ID GLPK_BURCC Reviewed; 500 AA. AC B1JY43; DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot. DT 29-APR-2008, sequence version 1. DT 22-JUL-2015, entry version 51. 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=Bcenmc03_2707; OS Burkholderia cenocepacia (strain MC0-3). OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Burkholderiaceae; Burkholderia; Burkholderia cepacia complex. OX NCBI_TaxID=406425; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC0-3; RA Copeland A., Lucas S., Lapidus A., Barry K., Bruce D., Goodwin L., RA Glavina del Rio T., Dalin E., Tice H., Pitluck S., Chain P., RA Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M., RA Hauser L., Kyrpides N., Mikhailova N., Tiedje J., Richardson P.; RT "Complete sequence of chromosome 1 of Burkholderia cenocepacia MC0- RT 3."; RL Submitted (FEB-2008) to the EMBL/GenBank/DDBJ databases. 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 -!- CATALYTIC ACTIVITY: ATP + glycerol = ADP + sn-glycerol 3- CC phosphate. {ECO:0000255|HAMAP-Rule:MF_00186}. CC -!- ENZYME REGULATION: Inhibited by fructose 1,6-bisphosphate (FBP). CC {ECO:0000255|HAMAP-Rule:MF_00186}. CC -!- PATHWAY: Polyol metabolism; glycerol degradation via glycerol CC kinase pathway; sn-glycerol 3-phosphate from glycerol: step 1/1. CC {ECO:0000255|HAMAP-Rule:MF_00186}. CC -!- SIMILARITY: Belongs to the FGGY kinase family. {ECO:0000255|HAMAP- CC Rule:MF_00186}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; CP000958; ACA91867.1; -; Genomic_DNA. DR RefSeq; WP_011546147.1; NC_010508.1. DR ProteinModelPortal; B1JY43; -. DR SMR; B1JY43; 2-497. DR EnsemblBacteria; ACA91867; ACA91867; Bcenmc03_2707. DR KEGG; bcm:Bcenmc03_2707; -. DR PATRIC; 19092650; VBIBurCen61509_2807. DR eggNOG; COG0554; -. DR HOGENOM; HOG000222134; -. DR KO; K00864; -. DR OMA; GWVEHEP; -. DR OrthoDB; EOG6RZB46; -. DR BioCyc; BCEN406425:GHD9-2780-MONOMER; -. DR UniPathway; UPA00618; UER00672. DR Proteomes; UP000002169; Chromosome 1. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP. 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-HAMAP. DR HAMAP; MF_00186; Glycerol_kin; 1. 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 TIGRFAMs; TIGR01311; glycerol_kin; 1. DR PROSITE; PS00933; FGGY_KINASES_1; 1. DR PROSITE; PS00445; FGGY_KINASES_2; 1. PE 3: Inferred from homology; KW ATP-binding; Complete proteome; Glycerol metabolism; Kinase; KW Nucleotide-binding; Transferase. FT CHAIN 1 500 Glycerol kinase. FT /FTId=PRO_1000098720. FT NP_BIND 13 15 ATP. {ECO:0000255|HAMAP-Rule:MF_00186}. FT NP_BIND 410 414 ATP. {ECO:0000255|HAMAP-Rule:MF_00186}. FT REGION 83 84 Substrate binding. {ECO:0000255|HAMAP- FT Rule:MF_00186}. FT REGION 244 245 Substrate binding. {ECO:0000255|HAMAP- FT Rule:MF_00186}. FT BINDING 13 13 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_00186}. FT BINDING 17 17 ATP. {ECO:0000255|HAMAP-Rule:MF_00186}. FT BINDING 135 135 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_00186}. FT BINDING 266 266 ATP. {ECO:0000255|HAMAP-Rule:MF_00186}. FT BINDING 309 309 ATP; via carbonyl oxygen. FT {ECO:0000255|HAMAP-Rule:MF_00186}. FT BINDING 313 313 ATP; via amide nitrogen. FT {ECO:0000255|HAMAP-Rule:MF_00186}. SQ SEQUENCE 500 AA; 54661 MW; 93324BE747D97438 CRC64; MQDQYILALD QGTTSSRAML FDRQGNIVSI AQKEFEQIYP QPGWVEHDPQ EIWSTQAGVA AEAVTRTGLN GTSIAAIGIT NQRETTIVWD RETGQPVYNA IVWQDRRTAD FCDSLKKQGL EAKVRAKTGL PIDSYFSATK IRWILDNVPG ARDKARQGKL AFGTVDSWLV WNFTKHELHV TDVTNASRTM LFNIHTREWD SELLELLDIP RSMLPEVKAS SEIYGHTKTT VFASKIPLAG IAGDQHAALF GQMCTTSGMV KNTYGTGCFL MMNTGDKPIE SKNNLVTTIA WQIGDDVQYA LEGSIFIAGA VVQWLRDGVG LIKTAAEIEA LAASVPHTDG VYLVPAFAGL GAPHWNARAR GSVFGVTRGT SAAHLARAAL DAIAYQSLDV LAAMEADSGI SIGELRVDGG ASANDLLMQF QADLLGVDAV RPQITETTAL GAAYLAGLAI GYWKNLDEVR DQWQLDRRFA PSMPKEQVEQ RMAGWQRAVR AAKAWADDTQ //