ID GLPK_SHEWM Reviewed; 495 AA. AC B1KKY8; DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot. DT 29-APR-2008, sequence version 1. DT 27-MAR-2024, entry version 89. 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=Swoo_4544; OS Shewanella woodyi (strain ATCC 51908 / MS32). OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales; OC Shewanellaceae; Shewanella. OX NCBI_TaxID=392500; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51908 / MS32; RG US DOE Joint Genome Institute; RA Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E., Tice H., RA Bruce D., Goodwin L., Pitluck S., Sims D., Brettin T., Detter J.C., Han C., RA Kuske C.R., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., RA Lykidis A., Zhao J.-S., Richardson P.; RT "Complete sequence of Shewanella woodyi ATCC 51908."; 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; CP000961; ACA88794.1; -; Genomic_DNA. DR RefSeq; WP_012327120.1; NC_010506.1. DR AlphaFoldDB; B1KKY8; -. DR SMR; B1KKY8; -. DR STRING; 392500.Swoo_4544; -. DR KEGG; swd:Swoo_4544; -. DR eggNOG; COG0554; Bacteria. DR HOGENOM; CLU_009281_2_3_6; -. DR UniPathway; UPA00618; UER00672. DR Proteomes; UP000002168; Chromosome. 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 CDD; cd07786; FGGY_EcGK_like; 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 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..495 FT /note="Glycerol kinase" FT /id="PRO_1000098762" FT BINDING 13 FT /ligand="ADP" FT /ligand_id="ChEBI:CHEBI:456216" 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 13 FT /ligand="sn-glycerol 3-phosphate" FT /ligand_id="ChEBI:CHEBI:57597" 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 15 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00186" FT BINDING 17 FT /ligand="ADP" FT /ligand_id="ChEBI:CHEBI:456216" 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 84 FT /ligand="glycerol" FT /ligand_id="ChEBI:CHEBI:17754" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00186" FT BINDING 84 FT /ligand="sn-glycerol 3-phosphate" FT /ligand_id="ChEBI:CHEBI:57597" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00186" FT BINDING 135 FT /ligand="glycerol" FT /ligand_id="ChEBI:CHEBI:17754" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00186" FT BINDING 135 FT /ligand="sn-glycerol 3-phosphate" FT /ligand_id="ChEBI:CHEBI:57597" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00186" FT BINDING 244 FT /ligand="glycerol" FT /ligand_id="ChEBI:CHEBI:17754" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00186" FT BINDING 244 FT /ligand="sn-glycerol 3-phosphate" FT /ligand_id="ChEBI:CHEBI:57597" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00186" FT BINDING 245 FT /ligand="glycerol" FT /ligand_id="ChEBI:CHEBI:17754" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00186" FT BINDING 266 FT /ligand="ADP" FT /ligand_id="ChEBI:CHEBI:456216" 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="ADP" FT /ligand_id="ChEBI:CHEBI:456216" 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 FT /ligand="ADP" FT /ligand_id="ChEBI:CHEBI:456216" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00186" FT BINDING 410 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00186" FT BINDING 414 FT /ligand="ADP" FT /ligand_id="ChEBI:CHEBI:456216" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00186" SQ SEQUENCE 495 AA; 54095 MW; D44BAFEED2822485 CRC64; MTKKYVVALD QGTTSSRAII FDHDANIVSV SQREFTQIYP QAGWVEHDPM EIWASQSSTL IEVIARSGIH ASEIASIGIT NQRETTVIWD KQTGKPVYNA IVWQCRRSSE ICEELKSQGL EAYIRDTTGL LLDPYFSGTK IKWILDNVSG VRERAERGEL LFGTIDTWLV WKLTEGKVHV TDPTNASRTL LFNIHTQSWD KRILEALTIP ESLLPQVKPS SAVYGKTRIA GEGGEISIAG IAGDQQSALF GQLCTEPGMA KNTYGTGCFL LMNTGEKAVK SNHGLLTTIA IGAKGEVNYA LEGSVFMGGA TIQWLRDELG LIRDAQDTEY FASRVESTNG VYLVPAFVGL GAPYWDPSAR GALVGLTRGS NRNHIIRAAL EAIAYQSRDL LDAMAKDSGV ELKKLKVDGG AVANDFLMQF QADITSVEVQ RPAVTETTAM GAAFLAGLAV GFWDSTSELK HRADIDKSFM PSISEEQKDE LYAGWQKAVS QTING //