GLK_BRUME
ID GLK_BRUME Reviewed; 343 AA.
AC Q8YDC6;
DT 06-JUN-2002, integrated into UniProtKB/Swiss-Prot.
DT 06-JUN-2002, sequence version 2.
DT 03-AUG-2022, entry version 94.
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=BMEII0251;
OS Brucella melitensis biotype 1 (strain 16M / ATCC 23456 / NCTC 10094).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Brucellaceae; Brucella/Ochrobactrum group; Brucella.
OX NCBI_TaxID=224914;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=16M / ATCC 23456 / NCTC 10094;
RX PubMed=11756688; DOI=10.1073/pnas.221575398;
RA DelVecchio V.G., Kapatral V., Redkar R.J., Patra G., Mujer C., Los T.,
RA Ivanova N., Anderson I., Bhattacharyya A., Lykidis A., Reznik G.,
RA Jablonski L., Larsen N., D'Souza M., Bernal A., Mazur M., Goltsman E.,
RA Selkov E., Elzer P.H., Hagius S., O'Callaghan D., Letesson J.-J.,
RA Haselkorn R., Kyrpides N.C., Overbeek R.;
RT "The genome sequence of the facultative intracellular pathogen Brucella
RT melitensis.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:443-448(2002).
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAL53492.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AE008918; AAL53492.1; ALT_INIT; Genomic_DNA.
DR PIR; AI3540; AI3540.
DR RefSeq; WP_004682470.1; NZ_GG703779.1.
DR AlphaFoldDB; Q8YDC6; -.
DR SMR; Q8YDC6; -.
DR STRING; 224914.BMEII0251; -.
DR EnsemblBacteria; AAL53492; AAL53492; BMEII0251.
DR GeneID; 29595726; -.
DR KEGG; bme:BMEII0251; -.
DR KEGG; bmel:DK63_2990; -.
DR PATRIC; fig|224914.52.peg.3136; -.
DR eggNOG; COG0837; Bacteria.
DR OMA; NNHWRLS; -.
DR PhylomeDB; Q8YDC6; -.
DR Proteomes; UP000000419; 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_0000215121"
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; 36919 MW; 8984E115FE71B9EE CRC64;
MQAIIDAEQS FKFPVLVGDI GGTNARFSIL VDSNAEPKEF PVLQTADYAT IDEAIQHAIL
DQTAIQPRSV ILAVAGPVDG DEIDLTNCDW VVRPKKMIAD LGFEDVTVLN DFEAQALAVV
SLEGHHMEQI GGKPEEAVAT RVVLGPGTGL GVAGLVCTRH AWVPVPGEGG HIDIGPRTER
DYQIFPHIER IEGRVTGEQI LSGRGLRNLY LGICAADKIT PTLETPVDIT SAGLDGSNPQ
AAETLDLFAT YLGRLAGDLA LIFMAHGGVY LSGGIPVRIL SALKAGSFRA AFEDKAPNKA
IMRDIPVRVI TYQLAALTGL SAFARTPSRF EVSTEGRRWR MRR
