ID   GLK_NEIMF               Reviewed;         328 AA.
AC   A1KUL0;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   06-FEB-2007, sequence version 1.
DT   03-AUG-2022, entry version 74.
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=NMC1329;
OS   Neisseria meningitidis serogroup C / serotype 2a (strain ATCC 700532 / DSM
OS   15464 / FAM18).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC   Neisseria.
OX   NCBI_TaxID=272831;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700532 / DSM 15464 / FAM18;
RX   PubMed=17305430; DOI=10.1371/journal.pgen.0030023;
RA   Bentley S.D., Vernikos G.S., Snyder L.A.S., Churcher C., Arrowsmith C.,
RA   Chillingworth T., Cronin A., Davis P.H., Holroyd N.E., Jagels K.,
RA   Maddison M., Moule S., Rabbinowitsch E., Sharp S., Unwin L., Whitehead S.,
RA   Quail M.A., Achtman M., Barrell B.G., Saunders N.J., Parkhill J.;
RT   "Meningococcal genetic variation mechanisms viewed through comparative
RT   analysis of serogroup C strain FAM18.";
RL   PLoS Genet. 3:230-240(2007).
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}.
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DR   EMBL; AM421808; CAM10555.1; -; Genomic_DNA.
DR   RefSeq; WP_002216974.1; NC_008767.1.
DR   AlphaFoldDB; A1KUL0; -.
DR   SMR; A1KUL0; -.
DR   PRIDE; A1KUL0; -.
DR   EnsemblBacteria; CAM10555; CAM10555; NMC1329.
DR   GeneID; 61281578; -.
DR   KEGG; nmc:NMC1329; -.
DR   HOGENOM; CLU_042582_1_0_4; -.
DR   OMA; NNHWRLS; -.
DR   OrthoDB; 992687at2; -.
DR   Proteomes; UP000002286; 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   HAMAP; MF_00524; Glucokinase; 1.
DR   InterPro; IPR043129; ATPase_NBD.
DR   InterPro; IPR003836; Glucokinase.
DR   Pfam; PF02685; Glucokinase; 1.
DR   SUPFAM; SSF53067; SSF53067; 1.
DR   TIGRFAMs; TIGR00749; glk; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Cytoplasm; Glycolysis; Kinase; Nucleotide-binding;
KW   Transferase.
FT   CHAIN           1..328
FT                   /note="Glucokinase"
FT                   /id="PRO_1000050972"
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