ID GLK_SALEP Reviewed; 321 AA. AC B5R3T6; DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot. DT 04-NOV-2008, sequence version 1. DT 27-MAR-2024, entry version 68. 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}; OrderedLocusNames=SEN2389; OS Salmonella enteritidis PT4 (strain P125109). OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales; OC Enterobacteriaceae; Salmonella. OX NCBI_TaxID=550537; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=P125109; RX PubMed=18583645; DOI=10.1101/gr.077404.108; RA Thomson N.R., Clayton D.J., Windhorst D., Vernikos G., Davidson S., RA Churcher C., Quail M.A., Stevens M., Jones M.A., Watson M., Barron A., RA Layton A., Pickard D., Kingsley R.A., Bignell A., Clark L., Harris B., RA Ormond D., Abdellah Z., Brooks K., Cherevach I., Chillingworth T., RA Woodward J., Norberczak H., Lord A., Arrowsmith C., Jagels K., Moule S., RA Mungall K., Saunders M., Whitehead S., Chabalgoity J.A., Maskell D., RA Humphreys T., Roberts M., Barrow P.A., Dougan G., Parkhill J.; RT "Comparative genome analysis of Salmonella enteritidis PT4 and Salmonella RT gallinarum 287/91 provides insights into evolutionary and host adaptation RT pathways."; RL Genome Res. 18:1624-1637(2008). 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; AM933172; CAR33975.1; -; Genomic_DNA. DR RefSeq; WP_000170380.1; NC_011294.1. DR AlphaFoldDB; B5R3T6; -. DR SMR; B5R3T6; -. DR KEGG; set:SEN2389; -. DR HOGENOM; CLU_042582_1_0_6; -. DR Proteomes; UP000000613; Chromosome. 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 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..321 FT /note="Glucokinase" FT /id="PRO_1000127719" FT BINDING 8..13 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00524" SQ SEQUENCE 321 AA; 34595 MW; 0ECD9CC77D8C6C8A CRC64; MTKYALVGDV GGTNARLALC DIASGEISQA KTYSGLDYPS LEAVVRVYLD EHSVSVEDGC IAIACPITGD WVAMTNHTWA FSIAEMKKNL GFSHLEIIND FTAVSMAIPM LKKEHLIQFG GGEPVDGKPI AVYGAGTGLG VAHLVHVDKR WISLPGEGGH VDFAPNSEEE AMILEILRAE IGHVSAERVL SGPGLVNLYR AIVKSDNRLP ENLRPKDITE RALADSCIDC RRALSLFCVI MGRFGGDLAL TMGTFGGVYI AGGIVPRFLE FFKASGFRGG FEDKGRFKDY VHGIPVYLIV HDNPGLLGSG AHLRQTLGHI L //