GLK_HELAH
ID GLK_HELAH Reviewed; 336 AA.
AC Q17YK6;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 25-JUL-2006, sequence version 1.
DT 03-AUG-2022, entry version 85.
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=Hac_0439;
OS Helicobacter acinonychis (strain Sheeba).
OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC Helicobacteraceae; Helicobacter.
OX NCBI_TaxID=382638;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Sheeba;
RX PubMed=16789826; DOI=10.1371/journal.pgen.0020120;
RA Eppinger M., Baar C., Linz B., Raddatz G., Lanz C., Keller H., Morelli G.,
RA Gressmann H., Achtman M., Schuster S.C.;
RT "Who ate whom? Adaptive Helicobacter genomic changes that accompanied a
RT host jump from early humans to large felines.";
RL PLoS Genet. 2:1097-1110(2006).
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; AM260522; CAJ99270.1; -; Genomic_DNA.
DR RefSeq; WP_011577384.1; NC_008229.1.
DR AlphaFoldDB; Q17YK6; -.
DR SMR; Q17YK6; -.
DR STRING; 382638.Hac_0439; -.
DR EnsemblBacteria; CAJ99270; CAJ99270; Hac_0439.
DR KEGG; hac:Hac_0439; -.
DR eggNOG; COG0837; Bacteria.
DR HOGENOM; CLU_042582_1_0_7; -.
DR OMA; NNHWRLS; -.
DR OrthoDB; 992687at2; -.
DR BioCyc; HACI382638:HAC_RS02000-MON; -.
DR Proteomes; UP000000775; 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 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..336
FT /note="Glucokinase"
FT /id="PRO_1000050969"
FT BINDING 12..17
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00524"
SQ SEQUENCE 336 AA; 36737 MW; B356F4AE0AA8DF75 CRC64;
MPKTETYPRL LADIGGTNAR FGLEVASRQI ECIEVLRCED FESLSDAVRF YLSKHQESLK
LCPIYGSFAV ATPIMGDFVQ MTNNHWTFSI ETTRQCLGLE RLLVVNDFVA QAFAISTMQE
NDLAQVGGIK CEINAPKAVL GPGTGLGVST LIQNSDGSLK VLPGEGGHVS FAPFDDLEIL
VWQYARSKFN HVSAERFLSG SGLVLIYEAL SKRKSMEKVA KLSKAELTPQ IISERALNGD
YPLCRLTLDT FCSMLGTLAA DVALTLGARG GVYLCGGIIP RFIDYFKTSP FRARFETKGR
MGAFLASIPV HVVLKKTPGL DGVGIALENY LLHDKI