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 27-MAR-2024, entry version 100. 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=BMEII0251; OS Brucella melitensis biotype 1 (strain 16M / ATCC 23456 / NCTC 10094). OC Bacteria; Pseudomonadota; 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}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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 GeneID; 29595726; -. DR KEGG; bme:BMEII0251; -. DR KEGG; bmel:DK63_2990; -. DR PATRIC; fig|224914.52.peg.3136; -. DR eggNOG; COG0837; Bacteria. 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 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_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 //