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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
 
 
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