ID   GLK_BRUAB               Reviewed;         343 AA.
AC   P0CB37; Q576R6; Q59171;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   22-SEP-2009, sequence version 1.
DT   27-MAR-2024, 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};
GN   OrderedLocusNames=BruAb2_0989;
OS   Brucella abortus biovar 1 (strain 9-941).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC   Brucellaceae; Brucella/Ochrobactrum group; Brucella.
OX   NCBI_TaxID=262698;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=9-941;
RX   PubMed=15805518; DOI=10.1128/jb.187.8.2715-2726.2005;
RA   Halling S.M., Peterson-Burch B.D., Bricker B.J., Zuerner R.L., Qing Z.,
RA   Li L.-L., Kapur V., Alt D.P., Olsen S.C.;
RT   "Completion of the genome sequence of Brucella abortus and comparison to
RT   the highly similar genomes of Brucella melitensis and Brucella suis.";
RL   J. Bacteriol. 187:2715-2726(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; AE017224; AAX76368.1; -; Genomic_DNA.
DR   RefSeq; WP_002967381.1; NC_006933.1.
DR   AlphaFoldDB; P0CB37; -.
DR   SMR; P0CB37; -.
DR   EnsemblBacteria; AAX76368; AAX76368; BruAb2_0989.
DR   GeneID; 3828237; -.
DR   KEGG; bmb:BruAb2_0989; -.
DR   HOGENOM; CLU_042582_1_0_5; -.
DR   Proteomes; UP000000540; 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   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..343
FT                   /note="Glucokinase"
FT                   /id="PRO_0000215120"
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
//