GLPK_ENTFA
ID GLPK_ENTFA Reviewed; 501 AA.
AC O34154;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 136.
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=EF_1929;
OS Enterococcus faecalis (strain ATCC 700802 / V583).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Enterococcaceae;
OC Enterococcus.
OX NCBI_TaxID=226185;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 2-19, FUNCTION, AND
RP ACTIVITY REGULATION.
RC STRAIN=26487;
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]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700802 / V583;
RX PubMed=12663927; DOI=10.1126/science.1080613;
RA Paulsen I.T., Banerjei L., Myers G.S.A., Nelson K.E., Seshadri R.,
RA Read T.D., Fouts D.E., Eisen J.A., Gill S.R., Heidelberg J.F., Tettelin H.,
RA Dodson R.J., Umayam L.A., Brinkac L.M., Beanan M.J., Daugherty S.C.,
RA DeBoy R.T., Durkin S.A., Kolonay J.F., Madupu R., Nelson W.C.,
RA Vamathevan J.J., Tran B., Upton J., Hansen T., Shetty J., Khouri H.M.,
RA Utterback T.R., Radune D., Ketchum K.A., Dougherty B.A., Fraser C.M.;
RT "Role of mobile DNA in the evolution of vancomycin-resistant Enterococcus
RT faecalis.";
RL Science 299:2071-2074(2003).
RN [3]
RP PHOSPHORYLATION AT HIS-231.
RX PubMed=3011747; DOI=10.1128/jb.166.3.829-836.1986;
RA Deutscher J., Sauerwald H.;
RT "Stimulation of dihydroxyacetone and glycerol kinase activity in
RT Streptococcus faecalis by phosphoenolpyruvate-dependent phosphorylation
RT catalyzed by enzyme I and HPr of the phosphotransferase system.";
RL J. Bacteriol. 166:829-836(1986).
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: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}.
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-231, which leads to the
CC activation of the enzyme. {ECO:0000269|PubMed:3011747}.
CC -!- SIMILARITY: Belongs to the FGGY kinase family. {ECO:0000255|HAMAP-
CC Rule:MF_00186}.
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DR EMBL; U94356; AAB69986.1; -; Genomic_DNA.
DR EMBL; AE016830; AAO81680.1; -; Genomic_DNA.
DR RefSeq; NP_815610.1; NC_004668.1.
DR RefSeq; WP_002357138.1; NZ_KE136528.1.
DR AlphaFoldDB; O34154; -.
DR SMR; O34154; -.
DR STRING; 226185.EF_1929; -.
DR iPTMnet; O34154; -.
DR EnsemblBacteria; AAO81680; AAO81680; EF_1929.
DR GeneID; 60894171; -.
DR KEGG; efa:EF1929; -.
DR PATRIC; fig|226185.45.peg.1590; -.
DR eggNOG; COG0554; Bacteria.
DR HOGENOM; CLU_009281_2_3_9; -.
DR OMA; FMLMNIG; -.
DR SABIO-RK; O34154; -.
DR UniPathway; UPA00618; UER00672.
DR Proteomes; UP000001415; 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 HAMAP; MF_00186; Glycerol_kin; 1.
DR InterPro; IPR043129; ATPase_NBD.
DR InterPro; IPR000577; Carb_kinase_FGGY.
DR InterPro; IPR018485; Carb_kinase_FGGY_C.
DR InterPro; IPR018483; Carb_kinase_FGGY_CS.
DR InterPro; IPR018484; Carb_kinase_FGGY_N.
DR InterPro; IPR005999; Glycerol_kin.
DR Pfam; PF02782; FGGY_C; 1.
DR Pfam; PF00370; FGGY_N; 1.
DR PIRSF; PIRSF000538; GlpK; 1.
DR SUPFAM; SSF53067; SSF53067; 2.
DR TIGRFAMs; TIGR01311; glycerol_kin; 1.
DR PROSITE; PS00933; FGGY_KINASES_1; 1.
DR PROSITE; PS00445; FGGY_KINASES_2; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Direct protein sequencing; Glycerol metabolism; Kinase;
KW Nucleotide-binding; Phosphoprotein; Reference proteome; Transferase.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:9162046"
FT CHAIN 2..501
FT /note="Glycerol kinase"
FT /id="PRO_0000059455"
FT BINDING 14..16
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00186"
FT BINDING 14
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00186"
FT BINDING 18
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00186"
FT BINDING 84..85
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00186"
FT BINDING 136
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00186"
FT BINDING 245..246
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00186"
FT BINDING 267
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00186"
FT BINDING 310
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00186"
FT BINDING 314
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00186"
FT BINDING 329
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00186"
FT BINDING 411..415
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00186"
FT MOD_RES 231
FT /note="Phosphohistidine; by HPr"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00186,
FT ECO:0000269|PubMed:3011747"
SQ SEQUENCE 501 AA; 55443 MW; F4B0FAB4320F8E3A CRC64;
MAEEKYIMAI DQGTTSSRAI IFDKKGNKIG SSQKEFTQYF PNAGWVEHNA NEIWNSVQSV
IAGSLIESGV KPTDIAGIGI TNQRETTVVW DKATGLPIYN AIVWQSRQTT PIADQLKEDG
YSEMIHEKTG LIIDAYFSAT KVRWILDHVE GAQERAENGE LMFGTIDTWL VWKLTGDTHV
TDYSNASRTM LFNIHDLDWD QEILDLLNIP RVMLPKVVSN SEVYGLTKNY HFYGSEVPIA
GMAGDQQAAL FGQMAFEPGM VKNTYGTGSF IVMNTGEEPQ LSKNNLLTTI GYGINGKVYY
ALEGSIFVAG SAIQWLRDGL KMLQTAAESE AVAKASTGHN EVYVVPAFTG LGAPYWDSQA
RGAVFGLTRG TTREDFVKAT LQAVAYQVRD IIDTMKEDTG IDIPVLKVDG GAANNDFLMQ
FQADILNTAV QRAHNLETTA LGAAFLAGLA VGFWKDLEEI KAFQEEGQQF EPIMAEEERE
DLYEGWQQAV AATQQFKRKN K
