ID GLK_ECOL6 Reviewed; 321 AA. AC Q8FFD4; DT 15-MAR-2005, integrated into UniProtKB/Swiss-Prot. DT 01-MAR-2003, sequence version 1. DT 27-MAR-2024, entry version 99. 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=c2927; OS Escherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC). OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=199310; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CFT073 / ATCC 700928 / UPEC; RX PubMed=12471157; DOI=10.1073/pnas.252529799; RA Welch R.A., Burland V., Plunkett G. III, Redford P., Roesch P., Rasko D., RA Buckles E.L., Liou S.-R., Boutin A., Hackett J., Stroud D., Mayhew G.F., RA Rose D.J., Zhou S., Schwartz D.C., Perna N.T., Mobley H.L.T., RA Donnenberg M.S., Blattner F.R.; RT "Extensive mosaic structure revealed by the complete genome sequence of RT uropathogenic Escherichia coli."; RL Proc. Natl. Acad. Sci. U.S.A. 99:17020-17024(2002). CC -!- FUNCTION: Not highly important in E.coli as glucose is transported into CC the cell by the PTS system already as glucose 6-phosphate. 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; AE014075; AAN81377.1; -; Genomic_DNA. DR RefSeq; WP_000170355.1; NZ_CP051263.1. DR AlphaFoldDB; Q8FFD4; -. DR SMR; Q8FFD4; -. DR STRING; 199310.c2927; -. DR KEGG; ecc:c2927; -. DR eggNOG; COG0837; Bacteria. DR HOGENOM; CLU_042582_1_0_6; -. DR BioCyc; ECOL199310:C2927-MONOMER; -. DR Proteomes; UP000001410; 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 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 Reference proteome; Transferase. FT CHAIN 1..321 FT /note="Glucokinase" FT /id="PRO_0000215126" 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; 34709 MW; 42ACBF56627A5C98 CRC64; MTKYALVGDV GGTNARLALC DIASGEISQA KTYSGLDYPS LEAVIRVYLE EHKVEVKDGC IAIACPITGD WVAMTNHTWA FSIAEMKKNL GFSHLEIIND FTAVSMAIPM LKKEHLIQFG GAEPVEGKPI AVYGAGTGLG VAHLVHVDKR WVSLPGEGGH VDFAPNSEEE GIILEILRAE IGHVSAERVL SGPGLVNLYR AIVKADNRLP ENLKPKDITE RALADSCTDC RRALSLFCVI MGRFGGNLAL NLGTFGGVFI AGGIVPRFLE FFKASGFRAA FEDKGRFKEY VHDIPVYLIV HDNPGLLGSG AHLRQTLGHI L //