ID   GLK_PSEAB               Reviewed;         331 AA.
AC   Q02PZ9;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   14-NOV-2006, sequence version 1.
DT   03-AUG-2022, entry version 71.
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=PA14_22930;
OS   Pseudomonas aeruginosa (strain UCBPP-PA14).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=208963;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UCBPP-PA14;
RX   PubMed=17038190; DOI=10.1186/gb-2006-7-10-r90;
RA   Lee D.G., Urbach J.M., Wu G., Liberati N.T., Feinbaum R.L., Miyata S.,
RA   Diggins L.T., He J., Saucier M., Deziel E., Friedman L., Li L., Grills G.,
RA   Montgomery K., Kucherlapati R., Rahme L.G., Ausubel F.M.;
RT   "Genomic analysis reveals that Pseudomonas aeruginosa virulence is
RT   combinatorial.";
RL   Genome Biol. 7:R90.1-R90.14(2006).
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; CP000438; ABJ12418.1; -; Genomic_DNA.
DR   RefSeq; WP_003091477.1; NZ_CP034244.1.
DR   AlphaFoldDB; Q02PZ9; -.
DR   SMR; Q02PZ9; -.
DR   PRIDE; Q02PZ9; -.
DR   EnsemblBacteria; ABJ12418; ABJ12418; PA14_22930.
DR   KEGG; pau:PA14_22930; -.
DR   HOGENOM; CLU_042582_1_0_6; -.
DR   OMA; NNHWRLS; -.
DR   BioCyc; PAER208963:G1G74-1909-MON; -.
DR   Proteomes; UP000000653; 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   Transferase.
FT   CHAIN           1..331
FT                   /note="Glucokinase"
FT                   /id="PRO_1000050974"
FT   BINDING         16..21
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00524"
SQ   SEQUENCE   331 AA;  34675 MW;  D3520D790B5130D0 CRC64;
     MNNDNKRSAG GLGLVGDIGG TNARFALWRG QRLESIEVLA CADYPRPELA VRDYLARIGE
     SVANIDSVCL ACAGPVGAAD FRFTNNHWVI NRAAFREELG LDHLLLVNDF STMAWAASRL
     GADELVQVRA GSAQADRARL IIGPGTGLGV GSLLPLGGGR WEVLPCEGGH VDLPVTSPRD
     FALWQGLQAR YGHVSAERAL SGNGLLALYE ISCALDGVAV RASSAAEVGA LAMAGDAQAD
     AVLEHFFLWL ARVAGNAVLT VGALGGVYIT GGIVPRFLER FIASGFAEAF ARRGKTSGAY
     LQDVPVWVMT AEHPGLLGAG VALQQALDAE G