GLPK_ECOLI
ID GLPK_ECOLI Reviewed; 502 AA.
AC P0A6F3; P08859; Q2M8M2; Q59381;
DT 29-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 138.
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=b3926, JW3897;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 2-24, FUNCTION, AND
RP INDUCTION.
RX PubMed=2826434; DOI=10.1016/s0021-9258(19)57368-9;
RA Pettigrew D.W., Ma D.-P., Conrad C.A., Johnson J.R.;
RT "Escherichia coli glycerol kinase. Cloning and sequencing of the glpK gene
RT and the primary structure of the enzyme.";
RL J. Biol. Chem. 263:135-139(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1372899; DOI=10.1016/s0021-9258(18)42670-1;
RA Weissenborn D.L., Wittekindt N., Larson T.J.;
RT "Structure and regulation of the glpFK operon encoding glycerol diffusion
RT facilitator and glycerol kinase of Escherichia coli K-12.";
RL J. Biol. Chem. 267:6122-6131(1992).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=8346018; DOI=10.1093/nar/21.15.3391;
RA Plunkett G. III, Burland V., Daniels D.L., Blattner F.R.;
RT "Analysis of the Escherichia coli genome. III. DNA sequence of the region
RT from 87.2 to 89.2 minutes.";
RL Nucleic Acids Res. 21:3391-3398(1993).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-31.
RX PubMed=2544860;
RA Muramatsu S., Mizuno T.;
RT "Nucleotide sequence of the region encompassing the glpKF operon and its
RT upstream region containing a bent DNA sequence of Escherichia coli.";
RL Nucleic Acids Res. 17:4378-4378(1989).
RN [7]
RP PROTEIN SEQUENCE OF 2-14.
RC STRAIN=K12;
RX PubMed=8899705; DOI=10.1111/j.1365-2958.1996.tb02652.x;
RA Gonzalez-Gil G., Bringmann P., Kahmann R.;
RT "FIS is a regulator of metabolism in Escherichia coli.";
RL Mol. Microbiol. 22:21-29(1996).
RN [8]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND MUTANT GLPK22.
RX PubMed=8631672; DOI=10.1128/jb.178.10.2846-2852.1996;
RA Pettigrew D.W., Liu W.Z., Holmes C., Meadow N.D., Roseman S.;
RT "A single amino acid change in Escherichia coli glycerol kinase abolishes
RT glucose control of glycerol utilization in vivo.";
RL J. Bacteriol. 178:2846-2852(1996).
RN [9]
RP ACTIVITY REGULATION.
RX PubMed=5328677; DOI=10.1126/science.153.3737.755;
RA Zwaig N., Lin E.C.;
RT "Feedback inhibition of glycerol kinase, a catabolic enzyme in Escherichia
RT coli.";
RL Science 153:755-757(1966).
RN [10]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND SUBSTRATE
RP SPECIFICITY.
RX PubMed=5335908; DOI=10.1016/s0021-9258(18)96228-9;
RA Hayashi S.I., Lin E.C.;
RT "Purification and properties of glycerol kinase from Escherichia coli.";
RL J. Biol. Chem. 242:1030-1035(1967).
RN [11]
RP SUBUNIT.
RX PubMed=4934840; DOI=10.1016/s0021-9258(18)62117-9;
RA Thorner J.W., Paulus H.;
RT "Composition and subunit structure of glycerol kinase from Escherichia
RT coli.";
RL J. Biol. Chem. 246:3885-3894(1971).
RN [12]
RP FUNCTION, ACTIVITY REGULATION, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=4575199; DOI=10.1016/s0021-9258(19)43821-0;
RA Thorner J.W., Paulus H.;
RT "Catalytic and allosteric properties of glycerol kinase from Escherichia
RT coli.";
RL J. Biol. Chem. 248:3922-3932(1973).
RN [13]
RP SUBUNIT.
RX PubMed=215194; DOI=10.1021/bi00617a010;
RA de Riel J.K., Paulus H.;
RT "Subunit dissociation in the allosteric regulation of glycerol kinase from
RT Escherichia coli. 1. Kinetic evidence.";
RL Biochemistry 17:5134-5140(1978).
RN [14]
RP SUBUNIT, AND ACTIVITY REGULATION.
RX PubMed=215195; DOI=10.1021/bi00617a011;
RA de Riel J.K., Paulus H.;
RT "Subunit dissociation in the allosteric regulation of glycerol kinase from
RT Escherichia coli. 2. Physical evidence.";
RL Biochemistry 17:5141-5146(1978).
RN [15]
RP ACTIVITY REGULATION.
RX PubMed=31903; DOI=10.1021/bi00617a012;
RA de Riel J.K., Paulus H.;
RT "Subunit dissociation in the allosteric regulation of glycerol kinase from
RT Escherichia coli. 3. Role in desensitization.";
RL Biochemistry 17:5146-5150(1978).
RN [16]
RP ACTIVITY REGULATION, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=2985549; DOI=10.1128/jb.162.2.810-816.1985;
RA Novotny M.J., Frederickson W.L., Waygood E.B., Saier M.H. Jr.;
RT "Allosteric regulation of glycerol kinase by enzyme IIIglc of the
RT phosphotransferase system in Escherichia coli and Salmonella typhimurium.";
RL J. Bacteriol. 162:810-816(1985).
RN [17]
RP IDENTIFICATION BY 2D-GEL.
RX PubMed=9298644; DOI=10.1002/elps.1150180805;
RA VanBogelen R.A., Abshire K.Z., Moldover B., Olson E.R., Neidhardt F.C.;
RT "Escherichia coli proteome analysis using the gene-protein database.";
RL Electrophoresis 18:1243-1251(1997).
RN [18]
RP MALONYLATION AT LYS-233.
RC STRAIN=K12;
RX PubMed=21908771; DOI=10.1074/mcp.m111.012658;
RA Peng C., Lu Z., Xie Z., Cheng Z., Chen Y., Tan M., Luo H., Zhang Y., He W.,
RA Yang K., Zwaans B.M., Tishkoff D., Ho L., Lombard D., He T.C., Dai J.,
RA Verdin E., Ye Y., Zhao Y.;
RT "The first identification of lysine malonylation substrates and its
RT regulatory enzyme.";
RL Mol. Cell. Proteomics 10:M111.012658.01-M111.012658.12(2011).
RN [19]
RP X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) IN COMPLEX WITH EIIA-GLC AND ADP,
RP ACTIVITY REGULATION, AND SUBUNIT.
RX PubMed=8430315; DOI=10.1126/science.8430315;
RA Hurley J.H., Faber H.R., Worthylake D., Meadow N.D., Roseman S.,
RA Pettigrew D.W., Remington S.J.;
RT "Structure of the regulatory complex of Escherichia coli IIIGlc with
RT glycerol kinase.";
RL Science 259:673-677(1993).
RN [20]
RP X-RAY CRYSTALLOGRAPHY (2.65 ANGSTROMS) IN COMPLEX WITH EIIA-GLC; SUBSTRATES
RP AND ZINC ION, AND SUBUNIT.
RX PubMed=8170944; DOI=10.1073/pnas.91.9.3544;
RA Feese M., Pettigrew D.W., Meadow N.D., Roseman S., Remington S.J.;
RT "Cation-promoted association of a regulatory and target protein is
RT controlled by protein phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 91:3544-3548(1994).
RN [21] {ECO:0007744|PDB:1BO5, ECO:0007744|PDB:1BOT}
RP X-RAY CRYSTALLOGRAPHY (3.2 ANGSTROMS) OF APOENZYME AND COMPLEX WITH
RP FRUCTOSE-1-6-BISPHOSPHATE, MUTAGENESIS OF ARG-237, ACTIVITY REGULATION, AND
RP SUBUNIT.
RX PubMed=9843423; DOI=10.1021/bi981616s;
RA Ormoe M., Bystrom C.E., Remington S.J.;
RT "Crystal structure of a complex of Escherichia coli glycerol kinase and an
RT allosteric effector fructose 1,6-bisphosphate.";
RL Biochemistry 37:16565-16572(1998).
RN [22]
RP X-RAY CRYSTALLOGRAPHY (2.37 ANGSTROMS) OF MUTANT THR-66 IN COMPLEX WITH
RP SUBSTRATE AND OF MUTANT ASP-475 IN COMPLEX WITH EIIA-GLC, MUTAGENESIS OF
RP ALA-66; ILE-475 AND ARG-480, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL
RP PROPERTIES, AND SUBUNIT.
RX PubMed=9817843; DOI=10.1016/s0969-2126(98)00140-3;
RA Feese M.D., Faber H.R., Bystrom C.E., Pettigrew D.W., Remington S.J.;
RT "Glycerol kinase from Escherichia coli and an Ala65-->Thr mutant: the
RT crystal structures reveal conformational changes with implications for
RT allosteric regulation.";
RL Structure 6:1407-1418(1998).
RN [23]
RP X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF MUTANT TRP-59 IN COMPLEX WITH ATP
RP ANALOGS, MUTAGENESIS OF SER-59, AND SUBUNIT.
RX PubMed=10090737; DOI=10.1021/bi982460z;
RA Bystrom C.E., Pettigrew D.W., Branchaud B.P., O'Brien P., Remington S.J.;
RT "Crystal structures of Escherichia coli glycerol kinase variant S58-->W in
RT complex with nonhydrolyzable ATP analogues reveal a putative active
RT conformation of the enzyme as a result of domain motion.";
RL Biochemistry 38:3508-3518(1999).
RN [24]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF MUTANT ASP-231 IN COMPLEX WITH
RP SUBSTRATE, MUTAGENESIS OF GLY-231, AND SUBUNIT.
RX PubMed=17441732; DOI=10.1021/bi700096p;
RA Anderson M.J., DeLabarre B., Raghunathan A., Palsson B.O., Brunger A.T.,
RA Quake S.R.;
RT "Crystal structure of a hyperactive Escherichia coli glycerol kinase mutant
RT Gly230 --> Asp obtained using microfluidic crystallization devices.";
RL Biochemistry 46:5722-5731(2007).
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. It also catalyzes the phosphorylation of
CC dihydroxyacetone, L-glyceraldehyde and D-glyceraldehyde. It uses only
CC ATP. {ECO:0000255|HAMAP-Rule:MF_00186, ECO:0000269|PubMed:2826434,
CC ECO:0000269|PubMed:4575199, ECO:0000269|PubMed:5335908}.
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 ECO:0000269|PubMed:5335908};
CC -!- ACTIVITY REGULATION: Activity of this regulatory enzyme is affected by
CC several metabolites. The non-competitive allosteric inhibition by
CC fructose 1,6-bisphosphate (FBP) causes alterations in the quaternary
CC structure of the enzyme. FBP inhibition requires that the enzyme exists
CC only in a tetrameric state. Salt such as KCl reduces the affinity of
CC the tetrameric form of the enzyme for FBP. Unphosphorylated
CC phosphocarrier protein EIIA-Glc (III-Glc), an integral component of the
CC bacterial phosphotransferase (PTS) system, also inhibits non-
CC competitively and allosterically the activity. Unlike FBP, both the
CC dimer and the tetramer appear to be fully sensitive to enzyme EIIA-Glc
CC inhibition. Zn(+2) greatly enhances the inhibitory potency of EIIA-Glc.
CC Both allosteric regulatory agents are strongly pH dependent, with
CC maximal inhibition occurring at pH 6.5. {ECO:0000269|PubMed:215195,
CC ECO:0000269|PubMed:2985549, ECO:0000269|PubMed:31903,
CC ECO:0000269|PubMed:4575199, ECO:0000269|PubMed:5328677,
CC ECO:0000269|PubMed:8430315, ECO:0000269|PubMed:9817843,
CC ECO:0000269|PubMed:9843423}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=1.3 uM for glycerol {ECO:0000269|PubMed:2985549,
CC ECO:0000269|PubMed:4575199, ECO:0000269|PubMed:5335908,
CC ECO:0000269|PubMed:9817843};
CC KM=400 uM for D-glyceraldehyde {ECO:0000269|PubMed:2985549,
CC ECO:0000269|PubMed:4575199, ECO:0000269|PubMed:5335908,
CC ECO:0000269|PubMed:9817843};
CC KM=500 uM for dihydroxyacetone {ECO:0000269|PubMed:2985549,
CC ECO:0000269|PubMed:4575199, ECO:0000269|PubMed:5335908,
CC ECO:0000269|PubMed:9817843};
CC KM=3 mM for L-glyceraldehyde {ECO:0000269|PubMed:2985549,
CC ECO:0000269|PubMed:4575199, ECO:0000269|PubMed:5335908,
CC ECO:0000269|PubMed:9817843};
CC KM=4 mM for ATP {ECO:0000269|PubMed:2985549,
CC ECO:0000269|PubMed:4575199, ECO:0000269|PubMed:5335908,
CC ECO:0000269|PubMed:9817843};
CC pH dependence:
CC Optimum pH is 9.8. {ECO:0000269|PubMed:2985549,
CC ECO:0000269|PubMed:4575199, ECO:0000269|PubMed:5335908,
CC ECO:0000269|PubMed:9817843};
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 (crr). Binds 1 zinc ion per glycerol kinase EIIA-Glc dimer.
CC The zinc ion is important for dimerization. {ECO:0000255|HAMAP-
CC Rule:MF_00186, ECO:0000269|PubMed:10090737,
CC ECO:0000269|PubMed:17441732, ECO:0000269|PubMed:215194,
CC ECO:0000269|PubMed:215195, ECO:0000269|PubMed:4934840,
CC ECO:0000269|PubMed:8170944, ECO:0000269|PubMed:8430315,
CC ECO:0000269|PubMed:9817843, ECO:0000269|PubMed:9843423}.
CC -!- INTERACTION:
CC P0A6F3; P0A6F3: glpK; NbExp=2; IntAct=EBI-548038, EBI-548038;
CC -!- INDUCTION: By L-alpha-glycerol 3-phosphate.
CC {ECO:0000269|PubMed:2826434}.
CC -!- SIMILARITY: Belongs to the FGGY kinase family. {ECO:0000255|HAMAP-
CC Rule:MF_00186}.
CC -!- WEB RESOURCE: Name=Worthington enzyme manual;
CC URL="https://www.worthington-biochem.com/GKEC/";
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DR EMBL; M18393; AAA23913.1; -; Genomic_DNA.
DR EMBL; M55990; AAA23887.1; -; Genomic_DNA.
DR EMBL; L19201; AAB03058.1; -; Genomic_DNA.
DR EMBL; U00096; AAC76908.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE77384.1; -; Genomic_DNA.
DR EMBL; X15054; CAA33154.1; -; Genomic_DNA.
DR EMBL; U41468; AAB60196.1; -; Genomic_DNA.
DR PIR; A27339; KIECGL.
DR RefSeq; NP_418361.1; NC_000913.3.
DR RefSeq; WP_000136788.1; NZ_SSZK01000014.1.
DR PDB; 1BO5; X-ray; 3.20 A; O/Z=2-502.
DR PDB; 1BOT; X-ray; 3.05 A; O/Z=2-502.
DR PDB; 1BU6; X-ray; 2.37 A; O/X/Y/Z=2-502.
DR PDB; 1BWF; X-ray; 3.00 A; O/Y=2-502.
DR PDB; 1GLA; X-ray; 2.60 A; G=2-502.
DR PDB; 1GLB; X-ray; 2.60 A; G=2-502.
DR PDB; 1GLC; X-ray; 2.65 A; G=2-502.
DR PDB; 1GLD; X-ray; 2.93 A; G=2-502.
DR PDB; 1GLE; X-ray; 2.94 A; G=2-502.
DR PDB; 1GLF; X-ray; 2.62 A; O/X/Y/Z=2-502.
DR PDB; 1GLJ; X-ray; 3.00 A; O/Y=2-502.
DR PDB; 1GLL; X-ray; 3.00 A; O/Y=2-502.
DR PDB; 3EZW; X-ray; 2.00 A; A/B/C/D/E/F/G/H=2-501.
DR PDBsum; 1BO5; -.
DR PDBsum; 1BOT; -.
DR PDBsum; 1BU6; -.
DR PDBsum; 1BWF; -.
DR PDBsum; 1GLA; -.
DR PDBsum; 1GLB; -.
DR PDBsum; 1GLC; -.
DR PDBsum; 1GLD; -.
DR PDBsum; 1GLE; -.
DR PDBsum; 1GLF; -.
DR PDBsum; 1GLJ; -.
DR PDBsum; 1GLL; -.
DR PDBsum; 3EZW; -.
DR AlphaFoldDB; P0A6F3; -.
DR SMR; P0A6F3; -.
DR BioGRID; 4263162; 380.
DR DIP; DIP-36011N; -.
DR IntAct; P0A6F3; 15.
DR STRING; 511145.b3926; -.
DR ChEMBL; CHEMBL4523174; -.
DR DrugBank; DB04551; beta-D-fructofuranose 1,6-bisphosphate.
DR DrugBank; DB02937; Gamma-Arsono-Beta, Gamma-Methyleneadenosine-5'-Diphosphate.
DR SwissLipids; SLP:000001805; -.
DR SWISS-2DPAGE; P0A6F3; -.
DR jPOST; P0A6F3; -.
DR PaxDb; P0A6F3; -.
DR PRIDE; P0A6F3; -.
DR EnsemblBacteria; AAC76908; AAC76908; b3926.
DR EnsemblBacteria; BAE77384; BAE77384; BAE77384.
DR GeneID; 66672166; -.
DR GeneID; 948423; -.
DR KEGG; ecj:JW3897; -.
DR KEGG; eco:b3926; -.
DR PATRIC; fig|1411691.4.peg.2779; -.
DR EchoBASE; EB0393; -.
DR eggNOG; COG0554; Bacteria.
DR HOGENOM; CLU_009281_2_3_6; -.
DR InParanoid; P0A6F3; -.
DR OMA; FMLMNIG; -.
DR PhylomeDB; P0A6F3; -.
DR BioCyc; EcoCyc:GLYCEROL-KIN-MON; -.
DR BioCyc; MetaCyc:GLYCEROL-KIN-MON; -.
DR BRENDA; 2.7.1.30; 2026.
DR UniPathway; UPA00618; UER00672.
DR EvolutionaryTrace; P0A6F3; -.
DR PRO; PR:P0A6F3; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005829; C:cytosol; IDA:EcoCyc.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004370; F:glycerol kinase activity; IDA:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0046872; F:metal ion binding; IDA:EcoCyc.
DR GO; GO:0016773; F:phosphotransferase activity, alcohol group as acceptor; IBA:GO_Central.
DR GO; GO:0008270; F:zinc ion binding; IDA:UniProtKB.
DR GO; GO:0006974; P:cellular response to DNA damage stimulus; IEP:EcoliWiki.
DR GO; GO:0019563; P:glycerol catabolic process; IMP:EcoCyc.
DR GO; GO:0006071; P:glycerol metabolic process; IDA:UniProtKB.
DR GO; GO:0006072; P:glycerol-3-phosphate metabolic process; IEA:UniProtKB-UniRule.
DR GO; GO:0016310; P:phosphorylation; IDA:EcoCyc.
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 3D-structure; Allosteric enzyme; ATP-binding; Direct protein sequencing;
KW Glycerol metabolism; Kinase; Metal-binding; Nucleotide-binding;
KW Reference proteome; Transferase; Zinc.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:2826434,
FT ECO:0000269|PubMed:8899705"
FT CHAIN 2..502
FT /note="Glycerol kinase"
FT /id="PRO_0000059451"
FT BINDING 14..16
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT BINDING 14
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00186,
FT ECO:0000269|PubMed:17441732"
FT BINDING 18
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT BINDING 84..85
FT /ligand="substrate"
FT BINDING 136
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00186,
FT ECO:0000269|PubMed:17441732"
FT BINDING 235
FT /ligand="beta-D-fructose 1,6-bisphosphate"
FT /ligand_id="ChEBI:CHEBI:32966"
FT /ligand_note="allosteric inhibitor"
FT /evidence="ECO:0000269|PubMed:9843423,
FT ECO:0007744|PDB:1BO5"
FT BINDING 237
FT /ligand="beta-D-fructose 1,6-bisphosphate"
FT /ligand_id="ChEBI:CHEBI:32966"
FT /ligand_note="allosteric inhibitor"
FT /evidence="ECO:0000269|PubMed:9843423,
FT ECO:0007744|PDB:1BO5"
FT BINDING 246..247
FT /ligand="substrate"
FT BINDING 268
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT BINDING 311
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT BINDING 315
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT BINDING 330
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT BINDING 412..416
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT BINDING 479
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="ligand shared with EIIA-Glc"
FT MOD_RES 233
FT /note="N6-malonyllysine"
FT /evidence="ECO:0000269|PubMed:21908771"
FT MUTAGEN 59
FT /note="S->W: Abolishes inhibition of GK by FBP via
FT disruption of the dimer-tetramer assembly reaction.
FT Inhibition by EIIA-Glc is unchanged compared to wild type.
FT The activity of this mutant is significantly higher than
FT wild-type, and the Michaelis constants are increased
FT slightly compared to wild-type."
FT /evidence="ECO:0000269|PubMed:10090737"
FT MUTAGEN 66
FT /note="A->T: Although it completely abolishes FBP
FT regulation and disrupts dimer-tetramer equilibrium, the
FT crystal structure is essentially identical to the symmetric
FT tetramer found in the FBP-bound form of the enzyme."
FT /evidence="ECO:0000269|PubMed:9817843"
FT MUTAGEN 231
FT /note="G->D: Displays an increased enzymatic activity and a
FT decreased allosteric regulation by FBP compared to wild-
FT type. It displays a dimer form and is resistant to tetramer
FT formation in the presence of FBP, whereas wild-type dimers
FT are converted into inactive tetramers in the presence of
FT FBP."
FT /evidence="ECO:0000269|PubMed:17441732"
FT MUTAGEN 237
FT /note="R->A: Drastically reduces inhibition of GK by FBP
FT and lowers, but did not eliminate, the ability of FBP to
FT promote tetramer association."
FT /evidence="ECO:0000269|PubMed:9843423"
FT MUTAGEN 305
FT /note="G->S: In glpK22; abolishes glucose control of
FT glycerol utilization."
FT /evidence="ECO:0000269|PubMed:8631672"
FT MUTAGEN 475
FT /note="I->D: It decreases Vmax to about 10% of the wild-
FT type value and the affinity for substrate is increased
FT about two- to fourfold. This mutation decreases the
FT catalytic activity in a manner that is analogous to that
FT obtained upon EIIA-Glc binding. It increases the affinity
FT for FBP about fivefold."
FT /evidence="ECO:0000269|PubMed:9817843"
FT MUTAGEN 480
FT /note="R->D: It decreases Vmax to about 10% of the wild-
FT type value and the affinity for substrate is increased
FT about two- to fourfold. This mutation decreases the
FT catalytic activity in a manner that is analogous to that
FT obtained upon EIIA-Glc binding. Regulation by FBP is not
FT affected by this substitution. No inhibition by EIIA-Glc is
FT observed, which is consistent with a decrease in affinity
FT for EIIA-Glc of about 250-fold."
FT /evidence="ECO:0000269|PubMed:9817843"
FT STRAND 6..12
FT /evidence="ECO:0007829|PDB:3EZW"
FT STRAND 14..22
FT /evidence="ECO:0007829|PDB:3EZW"
FT STRAND 24..26
FT /evidence="ECO:0007829|PDB:1GLA"
FT STRAND 28..35
FT /evidence="ECO:0007829|PDB:3EZW"
FT STRAND 41..44
FT /evidence="ECO:0007829|PDB:1GLA"
FT HELIX 50..68
FT /evidence="ECO:0007829|PDB:3EZW"
FT HELIX 72..74
FT /evidence="ECO:0007829|PDB:3EZW"
FT STRAND 75..82
FT /evidence="ECO:0007829|PDB:3EZW"
FT STRAND 87..91
FT /evidence="ECO:0007829|PDB:3EZW"
FT TURN 92..94
FT /evidence="ECO:0007829|PDB:3EZW"
FT STRAND 97..99
FT /evidence="ECO:0007829|PDB:3EZW"
FT HELIX 110..118
FT /evidence="ECO:0007829|PDB:3EZW"
FT TURN 119..121
FT /evidence="ECO:0007829|PDB:1BU6"
FT HELIX 122..129
FT /evidence="ECO:0007829|PDB:3EZW"
FT HELIX 138..148
FT /evidence="ECO:0007829|PDB:3EZW"
FT STRAND 149..151
FT /evidence="ECO:0007829|PDB:1GLA"
FT HELIX 152..157
FT /evidence="ECO:0007829|PDB:3EZW"
FT TURN 158..160
FT /evidence="ECO:0007829|PDB:1GLL"
FT STRAND 161..164
FT /evidence="ECO:0007829|PDB:3EZW"
FT HELIX 166..174
FT /evidence="ECO:0007829|PDB:3EZW"
FT TURN 175..177
FT /evidence="ECO:0007829|PDB:3EZW"
FT STRAND 181..183
FT /evidence="ECO:0007829|PDB:3EZW"
FT HELIX 184..187
FT /evidence="ECO:0007829|PDB:3EZW"
FT STRAND 190..194
FT /evidence="ECO:0007829|PDB:3EZW"
FT TURN 195..198
FT /evidence="ECO:0007829|PDB:3EZW"
FT HELIX 202..208
FT /evidence="ECO:0007829|PDB:3EZW"
FT HELIX 212..214
FT /evidence="ECO:0007829|PDB:3EZW"
FT STRAND 217..219
FT /evidence="ECO:0007829|PDB:3EZW"
FT STRAND 221..228
FT /evidence="ECO:0007829|PDB:3EZW"
FT STRAND 231..235
FT /evidence="ECO:0007829|PDB:1BU6"
FT STRAND 238..245
FT /evidence="ECO:0007829|PDB:3EZW"
FT HELIX 246..253
FT /evidence="ECO:0007829|PDB:3EZW"
FT STRAND 262..275
FT /evidence="ECO:0007829|PDB:3EZW"
FT STRAND 284..286
FT /evidence="ECO:0007829|PDB:3EZW"
FT STRAND 288..293
FT /evidence="ECO:0007829|PDB:3EZW"
FT TURN 295..297
FT /evidence="ECO:0007829|PDB:1GLC"
FT STRAND 299..308
FT /evidence="ECO:0007829|PDB:3EZW"
FT HELIX 311..319
FT /evidence="ECO:0007829|PDB:3EZW"
FT STRAND 326..328
FT /evidence="ECO:0007829|PDB:3EZW"
FT HELIX 330..334
FT /evidence="ECO:0007829|PDB:3EZW"
FT STRAND 337..339
FT /evidence="ECO:0007829|PDB:3EZW"
FT STRAND 344..346
FT /evidence="ECO:0007829|PDB:3EZW"
FT HELIX 348..350
FT /evidence="ECO:0007829|PDB:1GLL"
FT TURN 354..356
FT /evidence="ECO:0007829|PDB:3EZW"
FT STRAND 363..368
FT /evidence="ECO:0007829|PDB:3EZW"
FT HELIX 374..400
FT /evidence="ECO:0007829|PDB:3EZW"
FT STRAND 405..411
FT /evidence="ECO:0007829|PDB:3EZW"
FT HELIX 412..415
FT /evidence="ECO:0007829|PDB:3EZW"
FT HELIX 417..427
FT /evidence="ECO:0007829|PDB:3EZW"
FT STRAND 429..435
FT /evidence="ECO:0007829|PDB:3EZW"
FT HELIX 439..451
FT /evidence="ECO:0007829|PDB:3EZW"
FT STRAND 454..456
FT /evidence="ECO:0007829|PDB:3EZW"
FT HELIX 458..460
FT /evidence="ECO:0007829|PDB:3EZW"
FT TURN 461..463
FT /evidence="ECO:0007829|PDB:1GLF"
FT STRAND 467..471
FT /evidence="ECO:0007829|PDB:3EZW"
FT HELIX 477..494
FT /evidence="ECO:0007829|PDB:3EZW"
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
