ID   GLK_NEIG1               Reviewed;         328 AA.
AC   Q5F8Q0;
DT   12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT   15-MAR-2005, sequence version 1.
DT   03-AUG-2022, entry version 83.
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=NGO0717;
OS   Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC   Neisseria.
OX   NCBI_TaxID=242231;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700825 / FA 1090;
RA   Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F.,
RA   Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C.,
RA   Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S.,
RA   Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.;
RT   "The complete genome sequence of Neisseria gonorrhoeae.";
RL   Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases.
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; AE004969; AAW89437.1; -; Genomic_DNA.
DR   RefSeq; WP_010951113.1; NC_002946.2.
DR   RefSeq; YP_207849.1; NC_002946.2.
DR   AlphaFoldDB; Q5F8Q0; -.
DR   SMR; Q5F8Q0; -.
DR   STRING; 242231.NGO_0717; -.
DR   EnsemblBacteria; AAW89437; AAW89437; NGO_0717.
DR   KEGG; ngo:NGO_0717; -.
DR   PATRIC; fig|242231.10.peg.853; -.
DR   HOGENOM; CLU_042582_1_0_4; -.
DR   OMA; NNHWRLS; -.
DR   Proteomes; UP000000535; 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   Reference proteome; Transferase.
FT   CHAIN           1..328
FT                   /note="Glucokinase"
FT                   /id="PRO_0000268778"
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;  35112 MW;  765E9E4DD01AE499 CRC64;
     MSSTPNKHAD YPRLVADIGG TNARFALETA PCVIEKVAVL PCKEYDTVTD AVRAYLNQSG
     ATGVRHAAFA IANPILGDWV QMTNHHWAFS IETTRQALGL DTLILLNDFT AQALAVTQTS
     SKDLMQVGGQ KPVEFAPKAV IGPGTGLGVS GLVHSPAGWV ALAGEGGHTS FPPFDDMEVL
     IWQYAKNKYR HVSAERFLSG AGLSLIYETL AVKQKAEPAK LMPSEITEKA LNCESPLCRQ
     ALDIFCAMLG TVASNLALTL GARGGVYLCG GIIPRMLDYF KTSPFRSRFE NKGRFEAYLA
     AIPVYVVLSE FPGIAGAAAA LGNHLKNV