ID   GLK_CUPMC               Reviewed;         336 AA.
AC   Q1LB18;
DT   12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT   30-MAY-2006, 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=Rmet_5799;
OS   Cupriavidus metallidurans (strain ATCC 43123 / DSM 2839 / NBRC 102507 /
OS   CH34) (Ralstonia metallidurans).
OG   Plasmid megaplasmid CH34.
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Cupriavidus.
OX   NCBI_TaxID=266264;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43123 / DSM 2839 / NBRC 102507 / CH34;
RX   PubMed=20463976; DOI=10.1371/journal.pone.0010433;
RA   Janssen P.J., Van Houdt R., Moors H., Monsieurs P., Morin N., Michaux A.,
RA   Benotmane M.A., Leys N., Vallaeys T., Lapidus A., Monchy S., Medigue C.,
RA   Taghavi S., McCorkle S., Dunn J., van der Lelie D., Mergeay M.;
RT   "The complete genome sequence of Cupriavidus metallidurans strain CH34, a
RT   master survivalist in harsh and anthropogenic environments.";
RL   PLoS ONE 5:E10433-E10433(2010).
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; CP000353; ABF12658.1; -; Genomic_DNA.
DR   RefSeq; WP_011520194.1; NC_007974.2.
DR   AlphaFoldDB; Q1LB18; -.
DR   SMR; Q1LB18; -.
DR   STRING; 266264.Rmet_5799; -.
DR   EnsemblBacteria; ABF12658; ABF12658; Rmet_5799.
DR   KEGG; rme:Rmet_5799; -.
DR   eggNOG; COG0837; Bacteria.
DR   HOGENOM; CLU_042582_1_0_4; -.
DR   OMA; NNHWRLS; -.
DR   OrthoDB; 992687at2; -.
DR   Proteomes; UP000002429; Plasmid megaplasmid CH34.
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; Plasmid;
KW   Reference proteome; Transferase.
FT   CHAIN           1..336
FT                   /note="Glucokinase"
FT                   /id="PRO_0000268781"
FT   BINDING         13..18
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00524"
SQ   SEQUENCE   336 AA;  35185 MW;  47721EFB63A9591E CRC64;
     MTDRAMSYPR ILADVGGTNV RFAMETAPMR IGEITAYKVA EHASLEAAMR LYMLTRSGAA
     RPRHAAIGLA NPVTGDQVKL TNHNWAFSVE AMRRALDLDT LVAINDFTSL ALALPYLPDA
     SLVQVRDGTA VATAPRALIG PGTGLGVSGL IPAPGGAVAL AGEGGHIEIM PVTDDEWIAW
     RAAHDQFGRV SAERLLSGMG LSHIHAALSA EMGTPLEVPL APAQVTDGAM RAGDPVCRRA
     FDAFCGMLGS VAADVALVLG ARGGVYLGGG IVPRFVDALR ASTFAERFVA KGRMGSFLAD
     VPVYVITAEY PALPGLARAL ADRLEADARR AETSQS