ID GLK_YERPY Reviewed; 323 AA. AC B1JG01; DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot. DT 29-APR-2008, sequence version 1. DT 27-MAR-2024, entry version 75. DE RecName: Full=Glucokinase {ECO:0000255|HAMAP-Rule:MF_00524}; DE EC=2.7.1.2 {ECO:0000255|HAMAP-Rule:MF_00524}; DE AltName: Full=Glucose kinase {ECO:0000255|HAMAP-Rule:MF_00524}; GN Name=glk {ECO:0000255|HAMAP-Rule:MF_00524}; GN OrderedLocusNames=YPK_1444; OS Yersinia pseudotuberculosis serotype O:3 (strain YPIII). OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales; OC Yersiniaceae; Yersinia. OX NCBI_TaxID=502800; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=YPIII; RG US DOE Joint Genome Institute; RA Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E., Tice H., RA Bruce D., Goodwin L., Pitluck S., Munk A.C., Brettin T., Detter J.C., RA Han C., Tapia R., Schmutz J., Larimer F., Land M., Hauser L., RA Challacombe J.F., Green L., Lindler L.E., Nikolich M.P., Richardson P.; RT "Complete sequence of Yersinia pseudotuberculosis YPIII."; RL Submitted (FEB-2008) to the EMBL/GenBank/DDBJ databases. CC -!- CATALYTIC ACTIVITY: CC Reaction=ATP + D-glucose = ADP + D-glucose 6-phosphate + H(+); CC Xref=Rhea:RHEA:17825, ChEBI:CHEBI:4167, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:30616, ChEBI:CHEBI:61548, ChEBI:CHEBI:456216; EC=2.7.1.2; CC Evidence={ECO:0000255|HAMAP-Rule:MF_00524}; CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00524}. CC -!- SIMILARITY: Belongs to the bacterial glucokinase family. CC {ECO:0000255|HAMAP-Rule:MF_00524}. 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; CP000950; ACA67737.1; -; Genomic_DNA. DR RefSeq; WP_002211615.1; NZ_CP009792.1. DR AlphaFoldDB; B1JG01; -. DR SMR; B1JG01; -. DR GeneID; 66844879; -. DR KEGG; ypy:YPK_1444; -. DR PATRIC; fig|502800.11.peg.2081; -. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule. DR GO; GO:0004340; F:glucokinase activity; IEA:UniProtKB-UniRule. DR GO; GO:0005536; F:glucose binding; IEA:InterPro. DR GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-UniRule. DR CDD; cd00012; NBD_sugar-kinase_HSP70_actin; 1. DR Gene3D; 3.30.420.40; -; 1. DR Gene3D; 3.40.367.20; -; 1. DR HAMAP; MF_00524; Glucokinase; 1. DR InterPro; IPR043129; ATPase_NBD. DR InterPro; IPR003836; Glucokinase. DR NCBIfam; TIGR00749; glk; 1. DR PANTHER; PTHR47690; GLUCOKINASE; 1. DR PANTHER; PTHR47690:SF1; GLUCOKINASE; 1. DR Pfam; PF02685; Glucokinase; 1. DR SUPFAM; SSF53067; Actin-like ATPase domain; 1. PE 3: Inferred from homology; KW ATP-binding; Cytoplasm; Glycolysis; Kinase; Nucleotide-binding; KW Transferase. FT CHAIN 1..323 FT /note="Glucokinase" FT /id="PRO_1000127733" FT BINDING 8..13 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00524" SQ SEQUENCE 323 AA; 34664 MW; A2465D600781CE37 CRC64; MTTYALVGDV GGTNARLALC AVATGEILQA KTYSGLEYES LEDVIKQYLS EHQAKVTDAC IAIACPITGD WVAMTNHTWA FSIAAMQQNL GLDHLEVIND FTAVSMAIPV LPAQDVLQFG GTQPQPGKPV AVYGAGTGLG VAHLVNVDRR WISLAGEGGH VDFAPNSEEE DQILAVLRQE LGHVSAERVL SGPGLVNLYR AIVISDARLP EKLAPKDITA RALADSCTDC RRALSLFCVI MGRFGGNLAL NLSTFGGVYI AGGIVPRFME FFKASGFRAA FEDKGRFKDF LQDIPVYMIT HPQPGLLGAG AYLRQKLGYE LSS //