ID   GLK_SHISS               Reviewed;         321 AA.
AC   Q3YZE4;
DT   12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT   27-SEP-2005, sequence version 1.
DT   27-MAR-2024, entry version 93.
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=SSON_2480;
OS   Shigella sonnei (strain Ss046).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Shigella.
OX   NCBI_TaxID=300269;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Ss046;
RX   PubMed=16275786; DOI=10.1093/nar/gki954;
RA   Yang F., Yang J., Zhang X., Chen L., Jiang Y., Yan Y., Tang X., Wang J.,
RA   Xiong Z., Dong J., Xue Y., Zhu Y., Xu X., Sun L., Chen S., Nie H., Peng J.,
RA   Xu J., Wang Y., Yuan Z., Wen Y., Yao Z., Shen Y., Qiang B., Hou Y., Yu J.,
RA   Jin Q.;
RT   "Genome dynamics and diversity of Shigella species, the etiologic agents of
RT   bacillary dysentery.";
RL   Nucleic Acids Res. 33:6445-6458(2005).
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; CP000038; AAZ89118.1; -; Genomic_DNA.
DR   RefSeq; WP_000170351.1; NC_007384.1.
DR   AlphaFoldDB; Q3YZE4; -.
DR   SMR; Q3YZE4; -.
DR   KEGG; ssn:SSON_2480; -.
DR   HOGENOM; CLU_042582_1_0_6; -.
DR   Proteomes; UP000002529; 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   CDD; cd00012; NBD_sugar-kinase_HSP70_actin; 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; IPR003836; Glucokinase.
DR   NCBIfam; TIGR00749; glk; 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_0000268789"
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;  34726 MW;  AF62B534641A32C9 CRC64;
     MTKYALVGDV GGTNARLALC DIASGEISQA KTYSGLDYPS LEAVIRVYLE EHKVEVKDGC
     IAIACPITGD WVAMTNHTWA FSIAEMKKNL GFSHLEIIND FTAVSMAIPM LKKEHLIQFG
     GAEPVEGKPI AVYGAGTGLG VAHLVHVDKR WVSLPGEGGH VDFAPNSEEE AIILEILRAE
     IGHVSAERVL SGPGLVNLYR AIVKADNRLP ENLKPKDITE RALADSCTDC RRALSLFCVI
     MGRFGGNLAL TLGTFGGVYI AGGIVPRFLE FFKASGFRAA FEDKGRFKEY VHDIPVYLIV
     HDNPGLLGSG AHLRQTLGHI L
//