ID   GLK_XANCB               Reviewed;         335 AA.
AC   B0RSF9;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   08-APR-2008, sequence version 1.
DT   27-MAR-2024, entry version 73.
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=xcc-b100_2041;
OS   Xanthomonas campestris pv. campestris (strain B100).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC   Xanthomonadaceae; Xanthomonas.
OX   NCBI_TaxID=509169;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=B100;
RX   PubMed=18304669; DOI=10.1016/j.jbiotec.2007.12.013;
RA   Vorhoelter F.-J., Schneiker S., Goesmann A., Krause L., Bekel T.,
RA   Kaiser O., Linke B., Patschkowski T., Rueckert C., Schmid J., Sidhu V.K.,
RA   Sieber V., Tauch A., Watt S.A., Weisshaar B., Becker A., Niehaus K.,
RA   Puehler A.;
RT   "The genome of Xanthomonas campestris pv. campestris B100 and its use for
RT   the reconstruction of metabolic pathways involved in xanthan
RT   biosynthesis.";
RL   J. Biotechnol. 134:33-45(2008).
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; AM920689; CAP51394.1; -; Genomic_DNA.
DR   AlphaFoldDB; B0RSF9; -.
DR   SMR; B0RSF9; -.
DR   KEGG; xca:xcc-b100_2041; -.
DR   HOGENOM; CLU_042582_1_0_6; -.
DR   Proteomes; UP000001188; 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   Gene3D; 3.30.420.40; -; 1.
DR   Gene3D; 3.40.367.20; -; 1.
DR   HAMAP; MF_00524; Glucokinase; 1.
DR   InterPro; IPR043129; ATPase_NBD.
DR   InterPro; IPR003836; Glucokinase.
DR   NCBIfam; TIGR00749; glk; 1.
DR   PANTHER; PTHR47690; GLUCOKINASE; 1.
DR   PANTHER; PTHR47690:SF1; GLUCOKINASE; 1.
DR   Pfam; PF02685; Glucokinase; 1.
DR   SUPFAM; SSF53067; Actin-like ATPase domain; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Cytoplasm; Glycolysis; Kinase; Nucleotide-binding;
KW   Transferase.
FT   CHAIN           1..335
FT                   /note="Glucokinase"
FT                   /id="PRO_1000127728"
FT   BINDING         11..16
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00524"
SQ   SEQUENCE   335 AA;  35535 MW;  2DADE701903A8378 CRC64;
     MTAPSKPVLV ADIGGTNARF ALADIDASVP LLDDTCREFA VVEFGSLGEA ARYYLDQIGV
     QATKGVFAVA GRVDGDEARI TNHPWVISRS RTATMLGFST LHLINDFAAQ AMAISLLRPQ
     DVVQVGGASW RPAPIEQPRN YGVIGPGTGL GVGGLIIRNG RCFPLETEGG HVSFPPGTPE
     EIRVLEILSE QFGRVSNERL ICGPGLVNIH RALSEIAGID PGPLEPKDIT ARAAAGDPRA
     SRTIDLFCAI FGAIAGDMVL MQGAWDGVFL TGGLVPKVLD SLQHSGFRQR FEHKGRFSAI
     MSRVPSLAVM HPHAGLLGAA AYAVDAERAL PGEQR
//