GLK_PSEA8
ID GLK_PSEA8 Reviewed; 331 AA.
AC B7V9H3;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 10-FEB-2009, sequence version 1.
DT 03-AUG-2022, entry version 64.
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=PLES_18751;
OS Pseudomonas aeruginosa (strain LESB58).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=557722;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LESB58;
RX PubMed=19047519; DOI=10.1101/gr.086082.108;
RA Winstanley C., Langille M.G.I., Fothergill J.L., Kukavica-Ibrulj I.,
RA Paradis-Bleau C., Sanschagrin F., Thomson N.R., Winsor G.L., Quail M.A.,
RA Lennard N., Bignell A., Clarke L., Seeger K., Saunders D., Harris D.,
RA Parkhill J., Hancock R.E.W., Brinkman F.S.L., Levesque R.C.;
RT "Newly introduced genomic prophage islands are critical determinants of in
RT vivo competitiveness in the Liverpool epidemic strain of Pseudomonas
RT aeruginosa.";
RL Genome Res. 19:12-23(2009).
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; FM209186; CAW26603.1; -; Genomic_DNA.
DR RefSeq; WP_003114838.1; NC_011770.1.
DR AlphaFoldDB; B7V9H3; -.
DR SMR; B7V9H3; -.
DR KEGG; pag:PLES_18751; -.
DR HOGENOM; CLU_042582_1_0_6; -.
DR OMA; NNHWRLS; -.
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_1000127714"
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; 34606 MW; 321718790B5130D1 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 ASRGKTSGAY
LQDVPVWVMT AEHPGLLGAG VALQQALDAE G