ID GLPK_CORGB Reviewed; 509 AA. AC A4QHT1; DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot. DT 15-MAY-2007, sequence version 1. DT 04-NOV-2026, entry version 98. 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=cgR_2778; OS Corynebacterium glutamicum (strain R). OC Bacteria; Bacillati; Actinomycetota; Actinomycetes; Mycobacteriales; OC Corynebacteriaceae; Corynebacterium. OX NCBI_TaxID=340322; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=R; RX PubMed=17379713; DOI=10.1099/mic.0.2006/003657-0; RA Yukawa H., Omumasaba C.A., Nonaka H., Kos P., Okai N., Suzuki N., Suda M., RA Tsuge Y., Watanabe J., Ikeda Y., Vertes A.A., Inui M.; RT "Comparative analysis of the Corynebacterium glutamicum group and complete RT genome sequence of strain R."; RL Microbiology 153:1042-1058(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. {ECO:0000255|HAMAP-Rule:MF_00186}. CC -!- CATALYTIC ACTIVITY: CC Reaction=glycerol + ATP = sn-glycerol 3-phosphate + ADP + H(+); 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; AP009044; BAF55797.1; -; Genomic_DNA. DR RefSeq; WP_003857839.1; NC_009342.1. DR AlphaFoldDB; A4QHT1; -. DR SMR; A4QHT1; -. DR GeneID; 1020833; -. DR KEGG; cgt:cgR_2778; -. DR HOGENOM; CLU_009281_2_3_11; -. DR OMA; AACYQVK; -. DR PhylomeDB; A4QHT1; -. DR UniPathway; UPA00618; UER00672. DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-ARBA. 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-UniRule. DR GO; GO:0006071; P:glycerol metabolic process; ISS:UniProtKB. DR GO; GO:0006072; P:glycerol-3-phosphate metabolic process; IEA:InterPro. DR CDD; cd07769; ASKHA_NBD_FGGY_GK; 1. DR FunFam; 3.30.420.40:FF:000007; Glycerol kinase; 1. DR FunFam; 3.30.420.40:FF:000008; Glycerol kinase; 1. DR Gene3D; 3.30.420.40; -; 2. DR HAMAP; MF_00186; Glycerol_kin; 1. DR InterPro; IPR043129; ATPase_NBD. DR InterPro; IPR000577; Carb_kinase_FGGY. DR InterPro; IPR018483; Carb_kinase_FGGY_CS. DR InterPro; IPR018485; FGGY_C. DR InterPro; IPR018484; FGGY_N. DR InterPro; IPR005999; Glycerol_kin. DR NCBIfam; NF000756; glpK; 1. DR NCBIfam; TIGR01311; glycerol_kin; 1. DR PANTHER; PTHR10196:SF69; GLYCEROL KINASE; 1. DR PANTHER; PTHR10196; SUGAR KINASE; 1. 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 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..509 FT /note="Glycerol kinase" FT /id="PRO_1000020724" FT BINDING 17 FT /ligand="ADP" FT /ligand_id="ChEBI:CHEBI:456216" 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 17 FT /ligand="sn-glycerol 3-phosphate" FT /ligand_id="ChEBI:CHEBI:57597" 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 19 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00186" FT BINDING 21 FT /ligand="ADP" FT /ligand_id="ChEBI:CHEBI:456216" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00186" FT BINDING 87 FT /ligand="glycerol" FT /ligand_id="ChEBI:CHEBI:17754" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00186" FT BINDING 87 FT /ligand="sn-glycerol 3-phosphate" FT /ligand_id="ChEBI:CHEBI:57597" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00186" FT BINDING 88 FT /ligand="glycerol" FT /ligand_id="ChEBI:CHEBI:17754" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00186" FT BINDING 88 FT /ligand="sn-glycerol 3-phosphate" FT /ligand_id="ChEBI:CHEBI:57597" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00186" FT BINDING 139 FT /ligand="glycerol" FT /ligand_id="ChEBI:CHEBI:17754" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00186" FT BINDING 139 FT /ligand="sn-glycerol 3-phosphate" FT /ligand_id="ChEBI:CHEBI:57597" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00186" FT BINDING 256 FT /ligand="glycerol" FT /ligand_id="ChEBI:CHEBI:17754" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00186" FT BINDING 256 FT /ligand="sn-glycerol 3-phosphate" FT /ligand_id="ChEBI:CHEBI:57597" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00186" FT BINDING 257 FT /ligand="glycerol" FT /ligand_id="ChEBI:CHEBI:17754" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00186" FT BINDING 278 FT /ligand="ADP" FT /ligand_id="ChEBI:CHEBI:456216" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00186" FT BINDING 278 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00186" FT BINDING 322 FT /ligand="ADP" FT /ligand_id="ChEBI:CHEBI:456216" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00186" FT BINDING 322 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00186" FT BINDING 326 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00186" FT BINDING 423 FT /ligand="ADP" FT /ligand_id="ChEBI:CHEBI:456216" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00186" FT BINDING 423 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00186" FT BINDING 427 FT /ligand="ADP" FT /ligand_id="ChEBI:CHEBI:456216" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00186" SQ SEQUENCE 509 AA; 56145 MW; EC8B65618D84C480 CRC64; MRISKANAYV AAIDQGTTST RCIFIDAQGK VVSSASKEHR QIFPQQGWVE HDPEEIWDNI RSVVSQAMVS IDITPHEVAS LGVTNQRETT VVWDKHTGEP VYNAIVWQDT RTSDICLEIA GEEGQEKWLD RTGLLINSYP SGPKIKWILD NVEGARERAE KGDLLFGTMD TWVLWNLTGG VRGDDGDDAI HVTDVTNASR TLLMDLRTQQ WDPELCEALD IPMSMLPEIR PSVGEFRSVR HRGTLADVPI TGVLGDQQAA LFGQGGFHEG AAKNTYGTGL FLLMNTGTSL KISEHGLLST IAYQREGSAP VYALEGSVSM GGSLVQWLRD NLQLIPNAPA IENLAREVED NGGVHVVPAF TGLFAPRWRP DARGVITGLT RFANRKHIAR AVLEANAFQT REVVDAMAKD AGKALESLRV DGAMVENDLL MQMQADFLGI DVQRLEDVET TAVGVAFAAG LGSGFFKTTD EIEKLIAVKK VWNPDMSEEE RERRYAEWNR AVEHSYDQA //