ID   GLK_ERWT9               Reviewed;         321 AA.
AC   B2VE30;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-2008, sequence version 1.
DT   18-JUN-2025, entry version 86.
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=ETA_11140;
OS   Erwinia tasmaniensis (strain DSM 17950 / CFBP 7177 / CIP 109463 / NCPPB
OS   4357 / Et1/99).
OC   Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
OC   Enterobacterales; Erwiniaceae; Erwinia.
OX   NCBI_TaxID=465817;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 17950 / CFBP 7177 / CIP 109463 / NCPPB 4357 / Et1/99;
RX   PubMed=18462403; DOI=10.1111/j.1462-2920.2008.01639.x;
RA   Kube M., Migdoll A.M., Mueller I., Kuhl H., Beck A., Reinhardt R.,
RA   Geider K.;
RT   "The genome of Erwinia tasmaniensis strain Et1/99, a non-pathogenic
RT   bacterium in the genus Erwinia.";
RL   Environ. Microbiol. 10:2211-2222(2008).
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; CU468135; CAO96160.1; -; Genomic_DNA.
DR   RefSeq; WP_012440860.1; NC_010694.1.
DR   AlphaFoldDB; B2VE30; -.
DR   SMR; B2VE30; -.
DR   STRING; 465817.ETA_11140; -.
DR   KEGG; eta:ETA_11140; -.
DR   eggNOG; COG0837; Bacteria.
DR   HOGENOM; CLU_042582_1_0_6; -.
DR   OrthoDB; 9800595at2; -.
DR   Proteomes; UP000001726; 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; 3.40.367.20: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   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_1000127707"
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;  34958 MW;  F3552D11EEEF0B1F CRC64;
     MTKYALVGDV GGTNARLALC EIDNGAISQA KTFSTADYDS LEAVIRAYLA EKQQDIKHGC
     IAIACPITDD WVEMTNHDWA FSTSSMKANL AFDSLEIIND FTAVSMAIPM LSEEHLMQFG
     GTTPAEDKPV AVYGAGTGLG VAHLVHVDKR WVSLPGEGGH VDFAANSEEE DLILEVLREE
     LGHVSAERIL SGNGLVNLYR AIVKSDHRQP EDLKPRDVTE RALQDTCTDC RRALSMFCVI
     MGRFGGNLAL NLGTFGGVYI AGGIVPRFLE FFKASGFRAA FEDKGRFKDY VAPIPVYLIT
     HDYPGLLGSG AHLRQTLGRV L
//