ID GLK_HAHCH Reviewed; 322 AA. AC Q2SPT0; DT 12-DEC-2006, integrated into UniProtKB/Swiss-Prot. DT 24-JAN-2006, sequence version 1. DT 27-MAR-2024, entry version 89. 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=HCH_00434; OS Hahella chejuensis (strain KCTC 2396). OC Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales; OC Hahellaceae; Hahella. OX NCBI_TaxID=349521; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=KCTC 2396; RX PubMed=16352867; DOI=10.1093/nar/gki1016; RA Jeong H., Yim J.H., Lee C., Choi S.-H., Park Y.K., Yoon S.H., Hur C.-G., RA Kang H.-Y., Kim D., Lee H.H., Park K.H., Park S.-H., Park H.-S., Lee H.K., RA Oh T.K., Kim J.F.; RT "Genomic blueprint of Hahella chejuensis, a marine microbe producing an RT algicidal agent."; RL Nucleic Acids Res. 33:7066-7073(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}. 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; CP000155; ABC27344.1; -; Genomic_DNA. DR RefSeq; WP_011394421.1; NC_007645.1. DR AlphaFoldDB; Q2SPT0; -. DR SMR; Q2SPT0; -. DR STRING; 349521.HCH_00434; -. DR KEGG; hch:HCH_00434; -. DR eggNOG; COG0837; Bacteria. DR HOGENOM; CLU_042582_1_0_6; -. DR OrthoDB; 9800595at2; -. DR Proteomes; UP000000238; Chromosome. 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 Reference proteome; Transferase. FT CHAIN 1..322 FT /note="Glucokinase" FT /id="PRO_0000268774" FT BINDING 10..15 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00524" SQ SEQUENCE 322 AA; 35028 MW; E80521B264A321D5 CRC64; MSKAQYALVG DIGGTNARFA LVARDSFELE HIQVLPCNDY ANLDEAVRDY LAHHPEAEVH EACMAFACPV HGDTIKMTNN HWTFNKADMQ ARLGFDTFKY VNDFTAMALG TLHVADERLQ KVGGGEGKDG AARLVIGPGT GLGVSGLVRT MTDWAPLSTE GGHVDFAPTD EVEISVLRIL KERFGRVSVE RILCGEGLLN LYRSLCEIDG VEPAHTQPSQ VTEAALANSD VIAHKTLKLF CAIFGRVTGN AALTLGALGG VYVCGGIIPR FIEFFRDSDF RQCFEDKGRM RDYLGGIPVY VVTETYTGLL GAAEALKNQE VH //