ID A0A6I2F1T3_9MICO Unreviewed; 504 AA. AC A0A6I2F1T3; DT 12-AUG-2020, integrated into UniProtKB/TrEMBL. DT 12-AUG-2020, sequence version 1. DT 02-OCT-2024, entry version 19. DE RecName: Full=Glycerol kinase {ECO:0000256|HAMAP-Rule:MF_00186}; DE EC=2.7.1.30 {ECO:0000256|HAMAP-Rule:MF_00186}; DE AltName: Full=ATP:glycerol 3-phosphotransferase {ECO:0000256|HAMAP-Rule:MF_00186}; DE AltName: Full=Glycerokinase {ECO:0000256|HAMAP-Rule:MF_00186}; DE Short=GK {ECO:0000256|HAMAP-Rule:MF_00186}; GN Name=glpK {ECO:0000256|HAMAP-Rule:MF_00186, GN ECO:0000313|EMBL:MRG58384.1}; GN ORFNames=GE115_00625 {ECO:0000313|EMBL:MRG58384.1}; OS Agromyces agglutinans. OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae; OC Agromyces. OX NCBI_TaxID=2662258 {ECO:0000313|EMBL:MRG58384.1, ECO:0000313|Proteomes:UP000431080}; RN [1] {ECO:0000313|EMBL:MRG58384.1, ECO:0000313|Proteomes:UP000431080} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CFH 90414 {ECO:0000313|EMBL:MRG58384.1, RC ECO:0000313|Proteomes:UP000431080}; RA Nie G., Ming H., Yi B.; RL Submitted (OCT-2019) 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:0000256|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:0000256|HAMAP-Rule:MF_00186}; CC -!- ACTIVITY REGULATION: Inhibited by fructose 1,6-bisphosphate (FBP). CC {ECO:0000256|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:0000256|HAMAP-Rule:MF_00186}. CC -!- SIMILARITY: Belongs to the FGGY kinase family. CC {ECO:0000256|ARBA:ARBA00009156, ECO:0000256|HAMAP-Rule:MF_00186, CC ECO:0000256|RuleBase:RU003733}. CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ CC whole genome shotgun (WGS) entry which is preliminary data. CC {ECO:0000313|EMBL:MRG58384.1}. 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; WJIF01000001; MRG58384.1; -; Genomic_DNA. DR AlphaFoldDB; A0A6I2F1T3; -. DR UniPathway; UPA00618; UER00672. DR Proteomes; UP000431080; Unassembled WGS sequence. DR GO; GO:0005829; C:cytosol; IEA:TreeGrafter. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule. DR GO; GO:0004370; F:glycerol kinase activity; IEA:UniProtKB-UniRule. DR GO; GO:0019563; P:glycerol catabolic process; IEA:UniProtKB-UniPathway. DR GO; GO:0006072; P:glycerol-3-phosphate metabolic process; IEA:UniProtKB-UniRule. DR CDD; cd07789; FGGY_CsGK_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 {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP- KW Rule:MF_00186}; KW Glycerol metabolism {ECO:0000256|ARBA:ARBA00022798, ECO:0000256|HAMAP- KW Rule:MF_00186}; KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|HAMAP-Rule:MF_00186}; KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP- KW Rule:MF_00186}; Reference proteome {ECO:0000313|Proteomes:UP000431080}; KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP- KW Rule:MF_00186}. FT DOMAIN 4..253 FT /note="Carbohydrate kinase FGGY N-terminal" FT /evidence="ECO:0000259|Pfam:PF00370" FT DOMAIN 264..452 FT /note="Carbohydrate kinase FGGY C-terminal" FT /evidence="ECO:0000259|Pfam:PF02782" FT BINDING 12 FT /ligand="ADP" FT /ligand_id="ChEBI:CHEBI:456216" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00186" FT BINDING 12 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00186" FT BINDING 12 FT /ligand="sn-glycerol 3-phosphate" FT /ligand_id="ChEBI:CHEBI:57597" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00186" FT BINDING 13 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00186" FT BINDING 14 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00186" FT BINDING 16 FT /ligand="ADP" FT /ligand_id="ChEBI:CHEBI:456216" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00186" FT BINDING 82 FT /ligand="glycerol" FT /ligand_id="ChEBI:CHEBI:17754" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00186" FT BINDING 82 FT /ligand="sn-glycerol 3-phosphate" FT /ligand_id="ChEBI:CHEBI:57597" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00186" FT BINDING 83 FT /ligand="glycerol" FT /ligand_id="ChEBI:CHEBI:17754" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00186" FT BINDING 83 FT /ligand="sn-glycerol 3-phosphate" FT /ligand_id="ChEBI:CHEBI:57597" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00186" FT BINDING 134 FT /ligand="glycerol" FT /ligand_id="ChEBI:CHEBI:17754" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00186" FT BINDING 134 FT /ligand="sn-glycerol 3-phosphate" FT /ligand_id="ChEBI:CHEBI:57597" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00186" FT BINDING 246 FT /ligand="glycerol" FT /ligand_id="ChEBI:CHEBI:17754" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00186" FT BINDING 246 FT /ligand="sn-glycerol 3-phosphate" FT /ligand_id="ChEBI:CHEBI:57597" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00186" FT BINDING 247 FT /ligand="glycerol" FT /ligand_id="ChEBI:CHEBI:17754" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00186" FT BINDING 268 FT /ligand="ADP" FT /ligand_id="ChEBI:CHEBI:456216" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00186" FT BINDING 268 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00186" FT BINDING 312 FT /ligand="ADP" FT /ligand_id="ChEBI:CHEBI:456216" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00186" FT BINDING 312 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00186" FT BINDING 316 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00186" FT BINDING 413 FT /ligand="ADP" FT /ligand_id="ChEBI:CHEBI:456216" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00186" FT BINDING 413 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00186" FT BINDING 417 FT /ligand="ADP" FT /ligand_id="ChEBI:CHEBI:456216" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00186" SQ SEQUENCE 504 AA; 55174 MW; A5B99CA503573546 CRC64; MADYILAIDQ GTTSTRAIIF DKRGSIVATG QLEHEQIFPK AGWVEHDPME IWRNTREVIG QALGKADLTR HDIAAVGITN QRETAVVWDR NTGEPVYNAI VWQDTRTQPI VDRLAADGGV ERFKQDVGLP LATYFSGTKI VWILENVEGA RERAEAGDLL FGTTDCWVLW NLTGGADGGV HATDVTNASR TLFMDLETLS WRDDILEAFG VPRSMLPEIR SSSEVYGTVE PSSLLREVPV AGILGDQQAA TFGQAAFDQG ESKNTYGTGN FLIFNTDTEI VHSKNGLLTT LGYKLGDQPA HYALEGSIAV TGSLIQWLRD NLGIISSAPE VEELAKTVDD NGGAYFVPAF SGLFAPYWRS DARGALVGLT RYVNKGHIAR AALEATAFQT REVLDAVNAD SGVDLTELKV DGGMIANNTL MQFQADILGV PVVRPVVAET TALGAAYAAG LAVGFWSDLD ELRANWQEDS RWEPKMDADE RERQLRLWKK AVSKTFDWVD EDVS //