ID GLK_NEIMB Reviewed; 328 AA. AC P64254; Q9JQX3; DT 11-OCT-2004, integrated into UniProtKB/Swiss-Prot. DT 11-OCT-2004, sequence version 1. DT 27-MAR-2024, entry version 91. 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=NMB1390; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Pseudomonadota; Betaproteobacteria; Neisseriales; Neisseriaceae; OC Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., Nelson W.C., RA Gwinn M.L., DeBoy R.T., Peterson J.D., Hickey E.K., Haft D.H., RA Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., Mason T.M., RA Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., Cotton M.D., RA Utterback T.R., Khouri H.M., Qin H., Vamathevan J.J., Gill J., Scarlato V., RA Masignani V., Pizza M., Grandi G., Sun L., Smith H.O., Fraser C.M., RA Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). 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; AE002098; AAF41754.1; -; Genomic_DNA. DR PIR; E81089; E81089. DR RefSeq; NP_274404.1; NC_003112.2. DR RefSeq; WP_002216974.1; NC_003112.2. DR AlphaFoldDB; P64254; -. DR SMR; P64254; -. DR STRING; 122586.NMB1390; -. DR PaxDb; 122586-NMB1390; -. DR GeneID; 61281578; -. DR KEGG; nme:NMB1390; -. DR PATRIC; fig|122586.8.peg.1743; -. DR HOGENOM; CLU_042582_1_0_4; -. DR InParanoid; P64254; -. DR OrthoDB; 257751at2; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0005829; C:cytosol; IBA:GO_Central. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule. DR GO; GO:0004340; F:glucokinase activity; IBA:GO_Central. 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 Reference proteome; Transferase. FT CHAIN 1..328 FT /note="Glucokinase" FT /id="PRO_0000215131" FT BINDING 16..21 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00524" SQ SEQUENCE 328 AA; 34951 MW; A7B4AA6BD6C92F0C CRC64; MSSTPNKQAG YPRLVADIGG TNARFALETA PRVIEKAAVL PCKDYDTVTD AVRAYLNQSG ATAVRHAAFA IANPILGDWV QMTNHHWAFS IETTRQTLGL DTLILLNDFT AQALAVTQTS SKDLMQVGGQ KPVEFAPKAV IGPGTGLGVS GLVHSHAGWV ALAGEGGHTS FPPFDDMEVL IWQYAKNKYG HVSAERFLSG AGLSLVYEAL AAKQKAKPAK LMPSEITEKA LSGASPLCRQ TLDIFCAMLG TVASNLALTL GARGGVYLCG GIIPRVLEYF KTSPFRSRFE NKGRFEAYLA AIPVYVVLSE FPGISGAAAA LDNHLRNV //