ID   GLK_CUPPJ               Reviewed;         343 AA.
AC   Q46QB2;
DT   12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT   13-SEP-2005, sequence version 1.
DT   03-AUG-2022, entry version 87.
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=Reut_B5327;
OS   Cupriavidus pinatubonensis (strain JMP 134 / LMG 1197) (Cupriavidus necator
OS   (strain JMP 134)).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Cupriavidus.
OX   NCBI_TaxID=264198;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JMP134 / LMG 1197;
RX   PubMed=20339589; DOI=10.1371/journal.pone.0009729;
RA   Lykidis A., Perez-Pantoja D., Ledger T., Mavromatis K., Anderson I.J.,
RA   Ivanova N.N., Hooper S.D., Lapidus A., Lucas S., Gonzalez B.,
RA   Kyrpides N.C.;
RT   "The complete multipartite genome sequence of Cupriavidus necator JMP134, a
RT   versatile pollutant degrader.";
RL   PLoS ONE 5:E9729-E9729(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; CP000091; AAZ64672.1; -; Genomic_DNA.
DR   RefSeq; WP_011301436.1; NC_007348.1.
DR   AlphaFoldDB; Q46QB2; -.
DR   SMR; Q46QB2; -.
DR   STRING; 264198.Reut_B5327; -.
DR   EnsemblBacteria; AAZ64672; AAZ64672; Reut_B5327.
DR   KEGG; reu:Reut_B5327; -.
DR   eggNOG; COG0837; Bacteria.
DR   HOGENOM; CLU_042582_1_0_4; -.
DR   OMA; NNHWRLS; -.
DR   OrthoDB; 992687at2; -.
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..343
FT                   /note="Glucokinase"
FT                   /id="PRO_0000268780"
FT   BINDING         21..26
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00524"
SQ   SEQUENCE   343 AA;  35393 MW;  DDC0B2E1ACE82FA7 CRC64;
     MSNAMAASAV PDDTAYPRLL ADVGGTNVRF ALETAPMQIG AVTALKVADH PSLEAAMRHY
     RDALSASGAK LPRHAAIGLA NPVTGDHVRL TNHDWAFSIE ATRQALGLQT LVAINDFTSL
     ALGLPYLGAN DLVQIRSGQA VATAPRALIG PGTGLGVSGL VPAPGGGAVA LAGEGGHIEL
     MPVTDDEWIA WRATHASLGR VSAERLLSGM GLSQIHAALS AETGTRVDVP LTPEQVTTGA
     FARHDPLCER TMAVFFGLLG SVAADIALVM GALGGVYLGG GILPRFVPAL QASAFNARFV
     AKGRMRGYLD KLPVYVITAS YPALPGLARA LADTLSHGRP HIG