ID A0A2M9R036_9GAMM Unreviewed; 499 AA. AC A0A2M9R036; DT 25-APR-2018, integrated into UniProtKB/TrEMBL. DT 25-APR-2018, sequence version 1. DT 13-SEP-2023, 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:PJO53693.1}; GN ORFNames=CR156_16690 {ECO:0000313|EMBL:PJO53693.1}; OS Stenotrophomonas lactitubi. OC Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales; OC Xanthomonadaceae; Stenotrophomonas. OX NCBI_TaxID=2045214 {ECO:0000313|EMBL:PJO53693.1, ECO:0000313|Proteomes:UP000231985}; RN [1] {ECO:0000313|EMBL:PJO53693.1, ECO:0000313|Proteomes:UP000231985} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=M15 {ECO:0000313|EMBL:PJO53693.1, RC ECO:0000313|Proteomes:UP000231985}; RA Weber M., Schuenemann W., Fuss J., Kaempfer P., Lipski A.; RT "Stenotrophomonas lactitubi sp. nov., and Stenotrophomonas indicatrix sp. RT nov., isolated from food related matrices."; RL Submitted (NOV-2017) 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:PJO53693.1}. 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; PHQX01000001; PJO53693.1; -; Genomic_DNA. DR AlphaFoldDB; A0A2M9R036; -. DR EnsemblBacteria; PJO53693; PJO53693; CR156_16690. DR UniPathway; UPA00618; UER00672. DR Proteomes; UP000231985; Unassembled WGS sequence. 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 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; IPR018485; Carb_kinase_FGGY_C. DR InterPro; IPR018483; Carb_kinase_FGGY_CS. DR InterPro; IPR018484; Carb_kinase_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}; KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP- KW Rule:MF_00186}. FT DOMAIN 5..252 FT /note="Carbohydrate kinase FGGY N-terminal" FT /evidence="ECO:0000259|Pfam:PF00370" FT DOMAIN 262..450 FT /note="Carbohydrate kinase FGGY C-terminal" FT /evidence="ECO:0000259|Pfam:PF02782" FT BINDING 13..15 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00186" FT BINDING 13 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00186" FT BINDING 17 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00186" FT BINDING 83..84 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00186" FT BINDING 135 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00186" FT BINDING 245..246 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00186" FT BINDING 267 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00186" FT BINDING 310 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00186" FT BINDING 314 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00186" FT BINDING 329 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00186" FT BINDING 411..415 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00186" SQ SEQUENCE 499 AA; 54914 MW; 7BACE7110AAC7995 CRC64; MTPRYVLAID QGTTSSRAIL FDRTGDTVGS AQREFAQLFP QPGWVEHDPR EILTSVYATI TELLSREQID PRHIAALGIT NQRETTVVWD RASGQPIHNA IVWQSRQSQA ICERLKSGGH EALIRERTGL LIDAYFSATK IRWILDHVEG AQQRAERGEL LFGTIDSWLV WNLSGGQAHV TDYSNAARTL LFNIHTLEWD DDLLALLDIP RAMLPQVRDS SSVYAHTRPQ FFFDHPIPIA GIAGDQQAAL FGQACFQPGM VKNTYGTGCF MLMHTGTQAV RSRNGLLTTI AWGLDGKVEY ALEGSIFVAG SVVQWLRDGL RMIDRAADSQ ALAAQVPDSA GVYLVPAFVG LGAPYWRSDV RGAMFGLTRG TRKAHFVRAA LEAMAYQTRD VLDAMQSDAG ISLSELRADG GAIGNDFLAG FQADILGVPL LRPRLTETTA LGAAYLAGLA VGFWESREQI AAQWGLDRRF EPQMAVARRE KLYAGWQQAV AATLAFHVD //