ID   GLK_XYLF2               Reviewed;         337 AA.
AC   B2I7Q9;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   10-JUN-2008, sequence version 1.
DT   03-AUG-2022, entry version 60.
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=XfasM23_0337;
OS   Xylella fastidiosa (strain M23).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales;
OC   Xanthomonadaceae; Xylella.
OX   NCBI_TaxID=405441;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=M23;
RX   PubMed=20601474; DOI=10.1128/jb.00651-10;
RA   Chen J., Xie G., Han S., Chertkov O., Sims D., Civerolo E.L.;
RT   "Whole genome sequences of two Xylella fastidiosa strains (M12 and M23)
RT   causing almond leaf scorch disease in California.";
RL   J. Bacteriol. 192:4534-4534(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; CP001011; ACB91785.1; -; Genomic_DNA.
DR   RefSeq; WP_004089300.1; NC_010577.1.
DR   AlphaFoldDB; B2I7Q9; -.
DR   SMR; B2I7Q9; -.
DR   EnsemblBacteria; ACB91785; ACB91785; XfasM23_0337.
DR   GeneID; 58015896; -.
DR   KEGG; xfn:XfasM23_0337; -.
DR   HOGENOM; CLU_042582_1_0_6; -.
DR   OMA; NNHWRLS; -.
DR   Proteomes; UP000001698; 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..337
FT                   /note="Glucokinase"
FT                   /id="PRO_1000127729"
FT   BINDING         11..16
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00524"
SQ   SEQUENCE   337 AA;  36273 MW;  0A78312314E4DEC1 CRC64;
     MNAPQAPVLV ADIGGTNARF ALANPTLTSA PLLNDSMREF AVIEFPSLGE AAQHYLHHIG
     IHTTKGVFAI AGHVDGDEAR ITNHPWVITR TRTATMLGFD TLHLINDFVA QAMAISVLGP
     QDVIQIGSAK WEQFPLSAAT RNYGIIGPGT GLGVGGLMIR NGRCYPLETE GGHVSFPPST
     PEEIRILEIL SQQFGRVSNE RLISGPGIVN IHRALSEIDG IDPGPLRPQD ITMRAADGDI
     RATRTINLFC NIFGTITGDL VLIQGAWDGV FLTGGLVPKL LNSIQHSGFR QRFEHKGRFS
     AIMARIPSLA VIHPHPGLLG AAAYARDTEQ VPQEIKA