ID   GLK_STRMK               Reviewed;         335 AA.
AC   B2FL80;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   10-JUN-2008, sequence version 1.
DT   03-AUG-2022, entry version 67.
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=Smlt1792;
OS   Stenotrophomonas maltophilia (strain K279a).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales;
OC   Xanthomonadaceae; Stenotrophomonas; Stenotrophomonas maltophilia group.
OX   NCBI_TaxID=522373;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K279a;
RX   PubMed=18419807; DOI=10.1186/gb-2008-9-4-r74;
RA   Crossman L.C., Gould V.C., Dow J.M., Vernikos G.S., Okazaki A.,
RA   Sebaihia M., Saunders D., Arrowsmith C., Carver T., Peters N., Adlem E.,
RA   Kerhornou A., Lord A., Murphy L., Seeger K., Squares R., Rutter S.,
RA   Quail M.A., Rajandream M.A., Harris D., Churcher C., Bentley S.D.,
RA   Parkhill J., Thomson N.R., Avison M.B.;
RT   "The complete genome, comparative and functional analysis of
RT   Stenotrophomonas maltophilia reveals an organism heavily shielded by drug
RT   resistance determinants.";
RL   Genome Biol. 9:R74.1-R74.13(2008).
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; AM743169; CAQ45313.1; -; Genomic_DNA.
DR   RefSeq; WP_005412971.1; NC_010943.1.
DR   AlphaFoldDB; B2FL80; -.
DR   SMR; B2FL80; -.
DR   STRING; 522373.Smlt1792; -.
DR   EnsemblBacteria; CAQ45313; CAQ45313; Smlt1792.
DR   GeneID; 61465631; -.
DR   KEGG; sml:Smlt1792; -.
DR   eggNOG; COG0837; Bacteria.
DR   HOGENOM; CLU_042582_1_0_6; -.
DR   OMA; NNHWRLS; -.
DR   OrthoDB; 992687at2; -.
DR   Proteomes; UP000008840; 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..335
FT                   /note="Glucokinase"
FT                   /id="PRO_1000127727"
FT   BINDING         11..16
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00524"
SQ   SEQUENCE   335 AA;  35266 MW;  0000C36BA325CCEF CRC64;
     MSANSQPVLV ADIGGTNARF ALADTSLDAP LLKESIREYA VAEFPSLGDA ARHHLEQIGA
     AASRGVFAVA GRVDGDEARI TNHPWVISRS RTAAMLGFDE LHLINDFAAQ AMAISLLQPE
     DVVQVGGAAW VPGKPGQPRN YAVIGPGTGL GVGGLILRHG RCYPLETEGG HVSFPPGTPE
     EIRILEILSE QFGRVSNERL ICGPGLVNIH RAVCEMAGID PGQLQPVDVT ARALHGDPQA
     MRTVDVFCAV FGAIAGDLVL TQGAWDGVFL TGGLTPKMLD SLQHSGFRQR FEHKGRFSSI
     MARVPSLAVM HPHAGLLGAA AYAADAERDA PGVAA