ID GLPK_STAAC Reviewed; 498 AA.
AC Q5HGD2;
DT 19-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 15-FEB-2005, sequence version 1.
DT 27-MAR-2024, entry version 105.
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}; OrderedLocusNames=SACOL1320;
OS Staphylococcus aureus (strain COL).
OC Bacteria; Bacillota; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=93062;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=COL;
RX PubMed=15774886; DOI=10.1128/jb.187.7.2426-2438.2005;
RA Gill S.R., Fouts D.E., Archer G.L., Mongodin E.F., DeBoy R.T., Ravel J.,
RA Paulsen I.T., Kolonay J.F., Brinkac L.M., Beanan M.J., Dodson R.J.,
RA Daugherty S.C., Madupu R., Angiuoli S.V., Durkin A.S., Haft D.H.,
RA Vamathevan J.J., Khouri H., Utterback T.R., Lee C., Dimitrov G., Jiang L.,
RA Qin H., Weidman J., Tran K., Kang K.H., Hance I.R., Nelson K.E.,
RA Fraser C.M.;
RT "Insights on evolution of virulence and resistance from the complete genome
RT analysis of an early methicillin-resistant Staphylococcus aureus strain and
RT a biofilm-producing methicillin-resistant Staphylococcus epidermidis
RT strain.";
RL J. Bacteriol. 187:2426-2438(2005).
RN [2] {ECO:0007744|PDB:3G25}
RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) IN COMPLEX WITH GLYCEROL, AND
RP SUBUNIT.
RG Center for structural genomics of infectious diseases (CSGID);
RT "1.9 Angstrom crystal structure of glycerol kinase (glpk) from
RT Staphylococcus aureus in complex with glycerol.";
RL Submitted (JAN-2009) to the PDB data bank.
RN [3] {ECO:0007744|PDB:3GE1}
RP X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) IN COMPLEX WITH GLYCEROL AND ADP, AND
RP SUBUNIT.
RG Center for structural genomics of infectious diseases (CSGID);
RT "2.7 Angstrom crystal structure of glycerol kinase (glpk) from
RT Staphylococcus aureus in complex with ADP and glycerol.";
RL Submitted (FEB-2009) to the PDB data bank.
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 (By similarity). {ECO:0000250}.
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 -!- 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:0000305|Ref.2, ECO:0000305|Ref.3}.
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. {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; CP000046; AAW38149.1; -; Genomic_DNA.
DR RefSeq; WP_000417369.1; NC_002951.2.
DR PDB; 3G25; X-ray; 1.90 A; A/B/C/D=1-498.
DR PDB; 3GE1; X-ray; 2.70 A; A/B/C/D=1-498.
DR PDBsum; 3G25; -.
DR PDBsum; 3GE1; -.
DR AlphaFoldDB; Q5HGD2; -.
DR SMR; Q5HGD2; -.
DR KEGG; sac:SACOL1320; -.
DR HOGENOM; CLU_009281_2_3_9; -.
DR UniPathway; UPA00618; UER00672.
DR EvolutionaryTrace; Q5HGD2; -.
DR Proteomes; UP000000530; Chromosome.
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; 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 CHAIN 1..498
FT /note="Glycerol kinase"
FT /id="PRO_0000059489"
FT BINDING 12
FT /ligand="ADP"
FT /ligand_id="ChEBI:CHEBI:456216"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00186,
FT ECO:0000269|Ref.3, ECO:0007744|PDB:3GE1"
FT BINDING 12
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00186"
FT BINDING 12
FT /ligand="sn-glycerol 3-phosphate"
FT /ligand_id="ChEBI:CHEBI:57597"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00186"
FT BINDING 13
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
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 16
FT /ligand="ADP"
FT /ligand_id="ChEBI:CHEBI:456216"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00186,
FT ECO:0000269|Ref.3, ECO:0007744|PDB:3GE1"
FT BINDING 82
FT /ligand="glycerol"
FT /ligand_id="ChEBI:CHEBI:17754"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00186,
FT ECO:0000269|Ref.2, ECO:0000269|Ref.3, ECO:0007744|PDB:3G25,
FT ECO:0007744|PDB:3GE1"
FT BINDING 82
FT /ligand="sn-glycerol 3-phosphate"
FT /ligand_id="ChEBI:CHEBI:57597"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00186"
FT BINDING 83
FT /ligand="glycerol"
FT /ligand_id="ChEBI:CHEBI:17754"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00186,
FT ECO:0000269|Ref.2, ECO:0000269|Ref.3, ECO:0007744|PDB:3G25,
FT ECO:0007744|PDB:3GE1"
FT BINDING 83
FT /ligand="sn-glycerol 3-phosphate"
FT /ligand_id="ChEBI:CHEBI:57597"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00186"
FT BINDING 134
FT /ligand="glycerol"
FT /ligand_id="ChEBI:CHEBI:17754"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00186,
FT ECO:0000269|Ref.2, ECO:0000269|Ref.3, ECO:0007744|PDB:3G25,
FT ECO:0007744|PDB:3GE1"
FT BINDING 134
FT /ligand="sn-glycerol 3-phosphate"
FT /ligand_id="ChEBI:CHEBI:57597"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00186"
FT BINDING 244
FT /ligand="glycerol"
FT /ligand_id="ChEBI:CHEBI:17754"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00186,
FT ECO:0000269|Ref.2, ECO:0000269|Ref.3, ECO:0007744|PDB:3G25,
FT ECO:0007744|PDB:3GE1"
FT BINDING 244
FT /ligand="sn-glycerol 3-phosphate"
FT /ligand_id="ChEBI:CHEBI:57597"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00186"
FT BINDING 245
FT /ligand="glycerol"
FT /ligand_id="ChEBI:CHEBI:17754"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00186,
FT ECO:0000269|Ref.2, ECO:0000269|Ref.3, ECO:0007744|PDB:3G25,
FT ECO:0007744|PDB:3GE1"
FT BINDING 266
FT /ligand="ADP"
FT /ligand_id="ChEBI:CHEBI:456216"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00186,
FT ECO:0000269|Ref.3, ECO:0007744|PDB:3GE1"
FT BINDING 266
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00186"
FT BINDING 309
FT /ligand="ADP"
FT /ligand_id="ChEBI:CHEBI:456216"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00186,
FT ECO:0000269|Ref.3, ECO:0007744|PDB:3GE1"
FT BINDING 309
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00186"
FT BINDING 313
FT /ligand="ADP"
FT /ligand_id="ChEBI:CHEBI:456216"
FT /evidence="ECO:0000269|Ref.3, ECO:0007744|PDB:3GE1"
FT BINDING 313
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00186"
FT BINDING 410
FT /ligand="ADP"
FT /ligand_id="ChEBI:CHEBI:456216"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00186,
FT ECO:0000269|Ref.3, ECO:0007744|PDB:3GE1"
FT BINDING 410
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00186"
FT BINDING 414
FT /ligand="ADP"
FT /ligand_id="ChEBI:CHEBI:456216"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00186,
FT ECO:0000269|Ref.3, ECO:0007744|PDB:3GE1"
FT MOD_RES 230
FT /note="Phosphohistidine; by HPr"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00186"
FT STRAND 4..10
FT /evidence="ECO:0007829|PDB:3G25"
FT STRAND 12..20
FT /evidence="ECO:0007829|PDB:3G25"
FT STRAND 26..33
FT /evidence="ECO:0007829|PDB:3G25"
FT HELIX 48..64
FT /evidence="ECO:0007829|PDB:3G25"
FT TURN 65..67
FT /evidence="ECO:0007829|PDB:3G25"
FT HELIX 70..72
FT /evidence="ECO:0007829|PDB:3G25"
FT STRAND 73..80
FT /evidence="ECO:0007829|PDB:3G25"
FT STRAND 85..89
FT /evidence="ECO:0007829|PDB:3G25"
FT TURN 90..92
FT /evidence="ECO:0007829|PDB:3G25"
FT STRAND 95..97
FT /evidence="ECO:0007829|PDB:3G25"
FT HELIX 108..116
FT /evidence="ECO:0007829|PDB:3G25"
FT HELIX 120..127
FT /evidence="ECO:0007829|PDB:3G25"
FT HELIX 136..146
FT /evidence="ECO:0007829|PDB:3G25"
FT HELIX 150..155
FT /evidence="ECO:0007829|PDB:3G25"
FT STRAND 159..163
FT /evidence="ECO:0007829|PDB:3G25"
FT HELIX 164..172
FT /evidence="ECO:0007829|PDB:3G25"
FT TURN 173..175
FT /evidence="ECO:0007829|PDB:3G25"
FT STRAND 179..181
FT /evidence="ECO:0007829|PDB:3G25"
FT HELIX 182..185
FT /evidence="ECO:0007829|PDB:3G25"
FT STRAND 188..192
FT /evidence="ECO:0007829|PDB:3G25"
FT TURN 193..196
FT /evidence="ECO:0007829|PDB:3G25"
FT HELIX 200..206
FT /evidence="ECO:0007829|PDB:3G25"
FT HELIX 210..212
FT /evidence="ECO:0007829|PDB:3G25"
FT STRAND 215..217
FT /evidence="ECO:0007829|PDB:3G25"
FT STRAND 219..225
FT /evidence="ECO:0007829|PDB:3G25"
FT HELIX 228..230
FT /evidence="ECO:0007829|PDB:3G25"
FT TURN 231..233
FT /evidence="ECO:0007829|PDB:3G25"
FT STRAND 237..243
FT /evidence="ECO:0007829|PDB:3G25"
FT HELIX 244..251
FT /evidence="ECO:0007829|PDB:3G25"
FT STRAND 260..273
FT /evidence="ECO:0007829|PDB:3G25"
FT STRAND 282..284
FT /evidence="ECO:0007829|PDB:3G25"
FT STRAND 286..293
FT /evidence="ECO:0007829|PDB:3G25"
FT STRAND 296..306
FT /evidence="ECO:0007829|PDB:3G25"
FT HELIX 310..317
FT /evidence="ECO:0007829|PDB:3G25"
FT HELIX 325..327
FT /evidence="ECO:0007829|PDB:3G25"
FT HELIX 328..332
FT /evidence="ECO:0007829|PDB:3G25"
FT STRAND 342..344
FT /evidence="ECO:0007829|PDB:3G25"
FT TURN 352..354
FT /evidence="ECO:0007829|PDB:3G25"
FT STRAND 361..366
FT /evidence="ECO:0007829|PDB:3G25"
FT HELIX 372..397
FT /evidence="ECO:0007829|PDB:3G25"
FT STRAND 403..409
FT /evidence="ECO:0007829|PDB:3G25"
FT HELIX 410..413
FT /evidence="ECO:0007829|PDB:3G25"
FT HELIX 415..425
FT /evidence="ECO:0007829|PDB:3G25"
FT STRAND 427..433
FT /evidence="ECO:0007829|PDB:3G25"
FT HELIX 437..449
FT /evidence="ECO:0007829|PDB:3G25"
FT STRAND 452..454
FT /evidence="ECO:0007829|PDB:3G25"
FT HELIX 457..462
FT /evidence="ECO:0007829|PDB:3G25"
FT STRAND 465..469
FT /evidence="ECO:0007829|PDB:3G25"
FT HELIX 475..494
FT /evidence="ECO:0007829|PDB:3G25"
SQ SEQUENCE 498 AA; 55626 MW; 6B11099ED0AFB561 CRC64;
MEKYILSIDQ GTTSSRAILF NQKGEIAGVA QREFKQYFPQ SGWVEHDANE IWTSVLAVMT
EVINENDVRA DQIAGIGITN QRETTVVWDK HTGRPIYHAI VWQSRQTQSI CSELKQQGYE
QTFRDKTGLL LDPYFAGTKV KWILDNVEGA REKAENGDLL FGTIDTWLVW KLSGKAAHIT
DYSNASRTLM FNIHDLEWDD ELLELLTVPK NMLPEVKASS EVYGKTIDYH FYGQEVPIAG
VAGDQQAALF GQACFERGDV KNTYGTGGFM LMNTGDKAVK SESGLLTTIA YGIDGKVNYA
LEGSIFVSGS AIQWLRDGLR MINSAPQSES YATRVDSTEG VYVVPAFVGL GTPYWDSEAR
GAIFGLTRGT EKEHFIRATL ESLCYQTRDV MEAMSKDSGI DVQSLRVDGG AVKNNFIMQF
QADIVNTSVE RPEIQETTAL GAAFLAGLAV GFWESKDDIA KNWKLEEKFD PKMDEGEREK
LYRGWKKAVE ATQVFKTE
//
