GLK_YERPG
ID GLK_YERPG Reviewed; 323 AA.
AC A9QZG0;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 05-FEB-2008, sequence version 1.
DT 03-AUG-2022, entry version 74.
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=YpAngola_A2728;
OS Yersinia pestis bv. Antiqua (strain Angola).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Yersiniaceae; Yersinia.
OX NCBI_TaxID=349746;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Angola;
RX PubMed=20061468; DOI=10.1128/jb.01518-09;
RA Eppinger M., Worsham P.L., Nikolich M.P., Riley D.R., Sebastian Y., Mou S.,
RA Achtman M., Lindler L.E., Ravel J.;
RT "Genome sequence of the deep-rooted Yersinia pestis strain Angola reveals
RT new insights into the evolution and pangenome of the plague bacterium.";
RL J. Bacteriol. 192:1685-1699(2010).
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; CP000901; ABX85202.1; -; Genomic_DNA.
DR RefSeq; WP_002211615.1; NZ_CP009935.1.
DR AlphaFoldDB; A9QZG0; -.
DR SMR; A9QZG0; -.
DR GeneID; 66844879; -.
DR KEGG; ypg:YpAngola_A2728; -.
DR PATRIC; fig|349746.12.peg.3760; -.
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..323
FT /note="Glucokinase"
FT /id="PRO_1000127732"
FT BINDING 8..13
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00524"
SQ SEQUENCE 323 AA; 34664 MW; A2465D600781CE37 CRC64;
MTTYALVGDV GGTNARLALC AVATGEILQA KTYSGLEYES LEDVIKQYLS EHQAKVTDAC
IAIACPITGD WVAMTNHTWA FSIAAMQQNL GLDHLEVIND FTAVSMAIPV LPAQDVLQFG
GTQPQPGKPV AVYGAGTGLG VAHLVNVDRR WISLAGEGGH VDFAPNSEEE DQILAVLRQE
LGHVSAERVL SGPGLVNLYR AIVISDARLP EKLAPKDITA RALADSCTDC RRALSLFCVI
MGRFGGNLAL NLSTFGGVYI AGGIVPRFME FFKASGFRAA FEDKGRFKDF LQDIPVYMIT
HPQPGLLGAG AYLRQKLGYE LSS