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 14-DEC-2022, entry version 74. 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., Malfatti S., RA Shin M., Vergez L., Schmutz J., Larimer F., Land M., Hauser L., RA Kyrpides N., Mikhailova N., Tiedje J., Richardson P.; RT "Complete sequence of chromosome 1 of Burkholderia cenocepacia MC0-3."; 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: 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: Inhibited by fructose 1,6-bisphosphate (FBP). CC {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 -!- 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 AlphaFoldDB; B1JY43; -. DR SMR; B1JY43; -. DR EnsemblBacteria; ACA91867; ACA91867; Bcenmc03_2707. DR KEGG; bcm:Bcenmc03_2707; -. DR HOGENOM; CLU_009281_2_3_4; -. DR OMA; FMLMNIG; -. DR UniPathway; UPA00618; UER00672. DR Proteomes; UP000002169; Chromosome 1. 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; Actin-like ATPase domain; 2. 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; Glycerol metabolism; Kinase; Nucleotide-binding; Transferase. FT CHAIN 1..500 FT /note="Glycerol kinase" FT /id="PRO_1000098720" FT BINDING 13..15 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00186" FT BINDING 13 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00186" FT BINDING 17 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00186" FT BINDING 83..84 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00186" FT BINDING 135 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00186" FT BINDING 244..245 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00186" 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="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00186" FT BINDING 313 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00186" FT BINDING 410..414 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="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 //