphorylation of a single histidyl
RT residue.";
RL J. Biol. Chem. 272:14166-14174(1997).
RN [2] {ECO:0007744|PDB:1R59, ECO:0007744|PDB:1XUP}
RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) IN SUBSTRATE-FREE FORM AND IN COMPLEX
RP WITH GLYCEROL, ACTIVITY REGULATION, AND SUBUNIT.
RX PubMed=14717590; DOI=10.1021/bi034258o;
RA Yeh J.I., Charrier V., Paulo J., Hou L., Darbon E., Claiborne A.,
RA Hol W.G.J., Deutscher J.;
RT "Structures of enterococcal glycerol kinase in the absence and presence of
RT glycerol: correlation of conformation to substrate binding and a mechanism
RT of activation by phosphorylation.";
RL Biochemistry 43:362-373(2004).
RN [3] {ECO:0007744|PDB:3D7E, ECO:0007744|PDB:3FLC, ECO:0007744|PDB:3H3N, ECO:0007744|PDB:3H3O, ECO:0007744|PDB:3H45, ECO:0007744|PDB:3H46}
RP X-RAY CRYSTALLOGRAPHY (2.03 ANGSTROMS) OF MUTANTS ARG-232; GLU-232 AND
RP ALA-232 IN COMPLEX WITH GLYCEROL, MUTAGENESIS OF HIS-232, AND SUBUNIT.
RX PubMed=19102629; DOI=10.1021/bi8009407;
RA Yeh J.I., Kettering R., Saxl R., Bourand A., Darbon E., Joly N.,
RA Briozzo P., Deutscher J.;
RT "Structural characterizations of glycerol kinase: unraveling
RT phosphorylation-induced long-range activation.";
RL Biochemistry 48:346-356(2009).
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 ECO:0000269|PubMed:9162046}.
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: Activated by phosphorylation and inhibited by
CC fructose 1,6-bisphosphate (FBP). {ECO:0000255|HAMAP-Rule:MF_00186,
CC ECO:0000269|PubMed:14717590, ECO:0000269|PubMed:9162046}.
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).
CC {ECO:0000255|HAMAP-Rule:MF_00186, ECO:0000269|PubMed:14717590,
CC ECO:0000269|PubMed:19102629}.
CC -!- PTM: The phosphoenolpyruvate-dependent sugar phosphotransferase system
CC (PTS), including enzyme I, and histidine-containing protein (HPr) are
CC required for the phosphorylation of His-232, which leads to the
CC activation of the enzyme. {ECO:0000269|PubMed:9162046}.
CC -!- SIMILARITY: Belongs to the FGGY kinase family. {ECO:0000255|HAMAP-
CC Rule:MF_00186}.
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DR EMBL; U94355; AAB69985.1; -; Genomic_DNA.
DR PDB; 1R59; X-ray; 2.50 A; O/X=2-506.
DR PDB; 1XUP; X-ray; 2.75 A; O/X=6-492.
DR PDB; 3D7E; X-ray; 2.03 A; O/X=2-506.
DR PDB; 3FLC; X-ray; 1.85 A; O/X=1-506.
DR PDB; 3H3N; X-ray; 1.73 A; O/X=1-506.
DR PDB; 3H3O; X-ray; 2.30 A; B/C/O/X=1-506.
DR PDB; 3H45; X-ray; 2.65 A; C/D/O/X=1-506.
DR PDB; 3H46; X-ray; 1.75 A; O/X=1-506.
DR PDBsum; 1R59; -.
DR PDBsum; 1XUP; -.
DR PDBsum; 3D7E; -.
DR PDBsum; 3FLC; -.
DR PDBsum; 3H3N; -.
DR PDBsum; 3H3O; -.
DR PDBsum; 3H45; -.
DR PDBsum; 3H46; -.
DR AlphaFoldDB; O34153; -.
DR SMR; O34153; -.
DR iPTMnet; O34153; -.
DR UniPathway; UPA00618; UER00672.
DR EvolutionaryTrace; O34153; -.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004370; F:glycerol kinase activity; ISS:UniProtKB.
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 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Glycerol metabolism; Kinase; Nucleotide-binding;
KW Phosphoprotein; Transferase.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250"
FT CHAIN 2..506
FT /note="Glycerol kinase"
FT /id="PRO_0000059454"
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 ECO:0000269|PubMed:14717590, ECO:0000269|PubMed:19102629,
FT ECO:0007744|PDB:1XUP, ECO:0007744|PDB:3D7E"
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 ECO:0000269|PubMed:14717590, ECO:0000269|PubMed:19102629,
FT ECO:0007744|PDB:1XUP, ECO:0007744|PDB:3D7E"
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 ECO:0000269|PubMed:14717590, ECO:0000269|PubMed:19102629,
FT ECO:0007744|PDB:1XUP, ECO:0007744|PDB:3D7E"
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 ECO:0000269|PubMed:14717590, ECO:0000269|PubMed:19102629,
FT ECO:0007744|PDB:1XUP, ECO:0007744|PDB:3D7E"
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 ECO:0000269|PubMed:19102629, ECO:0007744|PDB:3D7E"
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"
FT MOD_RES 232
FT /note="Phosphohistidine; by HPr"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00186,
FT ECO:0000269|PubMed:9162046"
FT MUTAGEN 232
FT /note="H->A: Loss of phosphorylation, no effect on
FT activity."
FT /evidence="ECO:0000269|PubMed:19102629,
FT ECO:0000269|PubMed:9162046"
FT MUTAGEN 232
FT /note="H->E: Loss of phosphorylation, 2.5-fold reduced
FT activity."
FT /evidence="ECO:0000269|PubMed:19102629,
FT ECO:0000269|PubMed:9162046"
FT MUTAGEN 232
FT /note="H->R: Loss of phosphorylation, 3.4-fold increased
FT activity."
FT /evidence="ECO:0000269|PubMed:19102629,
FT ECO:0000269|PubMed:9162046"
FT STRAND 6..12
FT /evidence="ECO:0007829|PDB:3H3N"
FT STRAND 14..23
FT /evidence="ECO:0007829|PDB:3H3N"
FT STRAND 24..26
FT /evidence="ECO:0007829|PDB:1R59"
FT STRAND 28..35
FT /evidence="ECO:0007829|PDB:3H3N"
FT HELIX 50..68
FT /evidence="ECO:0007829|PDB:3H3N"
FT HELIX 72..74
FT /evidence="ECO:0007829|PDB:3H3N"
FT STRAND 75..82
FT /evidence="ECO:0007829|PDB:3H3N"
FT STRAND 87..91
FT /evidence="ECO:0007829|PDB:3H3N"
FT TURN 92..94
FT /evidence="ECO:0007829|PDB:3H3N"
FT STRAND 97..99
FT /evidence="ECO:0007829|PDB:3H3N"
FT HELIX 110..118
FT /evidence="ECO:0007829|PDB:3H3N"
FT HELIX 122..129
FT /evidence="ECO:0007829|PDB:3H3N"
FT STRAND 135..137
FT /evidence="ECO:0007829|PDB:1XUP"
FT HELIX 138..148
FT /evidence="ECO:0007829|PDB:3H3N"
FT STRAND 149..151
FT /evidence="ECO:0007829|PDB:1XUP"
FT HELIX 152..157
FT /evidence="ECO:0007829|PDB:3H3N"
FT STRAND 161..164
FT /evidence="ECO:0007829|PDB:3H3N"
FT HELIX 166..174
FT /evidence="ECO:0007829|PDB:3H3N"
FT TURN 175..177
FT /evidence="ECO:0007829|PDB:3H3N"
FT STRAND 181..183
FT /evidence="ECO:0007829|PDB:3H3N"
FT HELIX 184..188
FT /evidence="ECO:0007829|PDB:3H3N"
FT TURN 189..191
FT /evidence="ECO:0007829|PDB:3H3N"
FT STRAND 192..194
FT /evidence="ECO:0007829|PDB:3H3N"
FT TURN 195..198
FT /evidence="ECO:0007829|PDB:3H3N"
FT HELIX 202..207
FT /evidence="ECO:0007829|PDB:3H3N"
FT HELIX 212..214
FT /evidence="ECO:0007829|PDB:3H3N"
FT STRAND 217..219
FT /evidence="ECO:0007829|PDB:3H3N"
FT STRAND 221..227
FT /evidence="ECO:0007829|PDB:3H3N"
FT HELIX 230..232
FT /evidence="ECO:0007829|PDB:3H3N"
FT TURN 233..235
FT /evidence="ECO:0007829|PDB:3H3N"
FT STRAND 239..245
FT /evidence="ECO:0007829|PDB:3H3N"
FT HELIX 246..253
FT /evidence="ECO:0007829|PDB:3H3N"
FT STRAND 262..277
FT /evidence="ECO:0007829|PDB:3H3N"
FT TURN 284..286
FT /evidence="ECO:0007829|PDB:3D7E"
FT STRAND 287..295
FT /evidence="ECO:0007829|PDB:3H3N"
FT STRAND 298..307
FT /evidence="ECO:0007829|PDB:3H3N"
FT HELIX 312..319
FT /evidence="ECO:0007829|PDB:3H3N"
FT STRAND 324..327
FT /evidence="ECO:0007829|PDB:3H46"
FT HELIX 329..334
FT /evidence="ECO:0007829|PDB:3H3N"
FT STRAND 335..339
FT /evidence="ECO:0007829|PDB:1R59"
FT STRAND 344..346
FT /evidence="ECO:0007829|PDB:3H3N"
FT STRAND 349..351
FT /evidence="ECO:0007829|PDB:1XUP"
FT TURN 354..356
FT /evidence="ECO:0007829|PDB:3H3N"
FT STRAND 364..366
FT /evidence="ECO:0007829|PDB:3H3N"
FT HELIX 374..400
FT /evidence="ECO:0007829|PDB:3H3N"
FT STRAND 406..411
FT /evidence="ECO:0007829|PDB:3H3N"
FT HELIX 412..415
FT /evidence="ECO:0007829|PDB:3H3N"
FT HELIX 417..427
FT /evidence="ECO:0007829|PDB:3H3N"
FT STRAND 429..433
FT /evidence="ECO:0007829|PDB:3H3N"
FT STRAND 435..437
FT /evidence="ECO:0007829|PDB:3H3N"
FT HELIX 439..451
FT /evidence="ECO:0007829|PDB:3H3N"
FT HELIX 458..462
FT /evidence="ECO:0007829|PDB:3H3N"
FT STRAND 467..471
FT /evidence="ECO:0007829|PDB:3FLC"
FT HELIX 477..496
FT /evidence="ECO:0007829|PDB:3H3N"
SQ SEQUENCE 506 AA; 55760 MW; F0B557C6F5AF3B3E CRC64;
MAEKNYVMAI DQGTTSSRAI IFDRNGKKIG SSQKEFPQYF PKSGWVEHNA NEIWNSVQSV
IAGAFIESGI RPEAIAGIGI TNQRETTVVW DKTTGQPIAN AIVWQSRQSS PIADQLKVDG
HTEMIHEKTG LVIDAYFSAT KVRWLLDNIE GAQEKADNGE LLFGTIDSWL VWKLTDGQVH
VTDYSNASRT MLYNIHKLEW DQEILDLLNI PSSMLPEVKS NSEVYGHTRS YHFYGSEVPI
AGMAGDQQAA LFGQMAFEKG MIKNTYGTGA FIVMNTGEEP QLSDNDLLTT IGYGINGKVY
YALEGSIFVA GSAIQWLRDG LRMIETSPQS EELAAKAKGD NEVYVVPAFT GLGAPYWDSE
ARGAVFGLTR GTTKEDFVRA TLQAVAYQSK DVIDTMKKDS GIDIPLLKVD GGAAKNDLLM
QFQADILDID VQRAANLETT ALGAAYLAGL AVGFWKDLDE LKSMAEEGQM FTPEMPAEER
DNLYEGWKQA VAATQTFKFK AKKEGE
//
