ID   GLK_CHESB               Reviewed;         342 AA.
AC   Q11CB2;
DT   12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT   22-AUG-2006, sequence version 1.
DT   03-AUG-2022, entry version 76.
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=Meso_3594;
OS   Chelativorans sp. (strain BNC1).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Phyllobacteriaceae; Chelativorans; unclassified Chelativorans.
OX   NCBI_TaxID=266779;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BNC1;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA   Chertkov O., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Richardson P.;
RT   "Complete sequence of chromosome of Mesorhizobium sp. BNC1.";
RL   Submitted (JUN-2006) 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}.
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DR   EMBL; CP000390; ABG64963.1; -; Genomic_DNA.
DR   RefSeq; WP_011582904.1; NC_008254.1.
DR   AlphaFoldDB; Q11CB2; -.
DR   SMR; Q11CB2; -.
DR   STRING; 266779.Meso_3594; -.
DR   EnsemblBacteria; ABG64963; ABG64963; Meso_3594.
DR   KEGG; mes:Meso_3594; -.
DR   eggNOG; COG0837; Bacteria.
DR   HOGENOM; CLU_042582_1_0_5; -.
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..342
FT                   /note="Glucokinase"
FT                   /id="PRO_0000268777"
FT   BINDING         18..23
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00524"
SQ   SEQUENCE   342 AA;  36572 MW;  7D1C986971B2BD5A CRC64;
     MAYSTDHDVV LDFPILIGDI GGTNARFAIV VDSYAEPREF PVVQTADFAT IEDAIQTAIL
     DQTHLIPRSA VLAVAGPVNG DEIDLTNSNW VVRPREMMAH LGFSDIVVLN DFEAQALAVV
     ALGEEHLEKI GGNVAETVGS RVVLGPGTGL GVAGLVHARR TWIPVPGEGG HMDLGPRTAR
     DEQIFPHLER IEGRVSGEQV LCGRGLVNLY RAIAKADAKE AAFSSPAEIT TAGLAQADEI
     AVETLNLFVT YLGRVAGDLG LVFMSRGGVF LTGGIAQKIV PALKNSLFRA AFEDKAPHNE
     LMASMPVYVI THPLAALHGL AAYARTPARF GVETAGRRWR LR