ID GLPK_BEII9 Reviewed; 507 AA. AC B2IE09; DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot. DT 10-JUN-2008, sequence version 1. DT 10-JUN-2026, entry version 84. 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=Bind_0380; OS Beijerinckia indica subsp. indica (strain ATCC 9039 / DSM 1715 / NCIMB OS 8712). OC Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria; OC Hyphomicrobiales; Beijerinckiaceae; Beijerinckia. OX NCBI_TaxID=395963; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 9039 / DSM 1715 / NCIMB 8712; RX PubMed=20601475; DOI=10.1128/jb.00656-10; RA Tamas I., Dedysh S.N., Liesack W., Stott M.B., Alam M., Murrell J.C., RA Dunfield P.F.; RT "Complete genome sequence of Beijerinckia indica subsp. indica."; RL J. Bacteriol. 192:4532-4533(2010). 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; CP001016; ACB94033.1; -; Genomic_DNA. DR RefSeq; WP_012383391.1; NC_010581.1. DR AlphaFoldDB; B2IE09; -. DR SMR; B2IE09; -. DR STRING; 395963.Bind_0380; -. DR KEGG; bid:Bind_0380; -. DR eggNOG; COG0554; Bacteria. DR HOGENOM; CLU_009281_2_3_5; -. DR OrthoDB; 9805576at2; -. DR UniPathway; UPA00618; UER00672. DR Proteomes; UP000001695; Chromosome. 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; TIGR01311; glycerol_kin; 1. DR NCBIfam; NF000756; PRK00047.1; 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; KW Reference proteome; Transferase. FT CHAIN 1..507 FT /note="Glycerol kinase" FT /id="PRO_1000098716" FT BINDING 12 FT /ligand="ADP" FT /ligand_id="ChEBI:CHEBI:456216" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00186" FT BINDING 12 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00186" FT BINDING 12 FT /ligand="sn-glycerol 3-phosphate" FT /ligand_id="ChEBI:CHEBI:57597" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00186" FT BINDING 13 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00186" FT BINDING 14 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00186" FT BINDING 16 FT /ligand="ADP" FT /ligand_id="ChEBI:CHEBI:456216" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00186" FT BINDING 82 FT /ligand="glycerol" FT /ligand_id="ChEBI:CHEBI:17754" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00186" FT BINDING 82 FT /ligand="sn-glycerol 3-phosphate" FT /ligand_id="ChEBI:CHEBI:57597" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00186" FT BINDING 83 FT /ligand="glycerol" FT /ligand_id="ChEBI:CHEBI:17754" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00186" FT BINDING 83 FT /ligand="sn-glycerol 3-phosphate" FT /ligand_id="ChEBI:CHEBI:57597" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00186" FT BINDING 134 FT /ligand="glycerol" FT /ligand_id="ChEBI:CHEBI:17754" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00186" FT BINDING 134 FT /ligand="sn-glycerol 3-phosphate" FT /ligand_id="ChEBI:CHEBI:57597" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00186" FT BINDING 250 FT /ligand="glycerol" FT /ligand_id="ChEBI:CHEBI:17754" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00186" FT BINDING 250 FT /ligand="sn-glycerol 3-phosphate" FT /ligand_id="ChEBI:CHEBI:57597" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00186" FT BINDING 251 FT /ligand="glycerol" FT /ligand_id="ChEBI:CHEBI:17754" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00186" FT BINDING 272 FT /ligand="ADP" FT /ligand_id="ChEBI:CHEBI:456216" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00186" FT BINDING 272 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00186" FT BINDING 316 FT /ligand="ADP" FT /ligand_id="ChEBI:CHEBI:456216" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00186" FT BINDING 316 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00186" FT BINDING 320 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00186" FT BINDING 417 FT /ligand="ADP" FT /ligand_id="ChEBI:CHEBI:456216" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00186" FT BINDING 417 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00186" FT BINDING 421 FT /ligand="ADP" FT /ligand_id="ChEBI:CHEBI:456216" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00186" SQ SEQUENCE 507 AA; 55758 MW; 7E256793CAEE4535 CRC64; MTKYVAVIDQ GTTSTRCMVF NKQGEIVAQH QLEHEQICPQ AGWVEHDPLE IWERTKDVIH GSVAKAGLVA ADIAAIGITN QRETTMIWNR KTGQPYGNAI VWQDTRTDIV CNQMSAEGGQ NRFQAKTGLP LATYFSGPKI RWMLDHYPGL RQDAEKGEAL FGNMDSWLIW KLTGGPGPAA VHVTDVTNAS RTMLMNLKTL DWDEELLSAF AIPRAMLPSI RPSSDPEFYG FTRQDGPFGG EIPICGDLGD QQAATVGQVC FDAGEAKNTY GTGCFMLMNT GTEMVHSNHG LLTTVCYQFG HEKPHYALEG SVAIAGALVQ WLRDRMRVIN TAADIENLAK LVPDNGGMYF VPAFSGLFAP YWRSEARGLI IGMTRFINRG HFARASLEAA AYQTREVVDA MQADSNVSLK VLKVDGGMTA NDLLMQIQAD VLGVPVVRPK VAESTALGAA YAAGLAIGYW KNSDDLCQNW GVDKSWKPSG DDTLRTKNYA MWKKAVTRTF DWLDESA //