ID GLPK_ACIAD Reviewed; 495 AA. AC Q6FDN3; DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot. DT 19-JUL-2004, sequence version 1. DT 04-NOV-2026, entry version 135. 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=ACIAD0930; OS Acinetobacter baylyi (strain ATCC 33305 / BD413 / ADP1). OC Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria; OC Moraxellales; Moraxellaceae; Acinetobacter. OX NCBI_TaxID=62977; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33305 / BD413 / ADP1; RX PubMed=15514110; DOI=10.1093/nar/gkh910; RA Barbe V., Vallenet D., Fonknechten N., Kreimeyer A., Oztas S., Labarre L., RA Cruveiller S., Robert C., Duprat S., Wincker P., Ornston L.N., RA Weissenbach J., Marliere P., Cohen G.N., Medigue C.; RT "Unique features revealed by the genome sequence of Acinetobacter sp. ADP1, RT a versatile and naturally transformation competent bacterium."; RL Nucleic Acids Res. 32:5766-5779(2004). 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; CR543861; CAG67825.1; -; Genomic_DNA. DR RefSeq; WP_004921999.1; NC_005966.1. DR SMR; Q6FDN3; -. DR STRING; 202950.GCA_001485005_02674; -. DR GeneID; 45233386; -. DR KEGG; aci:ACIAD0930; -. DR eggNOG; COG0554; Bacteria. DR HOGENOM; CLU_009281_2_3_6; -. DR OMA; AACNWTM; -. DR OrthoDB; 9805576at2; -. DR BioCyc; ASP62977:ACIAD_RS04290-MONOMER; -. DR UniPathway; UPA00618; UER00672. DR CDD; cd07786; FGGY_EcGK_like; 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 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 NCBIfam; NF000756; glpK; 1. DR NCBIfam; TIGR01311; glycerol_kin; 1. DR PROSITE; PS00933; FGGY_KINASES_1; 1. DR PROSITE; PS00445; FGGY_KINASES_2; 1. 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 Proteomes; UP000000430; Chromosome. DR AlphaFoldDB; Q6FDN3; -. 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_1000118541" FT BINDING 11 FT /ligand="ADP" FT /ligand_id="ChEBI:CHEBI:456216" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00186" FT BINDING 11 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00186" FT BINDING 11 FT /ligand="sn-glycerol 3-phosphate" FT /ligand_id="ChEBI:CHEBI:57597" 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 13 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00186" FT BINDING 15 FT /ligand="ADP" FT /ligand_id="ChEBI:CHEBI:456216" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00186" FT BINDING 81 FT /ligand="glycerol" FT /ligand_id="ChEBI:CHEBI:17754" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00186" FT BINDING 81 FT /ligand="sn-glycerol 3-phosphate" FT /ligand_id="ChEBI:CHEBI:57597" 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 133 FT /ligand="glycerol" FT /ligand_id="ChEBI:CHEBI:17754" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00186" FT BINDING 133 FT /ligand="sn-glycerol 3-phosphate" FT /ligand_id="ChEBI:CHEBI:57597" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00186" FT BINDING 242 FT /ligand="glycerol" FT /ligand_id="ChEBI:CHEBI:17754" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00186" FT BINDING 242 FT /ligand="sn-glycerol 3-phosphate" FT /ligand_id="ChEBI:CHEBI:57597" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00186" FT BINDING 243 FT /ligand="glycerol" FT /ligand_id="ChEBI:CHEBI:17754" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00186" FT BINDING 264 FT /ligand="ADP" FT /ligand_id="ChEBI:CHEBI:456216" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00186" FT BINDING 264 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00186" FT BINDING 307 FT /ligand="ADP" FT /ligand_id="ChEBI:CHEBI:456216" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00186" FT BINDING 307 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00186" FT BINDING 311 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00186" FT BINDING 408 FT /ligand="ADP" FT /ligand_id="ChEBI:CHEBI:456216" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00186" FT BINDING 408 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00186" FT BINDING 412 FT /ligand="ADP" FT /ligand_id="ChEBI:CHEBI:456216" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00186" SQ SEQUENCE 495 AA; 54271 MW; C429160A95CDC587 CRC64; MSYLLALDQG TTSSRAIIFD EKGQIHATAQ RETRIKTPNS GWVEQDANEI WSSQIAVIQQ ALASAHILAK DIKALGLTNQ RETTVVWDKR TGKALAPAII WQDRRAAQWC NTLIENGMLV QVQQKTGLRI DPYFSAGKLV WLLENIAGFR ILAEQGHAAF GTIDSWLVWN LTQGAEHIIE ASNASRTMLM NLSTQMWDED LLNKFNIPAA ILPKIISSDA YVADTAQGLL GSTIPITGIL GDQQAALFGQ SCFEVGSAKN TYGTGCFMLF NTGDQLQFSQ NQLLTTLAWQ CQNQTRYALE GSVFMAGAIV QWLRDGLGLI QHSAQVEQLA SQVQSTEGVV LVPAFTGLGA PHWDSEARAL LCGMSRGTTK AHIARAALEA IAFQVSDVLC AMQSDLSRPL KELRVDGGAS QNDMLMQFQA DILNVPVLRP KMLESTAWGA AAMAGLKAGV FTNLDEIAAS WQLDRTFEPK MKNDERESRL CEWSQALKRA KSNLI //