GLK_BRUSU
ID GLK_BRUSU Reviewed; 343 AA.
AC Q8FV09; G0KE55;
DT 07-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 92.
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=BRA1049, BS1330_II1041;
OS Brucella suis biovar 1 (strain 1330).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Brucellaceae; Brucella/Ochrobactrum group; Brucella.
OX NCBI_TaxID=204722;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1330;
RX PubMed=12271122; DOI=10.1073/pnas.192319099;
RA Paulsen I.T., Seshadri R., Nelson K.E., Eisen J.A., Heidelberg J.F.,
RA Read T.D., Dodson R.J., Umayam L.A., Brinkac L.M., Beanan M.J.,
RA Daugherty S.C., DeBoy R.T., Durkin A.S., Kolonay J.F., Madupu R.,
RA Nelson W.C., Ayodeji B., Kraul M., Shetty J., Malek J.A., Van Aken S.E.,
RA Riedmuller S., Tettelin H., Gill S.R., White O., Salzberg S.L.,
RA Hoover D.L., Lindler L.E., Halling S.M., Boyle S.M., Fraser C.M.;
RT "The Brucella suis genome reveals fundamental similarities between animal
RT and plant pathogens and symbionts.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:13148-13153(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1330;
RX PubMed=22038969; DOI=10.1128/jb.06181-11;
RA Tae H., Shallom S., Settlage R., Preston D., Adams L.G., Garner H.R.;
RT "Revised genome sequence of Brucella suis 1330.";
RL J. Bacteriol. 193:6410-6410(2011).
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; AE014292; AAN34216.1; -; Genomic_DNA.
DR EMBL; CP002998; AEM20493.1; -; Genomic_DNA.
DR RefSeq; WP_004690408.1; NZ_KN046805.1.
DR AlphaFoldDB; Q8FV09; -.
DR SMR; Q8FV09; -.
DR PRIDE; Q8FV09; -.
DR EnsemblBacteria; AEM20493; AEM20493; BS1330_II1041.
DR GeneID; 45054034; -.
DR GeneID; 55592670; -.
DR KEGG; bms:BRA1049; -.
DR KEGG; bsi:BS1330_II1041; -.
DR PATRIC; fig|204722.21.peg.1071; -.
DR HOGENOM; CLU_042582_1_0_5; -.
DR OMA; NNHWRLS; -.
DR PhylomeDB; Q8FV09; -.
DR Proteomes; UP000007104; 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 Transferase.
FT CHAIN 1..343
FT /note="Glucokinase"
FT /id="PRO_0000215122"
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; 36995 MW; C0BE5AB4F5DCE5D1 CRC64;
MQAIIDAEQS FKFPVLVGDI GGTNARFSIL VDSNAEPKEF PVLQTADYAT IDEAIQHAIL
DQTAIQPRSV ILAVAGPVDG DEIDLTNCDW VVRPKKMIAD LGFEDVTVLN DFEAQALAVV
SLEGHHMEQI GGKPEEAVAT RVVLGPGTGL GVAGLVRTRH AWVPVPGEGG HIDIGPRTER
DYQIFPHIER IEGRVTGEQI LSGRGLRNLY LGICAADKIT PTLETPVDIT SAGLDGSNPQ
AAETLDLFAT YLGRLAGDLA LIFMAHGGVY LSGGIPVRIL SALKAGSFRA AFEDKAPHKA
IMRDIPVRVI TYQLAALTGL SAFARTPSRF EVSTEGRRWR MRR