ID   GLK_CROS8               Reviewed;         321 AA.
AC   A7MP52;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   02-OCT-2007, sequence version 1.
DT   18-JUN-2025, entry version 85.
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};
GN   OrderedLocusNames=ESA_00852;
OS   Cronobacter sakazakii (strain ATCC BAA-894) (Enterobacter sakazakii).
OC   Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
OC   Enterobacterales; Enterobacteriaceae; Cronobacter.
OX   NCBI_TaxID=290339;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-894;
RX   PubMed=20221447; DOI=10.1371/journal.pone.0009556;
RA   Kucerova E., Clifton S.W., Xia X.Q., Long F., Porwollik S., Fulton L.,
RA   Fronick C., Minx P., Kyung K., Warren W., Fulton R., Feng D., Wollam A.,
RA   Shah N., Bhonagiri V., Nash W.E., Hallsworth-Pepin K., Wilson R.K.,
RA   McClelland M., Forsythe S.J.;
RT   "Genome sequence of Cronobacter sakazakii BAA-894 and comparative genomic
RT   hybridization analysis with other Cronobacter species.";
RL   PLoS ONE 5:E9556-E9556(2010).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=D-glucose + ATP = D-glucose 6-phosphate + ADP + 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; CP000783; ABU76123.1; -; Genomic_DNA.
DR   RefSeq; WP_004388531.1; NC_009778.1.
DR   AlphaFoldDB; A7MP52; -.
DR   SMR; A7MP52; -.
DR   KEGG; esa:ESA_00852; -.
DR   PATRIC; fig|290339.8.peg.755; -.
DR   HOGENOM; CLU_042582_1_0_6; -.
DR   Proteomes; UP000000260; Chromosome.
DR   GO; GO:0005829; C:cytosol; IEA:TreeGrafter.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0005536; F:D-glucose binding; IEA:InterPro.
DR   GO; GO:0004340; F:glucokinase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-UniRule.
DR   CDD; cd24008; ASKHA_NBD_GLK; 1.
DR   FunFam; 3.30.420.40:FF:000045; Glucokinase; 1.
DR   FunFam; 3.40.367.20:FF:000002; Glucokinase; 1.
DR   Gene3D; 3.30.420.40; -; 1.
DR   Gene3D; 3.40.367.20; -; 1.
DR   HAMAP; MF_00524; Glucokinase; 1.
DR   InterPro; IPR043129; ATPase_NBD.
DR   InterPro; IPR050201; Bacterial_glucokinase.
DR   InterPro; IPR003836; Glucokinase.
DR   NCBIfam; TIGR00749; glk; 1.
DR   NCBIfam; NF001414; PRK00292.1-1; 1.
DR   NCBIfam; NF001416; PRK00292.1-3; 1.
DR   NCBIfam; NF009073; PRK12408.1; 1.
DR   PANTHER; PTHR47690; GLUCOKINASE; 1.
DR   PANTHER; PTHR47690:SF1; GLUCOKINASE; 1.
DR   Pfam; PF02685; Glucokinase; 1.
DR   SUPFAM; SSF53067; Actin-like ATPase domain; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Cytoplasm; Glycolysis; Kinase; Nucleotide-binding;
KW   Reference proteome; Transferase.
FT   CHAIN           1..321
FT                   /note="Glucokinase"
FT                   /id="PRO_1000050968"
FT   BINDING         8..13
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00524"
SQ   SEQUENCE   321 AA;  34569 MW;  70AC5F69D73B0786 CRC64;
     MTKYALVGDV GGTNARLALC DVDSGEILKA KTYSGLDYPS LEAVVRVYLE EHNATVTDGC
     IAIACPITGD WVAMTNHVWA FSVAEMKKNL GFDHLEIIND FTAVSMAIPM LKTDHLIQFG
     GGEPQPNKPI AVYGAGTGLG VAHLVHVDKR WVSLPGEGGH VDFAPNSEEE AIILEQLRAE
     VGHVSAERVL SGPGLVNLYR AIVKADGRLP DNLRPKDITE RALDDSCTDC RRALSLFCVI
     MGRFGGNLAL TLGTFGGVYI AGGIVPRFLD FFTSSGFRGG FEDKGRFKSY VQDIPVYLIV
     HDQPGLLGAG AHLRQTLGQI L
//