ID A0A9E0SV08_9PROT Unreviewed; 500 AA. AC A0A9E0SV08; DT 03-MAY-2023, integrated into UniProtKB/TrEMBL. DT 03-MAY-2023, sequence version 1. DT 28-JUN-2023, entry version 2. 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:MBS0446618.1}; GN ORFNames=JSR59_11800 {ECO:0000313|EMBL:MBS0446618.1}; OS Pseudomonadota bacterium. OC Bacteria; Pseudomonadota. OX NCBI_TaxID=1977087 {ECO:0000313|EMBL:MBS0446618.1, ECO:0000313|Proteomes:UP000811002}; RN [1] {ECO:0000313|EMBL:MBS0446618.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=SZAS AMP-55 {ECO:0000313|EMBL:MBS0446618.1}; RX PubMed=33819658; RA Wang Y., Zhao R., Liu L., Li B., Zhang T.; RT "Selective enrichment of comammox from activated sludge using RT antibiotics."; RL Water Res. 197:0-0(2021). RN [2] {ECO:0000313|EMBL:MBS0446618.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=SZAS AMP-55 {ECO:0000313|EMBL:MBS0446618.1}; RA Wang Y., Cao Y., Meng X., Hu T., Wang S., Cao K.; RL Submitted (JAN-2021) 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:MBS0446618.1}. 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; JAFEEF010000030; MBS0446618.1; -; Genomic_DNA. DR Proteomes; UP000811002; Unassembled WGS sequence. DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW. 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 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 TIGRFAMs; TIGR01311; glycerol_kin; 1. 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|HAMAP-Rule:MF_00186, ECO:0000256|RuleBase:RU003733}; KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP- KW Rule:MF_00186}; KW Transferase {ECO:0000256|HAMAP-Rule:MF_00186, KW ECO:0000256|RuleBase:RU003733}. FT DOMAIN 6..250 FT /note="Carbohydrate kinase FGGY N-terminal" FT /evidence="ECO:0000259|Pfam:PF00370" FT DOMAIN 259..453 FT /note="Carbohydrate kinase FGGY C-terminal" FT /evidence="ECO:0000259|Pfam:PF02782" FT BINDING 12..14 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00186" FT BINDING 12 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00186" FT BINDING 16 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00186" FT BINDING 82..83 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00186" FT BINDING 134 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00186" FT BINDING 243..244 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00186" FT BINDING 265 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00186" FT BINDING 308 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" 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 413..417 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00186" SQ SEQUENCE 500 AA; 53355 MW; B944EFFC98F059D6 CRC64; MTTHLLALDQ GTSSSRSIVF DARGRIVAMA QREFRQIYPQ PGWVEHDPKE IWQSQLATAQ EALAKAGLKA GDIAAIGITN QRETTLVWNR ATGEPVCNAI VWQDRRAEPT CAALRERGLE PTFRAKTGLV IDAYFSGTKL QWILDHVPGA RAAAERGELA FGTVDTWLMW QLTGGAVHAT DVSNASRTML LDVHRNAWDD ELLGILGVPR ALLPEVLPSS HVYGRTLPGF LGAPIAIGGV AGDQQSALFG QACFEAGLAK NTYGTGCFML MHTGERFQTS ANGLITTSAA QPRARPEFAL EGSVFIGGAV VQWLRDGLQA IKASGEVQRL AETVPDSGGV MFVPAFTGLG APYWKPDARG AIVGLTRGST VAHIARAALE SIAFQSAALL QAMSRDAVAA GGAPVAELRV DGGACVNDLL MQFQADLLGI PVVRPQVIET TALGAAYLAG LACGIYAGLD ELAAQWQVER RFLPTLPRER AGELMQRWEQ AVAQATLQPA //