ID GLK_ECOUT Reviewed; 321 AA. AC Q1R8X8; DT 12-DEC-2006, integrated into UniProtKB/Swiss-Prot. DT 16-MAY-2006, sequence version 1. DT 16-JUN-2009, entry version 20. DE RecName: Full=Glucokinase; DE EC=2.7.1.2; DE AltName: Full=Glucose kinase; GN Name=glk; OrderedLocusNames=UTI89_C2720; OS Escherichia coli (strain UTI89 / UPEC). OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=364106; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16585510; DOI=10.1073/pnas.0600938103; RA Chen S.L., Hung C.-S., Xu J., Reigstad C.S., Magrini V., Sabo A., RA Blasiar D., Bieri T., Meyer R.R., Ozersky P., Armstrong J.R., RA Fulton R.S., Latreille J.P., Spieth J., Hooton T.M., Mardis E.R., RA Hultgren S.J., Gordon J.I.; RT "Identification of genes subject to positive selection in RT uropathogenic strains of Escherichia coli: a comparative genomics RT approach."; RL Proc. Natl. Acad. Sci. U.S.A. 103:5977-5982(2006). CC -!- FUNCTION: Not highly important in E.coli as glucose is transported CC into the cell by the PTS system already as glucose 6-phosphate. CC -!- CATALYTIC ACTIVITY: ATP + D-glucose = ADP + D-glucose 6-phosphate. CC -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). CC -!- SIMILARITY: Belongs to the bacterial glucokinase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000243; ABE08186.1; -; Genomic_DNA. DR RefSeq; YP_541717.1; -. DR SMR; Q1R8X8; 2-321. DR GeneID; 3989780; -. DR GenomeReviews; CP000243_GR; UTI89_C2720. DR KEGG; eci:UTI89_C2720; -. DR HOGENOM; Q1R8X8; -. DR OMA; Q1R8X8; VDIGGTH. DR BioCyc; ECOL364106:UTI89_C2720-MON; -. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:HAMAP. DR GO; GO:0004340; F:glucokinase activity; IEA:HAMAP. DR GO; GO:0006096; P:glycolysis; IEA:HAMAP. DR HAMAP; MF_00524; -; 1. DR InterPro; IPR003836; Glucokinase. DR Pfam; PF02685; Glucokinase; 1. DR TIGRFAMs; TIGR00749; glk; 1. PE 3: Inferred from homology; KW ATP-binding; Complete proteome; Cytoplasm; Glycolysis; Kinase; KW Nucleotide-binding; Transferase. FT CHAIN 1 321 Glucokinase. FT /FTId=PRO_0000268772. FT NP_BIND 8 13 ATP (Potential). 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 //