ID GLK_HALH5 Reviewed; 330 AA. AC Q9KCZ4; DT 23-JAN-2002, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2000, sequence version 1. DT 27-MAR-2024, entry version 107. DE RecName: Full=Glucokinase; DE EC=2.7.1.2; DE AltName: Full=Glucose kinase; GN Name=glcK; Synonyms=glk; OrderedLocusNames=BH1425; OS Halalkalibacterium halodurans (strain ATCC BAA-125 / DSM 18197 / FERM 7344 OS / JCM 9153 / C-125) (Bacillus halodurans). OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; OC Halalkalibacterium (ex Joshi et al. 2022). OX NCBI_TaxID=272558; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC BAA-125 / DSM 18197 / FERM 7344 / JCM 9153 / C-125; RX PubMed=11058132; DOI=10.1093/nar/28.21.4317; RA Takami H., Nakasone K., Takaki Y., Maeno G., Sasaki R., Masui N., Fuji F., RA Hirama C., Nakamura Y., Ogasawara N., Kuhara S., Horikoshi K.; RT "Complete genome sequence of the alkaliphilic bacterium Bacillus halodurans RT and genomic sequence comparison with Bacillus subtilis."; RL Nucleic Acids Res. 28:4317-4331(2000). 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 -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. CC -!- SIMILARITY: Belongs to the ROK (NagC/XylR) family. {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; BA000004; BAB05144.1; -; Genomic_DNA. DR PIR; A83828; A83828. DR RefSeq; WP_010897590.1; NC_002570.2. DR AlphaFoldDB; Q9KCZ4; -. DR SMR; Q9KCZ4; -. DR STRING; 272558.gene:10727323; -. DR KEGG; bha:BH1425; -. DR eggNOG; COG1940; Bacteria. DR HOGENOM; CLU_036604_0_1_9; -. DR OrthoDB; 9810372at2; -. DR Proteomes; UP000001258; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0004340; F:glucokinase activity; IEA:UniProtKB-EC. DR GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-KW. DR CDD; cd00012; NBD_sugar-kinase_HSP70_actin; 1. DR Gene3D; 3.30.420.40; -; 2. DR InterPro; IPR043129; ATPase_NBD. DR InterPro; IPR000600; ROK. DR InterPro; IPR004654; ROK_glcA. DR NCBIfam; TIGR00744; ROK_glcA_fam; 1. DR PANTHER; PTHR18964:SF149; BIFUNCTIONAL UDP-N-ACETYLGLUCOSAMINE 2-EPIMERASE_N-ACETYLMANNOSAMINE KINASE; 1. DR PANTHER; PTHR18964; ROK (REPRESSOR, ORF, KINASE) FAMILY; 1. DR Pfam; PF00480; ROK; 1. DR SUPFAM; SSF53067; Actin-like ATPase domain; 1. DR PROSITE; PS01125; ROK; 1. PE 3: Inferred from homology; KW ATP-binding; Cytoplasm; Glycolysis; Kinase; Nucleotide-binding; KW Reference proteome; Transferase. FT CHAIN 1..330 FT /note="Glucokinase" FT /id="PRO_0000095675" SQ SEQUENCE 330 AA; 34496 MW; E5448D6CBD87456F CRC64; MSDRWYVGVD VGGTTIKMAF LTTAGEIVDK WEIPTNKQDG GALITTNIAD ALDKRLSGHH KSKSDLIGIG LGAPGFIEMD TGFIYHAVNI GWRDFPLKDK LEEETKLPVI VDNDANIAAL GEMWKGAGDG AKNMLLITLG TGVGGGIVAN GNILHGVNGM AGEIGHITVI PEGGAPCNCG KTGCLETVAS ATGIARIATE GVTEHKESQL ALDYDKHGVL TAKDVFSAAD ASDAFALSVV DHIAYYLGFA IANLANALNP EKIVIGGGVS KAGDTLLKPI KQHFEAYALP RVADGAEFRI ATLGNDAGVI GGGWLVKQQE NSMEKGNETE //