GLK_PSEA7
ID GLK_PSEA7 Reviewed; 339 AA.
AC A6V2N1;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 21-AUG-2007, sequence version 1.
DT 03-AUG-2022, entry version 70.
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=PSPA7_1935;
OS Pseudomonas aeruginosa (strain PA7).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=381754;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PA7;
RA Dodson R.J., Harkins D., Paulsen I.T.;
RL Submitted (JUN-2007) 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; CP000744; ABR83238.1; -; Genomic_DNA.
DR RefSeq; WP_012075001.1; NC_009656.1.
DR AlphaFoldDB; A6V2N1; -.
DR SMR; A6V2N1; -.
DR EnsemblBacteria; ABR83238; ABR83238; PSPA7_1935.
DR KEGG; pap:PSPA7_1935; -.
DR HOGENOM; CLU_042582_1_0_6; -.
DR OMA; NNHWRLS; -.
DR OrthoDB; 992687at2; -.
DR Proteomes; UP000001582; 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..339
FT /note="Glucokinase"
FT /id="PRO_1000050973"
FT BINDING 16..21
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00524"
SQ SEQUENCE 339 AA; 35506 MW; 6C5C8CB9ACD78E22 CRC64;
MNNDKNGSSG GLALIGDIGG TNARFALWRG QRLESIAVLA CADYPRPELA VRDYLARVGE
SLANIDSVCL ACAGPVGAGD FRFTNNHWSI NRAAFREELG LDHLLLVNDF STMAWAASRL
GADELVQVRP GSAQADRARL IIGPGTGLGV GSLLPLGEGR WEVLPCEGGH VDLPVTSARD
FAVWESLRER YGHVSAERVL SGNGLLALYE ISCALDGIPV RATSAAEVGA LALAGDAQAD
AVLEHFFLWL ARVAGNAALT VGALGGVYIT GGIVPRFRER FLASGFAGAF ASRGKTSGAY
LQDVPVWIMT AEHPGLLGAG VALQQALDAE SRTGVRATA