ID   GLK_BRUA2               Reviewed;         343 AA.
AC   Q2YJN9;
DT   12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT   20-DEC-2005, sequence version 1.
DT   03-AUG-2022, entry version 78.
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=BAB2_1010;
OS   Brucella abortus (strain 2308).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Brucellaceae; Brucella/Ochrobactrum group; Brucella.
OX   NCBI_TaxID=359391;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=2308;
RX   PubMed=16299333; DOI=10.1128/iai.73.12.8353-8361.2005;
RA   Chain P.S., Comerci D.J., Tolmasky M.E., Larimer F.W., Malfatti S.A.,
RA   Vergez L.M., Aguero F., Land M.L., Ugalde R.A., Garcia E.;
RT   "Whole-genome analyses of speciation events in pathogenic Brucellae.";
RL   Infect. Immun. 73:8353-8361(2005).
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; AM040265; CAJ13176.1; -; Genomic_DNA.
DR   RefSeq; WP_002967381.1; NZ_KN046823.1.
DR   AlphaFoldDB; Q2YJN9; -.
DR   SMR; Q2YJN9; -.
DR   STRING; 359391.BAB2_1010; -.
DR   EnsemblBacteria; CAJ13176; CAJ13176; BAB2_1010.
DR   GeneID; 3828237; -.
DR   KEGG; bmf:BAB2_1010; -.
DR   PATRIC; fig|359391.11.peg.697; -.
DR   HOGENOM; CLU_042582_1_0_5; -.
DR   OMA; NNHWRLS; -.
DR   PhylomeDB; Q2YJN9; -.
DR   Proteomes; UP000002719; Chromosome II.
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   Reference proteome; Transferase.
FT   CHAIN           1..343
FT                   /note="Glucokinase"
FT                   /id="PRO_0000268768"
FT   BINDING         18..23
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00524"
SQ   SEQUENCE   343 AA;  37073 MW;  2EBE41BFFF67FEC0 CRC64;
     MQAIIDAEQS FKFPVLVGDI GGTNARFSIL VDSNAEPKEF PVLQTADYAT IDEAIQHAIL
     DQTAIQPRSV ILAVAGPVDG DEIDLTNCDW VVRPKKMIAD LGFEDVTVLN DFEAQALAVV
     SLEGHHMEQI GGKPEEAVAT RVVLGPGTGL GVAGLFRTRH AWVPVPGEGG HIDIGPRTER
     DYQIFPHIER IEGRVTGEQI LSGRGLRNLY LGICAADKIT PTLETPVDIT SAGLDGSNPQ
     AAETLDLFAT YLGRLAGDLA LIFMAHGGVY LSGGIPVRIL SALKAGSFRA TFEDKAPHKA
     IMRDIPVRVI TYQLAALTGL SAFARTPSRF EVSTEGRRWR MRR