ID A0A6A7Y4P2_9HYPH Unreviewed; 495 AA. AC A0A6A7Y4P2; DT 17-JUN-2020, integrated into UniProtKB/TrEMBL. DT 17-JUN-2020, sequence version 1. DT 24-JUL-2024, entry version 18. 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:MQT13178.1}; GN ORFNames=F0357_11100 {ECO:0000313|EMBL:MQT13178.1}; OS Segnochrobactrum spirostomi. OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales; OC Segnochrobactraceae; Segnochrobactrum. OX NCBI_TaxID=2608987 {ECO:0000313|EMBL:MQT13178.1, ECO:0000313|Proteomes:UP000332515}; RN [1] {ECO:0000313|EMBL:MQT13178.1, ECO:0000313|Proteomes:UP000332515} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Sp-1 {ECO:0000313|EMBL:MQT13178.1, RC ECO:0000313|Proteomes:UP000332515}; RA Akter S., Shazib S.U.A., Shin M.K.; RT "Segnochrobactrum spirostomi gen. nov., sp. nov., isolated from the ciliate RT Spirostomum cf. yagiui and description of a novel family, RT Segnochrobactraceae fam. nov. within the order Rhizobiales of the class RT Alphaproteobacteria."; RL Submitted (SEP-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: Lacks conserved residue(s) required for the propagation of CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_00186}. 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:MQT13178.1}. 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; VWNA01000001; MQT13178.1; -; Genomic_DNA. DR AlphaFoldDB; A0A6A7Y4P2; -. DR UniPathway; UPA00618; UER00672. DR Proteomes; UP000332515; 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; 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:SF78; 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:UP000332515}; KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP- KW Rule:MF_00186}. FT DOMAIN 4..249 FT /note="Carbohydrate kinase FGGY N-terminal" FT /evidence="ECO:0000259|Pfam:PF00370" FT DOMAIN 260..448 FT /note="Carbohydrate kinase FGGY C-terminal" FT /evidence="ECO:0000259|Pfam:PF02782" FT BINDING 11 FT /ligand="ADP" FT /ligand_id="ChEBI:CHEBI:456216" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00186" FT BINDING 11 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00186" FT BINDING 11 FT /ligand="sn-glycerol 3-phosphate" FT /ligand_id="ChEBI:CHEBI:57597" 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 13 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00186" FT BINDING 15 FT /ligand="ADP" FT /ligand_id="ChEBI:CHEBI:456216" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00186" FT BINDING 81 FT /ligand="glycerol" FT /ligand_id="ChEBI:CHEBI:17754" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00186" FT BINDING 81 FT /ligand="sn-glycerol 3-phosphate" FT /ligand_id="ChEBI:CHEBI:57597" 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 133 FT /ligand="glycerol" FT /ligand_id="ChEBI:CHEBI:17754" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00186" FT BINDING 133 FT /ligand="sn-glycerol 3-phosphate" FT /ligand_id="ChEBI:CHEBI:57597" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00186" FT BINDING 242 FT /ligand="glycerol" FT /ligand_id="ChEBI:CHEBI:17754" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00186" FT BINDING 242 FT /ligand="sn-glycerol 3-phosphate" FT /ligand_id="ChEBI:CHEBI:57597" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00186" FT BINDING 243 FT /ligand="glycerol" FT /ligand_id="ChEBI:CHEBI:17754" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00186" FT BINDING 264 FT /ligand="ADP" FT /ligand_id="ChEBI:CHEBI:456216" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00186" FT BINDING 264 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00186" FT BINDING 307 FT /ligand="ADP" FT /ligand_id="ChEBI:CHEBI:456216" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00186" FT BINDING 307 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00186" FT BINDING 311 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00186" FT BINDING 410 FT /ligand="ADP" FT /ligand_id="ChEBI:CHEBI:456216" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00186" FT BINDING 410 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00186" SQ SEQUENCE 495 AA; 53598 MW; 442EC35584C87030 CRC64; MTHILAIDQG TTSSRAILFD AAMRLKAVAQ QEFPQHFPAS GWVEHDPADL WSSVAGTARA AIEQAGLTGA DIAAIGITNQ RETVVIWDRA TGEPIHRAIV WQDRRTADLC ARLKADGLEP EISAKTGLLI DPYFSATKIK WLLDHVEGAR ERARRGELAF GTVDCFLIWK LTDGAVHATD ATNAARTMLY DIREGRWDEA LCAAFGVPMA MLPEVRDCAA PYGTTRPDLF GRAIPILGVA GDQQAATVGQ ACFRPGMLKS TYGTGCFALL NTGDDLVASK NRLLGTIAYR LKGRTTYALE GSIFIAGAVV QWLRDGLKII RHAAETHPLA EKADPAQDLV LVPAFTGLGA PYWRPDCRGA VFGLTRNSGP AEFARAALES VGYQTRDLLE AMHADWKDAT AEGVLRVDGG MTASDWTMQF LADILGAPVD RPVVRETTAL GAAYLAGLEA GLYPDPDAFA ATWALERRFL PALDETTRTA KYARWRRAVE ATMAA //