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Glycerol kinase (EC 2.7.1.30) (ATP:glycerol 3-phosphotransferase) (Glycerokinase) (GK)

 GLPK_ENTFA              Reviewed;         501 AA.
O34154;
15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 3.
05-DEC-2018, entry version 122.
RecName: Full=Glycerol kinase {ECO:0000255|HAMAP-Rule:MF_00186};
EC=2.7.1.30 {ECO:0000255|HAMAP-Rule:MF_00186};
AltName: Full=ATP:glycerol 3-phosphotransferase {ECO:0000255|HAMAP-Rule:MF_00186};
AltName: Full=Glycerokinase {ECO:0000255|HAMAP-Rule:MF_00186};
Short=GK {ECO:0000255|HAMAP-Rule:MF_00186};
Name=glpK {ECO:0000255|HAMAP-Rule:MF_00186};
OrderedLocusNames=EF_1929;
Enterococcus faecalis (strain ATCC 700802 / V583).
Bacteria; Firmicutes; Bacilli; Lactobacillales; Enterococcaceae;
Enterococcus.
NCBI_TaxID=226185;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 2-19, FUNCTION,
AND ACTIVITY REGULATION.
STRAIN=26487;
PubMed=9162046; DOI=10.1074/jbc.272.22.14166;
Charrier V., Buckley E., Parsonage D., Galinier A., Darbon E.,
Jaquinod M., Forest E., Deutscher J., Claiborne A.;
"Cloning and sequencing of two enterococcal glpK genes and regulation
of the encoded glycerol kinases by phosphoenolpyruvate-dependent,
phosphotransferase system-catalyzed phosphorylation of a single
histidyl residue.";
J. Biol. Chem. 272:14166-14174(1997).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 700802 / V583;
PubMed=12663927; DOI=10.1126/science.1080613;
Paulsen I.T., Banerjei L., Myers G.S.A., Nelson K.E., Seshadri R.,
Read T.D., Fouts D.E., Eisen J.A., Gill S.R., Heidelberg J.F.,
Tettelin H., Dodson R.J., Umayam L.A., Brinkac L.M., Beanan M.J.,
Daugherty S.C., DeBoy R.T., Durkin S.A., Kolonay J.F., Madupu R.,
Nelson W.C., Vamathevan J.J., Tran B., Upton J., Hansen T., Shetty J.,
Khouri H.M., Utterback T.R., Radune D., Ketchum K.A., Dougherty B.A.,
Fraser C.M.;
"Role of mobile DNA in the evolution of vancomycin-resistant
Enterococcus faecalis.";
Science 299:2071-2074(2003).
[3]
PHOSPHORYLATION AT HIS-231.
PubMed=3011747; DOI=10.1128/jb.166.3.829-836.1986;
Deutscher J., Sauerwald H.;
"Stimulation of dihydroxyacetone and glycerol kinase activity in
Streptococcus faecalis by phosphoenolpyruvate-dependent
phosphorylation catalyzed by enzyme I and HPr of the
phosphotransferase system.";
J. Bacteriol. 166:829-836(1986).
-!- FUNCTION: Key enzyme in the regulation of glycerol uptake and
metabolism. Catalyzes the phosphorylation of glycerol to yield sn-
glycerol 3-phosphate. {ECO:0000255|HAMAP-Rule:MF_00186,
ECO:0000269|PubMed:9162046}.
-!- CATALYTIC ACTIVITY:
Reaction=ATP + glycerol = ADP + H(+) + sn-glycerol 3-phosphate;
Xref=Rhea:RHEA:21644, ChEBI:CHEBI:15378, ChEBI:CHEBI:17754,
ChEBI:CHEBI:30616, ChEBI:CHEBI:57597, ChEBI:CHEBI:456216;
EC=2.7.1.30; Evidence={ECO:0000255|HAMAP-Rule:MF_00186};
-!- ACTIVITY REGULATION: Activated by phosphorylation and inhibited by
fructose 1,6-bisphosphate (FBP). {ECO:0000255|HAMAP-Rule:MF_00186,
ECO:0000269|PubMed:9162046}.
-!- PATHWAY: Polyol metabolism; glycerol degradation via glycerol
kinase pathway; sn-glycerol 3-phosphate from glycerol: step 1/1.
{ECO:0000255|HAMAP-Rule:MF_00186}.
-!- SUBUNIT: Homotetramer and homodimer (in equilibrium).
{ECO:0000255|HAMAP-Rule:MF_00186}.
-!- PTM: The phosphoenolpyruvate-dependent sugar phosphotransferase
system (PTS), including enzyme I, and histidine-containing protein
(HPr) are required for the phosphorylation of His-231, which leads
to the activation of the enzyme. {ECO:0000269|PubMed:3011747}.
-!- SIMILARITY: Belongs to the FGGY kinase family. {ECO:0000255|HAMAP-
Rule:MF_00186}.
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EMBL; U94356; AAB69986.1; -; Genomic_DNA.
EMBL; AE016830; AAO81680.1; -; Genomic_DNA.
RefSeq; NP_815610.1; NC_004668.1.
RefSeq; WP_002357138.1; NZ_KE136528.1.
ProteinModelPortal; O34154; -.
SMR; O34154; -.
STRING; 226185.EF1929; -.
iPTMnet; O34154; -.
EnsemblBacteria; AAO81680; AAO81680; EF_1929.
GeneID; 1200808; -.
KEGG; efa:EF1929; -.
PATRIC; fig|226185.45.peg.1590; -.
eggNOG; ENOG4108HMR; Bacteria.
eggNOG; COG0554; LUCA.
KO; K00864; -.
OMA; WQDTRTQ; -.
BioCyc; EFAE226185:G1G0C-1894-MONOMER; -.
SABIO-RK; O34154; -.
UniPathway; UPA00618; UER00672.
Proteomes; UP000001415; Chromosome.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
GO; GO:0004370; F:glycerol kinase activity; ISS:UniProtKB.
GO; GO:0019563; P:glycerol catabolic process; IEA:UniProtKB-UniPathway.
GO; GO:0006071; P:glycerol metabolic process; ISS:UniProtKB.
GO; GO:0006072; P:glycerol-3-phosphate metabolic process; IEA:UniProtKB-UniRule.
HAMAP; MF_00186; Glycerol_kin; 1.
InterPro; IPR000577; Carb_kinase_FGGY.
InterPro; IPR018485; Carb_kinase_FGGY_C.
InterPro; IPR018483; Carb_kinase_FGGY_CS.
InterPro; IPR018484; Carb_kinase_FGGY_N.
InterPro; IPR005999; Glycerol_kin.
Pfam; PF02782; FGGY_C; 1.
Pfam; PF00370; FGGY_N; 1.
PIRSF; PIRSF000538; GlpK; 1.
TIGRFAMs; TIGR01311; glycerol_kin; 1.
PROSITE; PS00933; FGGY_KINASES_1; 1.
PROSITE; PS00445; FGGY_KINASES_2; 1.
1: Evidence at protein level;
ATP-binding; Complete proteome; Direct protein sequencing;
Glycerol metabolism; Kinase; Nucleotide-binding; Phosphoprotein;
Reference proteome; Transferase.
INIT_MET 1 1 Removed. {ECO:0000269|PubMed:9162046}.
CHAIN 2 501 Glycerol kinase.
/FTId=PRO_0000059455.
NP_BIND 14 16 ATP. {ECO:0000255|HAMAP-Rule:MF_00186}.
NP_BIND 411 415 ATP. {ECO:0000255|HAMAP-Rule:MF_00186}.
REGION 84 85 Substrate binding. {ECO:0000255|HAMAP-
Rule:MF_00186}.
REGION 245 246 Substrate binding. {ECO:0000255|HAMAP-
Rule:MF_00186}.
BINDING 14 14 Substrate. {ECO:0000255|HAMAP-
Rule:MF_00186}.
BINDING 18 18 ATP. {ECO:0000255|HAMAP-Rule:MF_00186}.
BINDING 136 136 Substrate. {ECO:0000255|HAMAP-
Rule:MF_00186}.
BINDING 267 267 ATP. {ECO:0000255|HAMAP-Rule:MF_00186}.
BINDING 310 310 ATP; via carbonyl oxygen.
{ECO:0000255|HAMAP-Rule:MF_00186}.
BINDING 314 314 ATP; via amide nitrogen.
{ECO:0000255|HAMAP-Rule:MF_00186}.
BINDING 329 329 ATP. {ECO:0000255|HAMAP-Rule:MF_00186}.
MOD_RES 231 231 Phosphohistidine; by HPr.
{ECO:0000255|HAMAP-Rule:MF_00186,
ECO:0000269|PubMed:3011747}.
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


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