GLK_HELP2
ID GLK_HELP2 Reviewed; 336 AA.
AC B6JMU2;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 16-DEC-2008, sequence version 1.
DT 03-AUG-2022, entry version 58.
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=HPP12_1068;
OS Helicobacter pylori (strain P12).
OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC Helicobacteraceae; Helicobacter.
OX NCBI_TaxID=570508;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=P12;
RA Fischer W., Windhager L., Karnholz A., Zeiller M., Zimmer R., Haas R.;
RT "The complete genome sequence of Helicobacter pylori strain P12.";
RL Submitted (OCT-2008) to the EMBL/GenBank/DDBJ databases.
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; CP001217; ACJ08220.1; -; Genomic_DNA.
DR RefSeq; WP_001126889.1; NC_011498.1.
DR AlphaFoldDB; B6JMU2; -.
DR SMR; B6JMU2; -.
DR EnsemblBacteria; ACJ08220; ACJ08220; HPP12_1068.
DR KEGG; hpp:HPP12_1068; -.
DR HOGENOM; CLU_042582_1_0_7; -.
DR OMA; NNHWRLS; -.
DR OrthoDB; 992687at2; -.
DR Proteomes; UP000008198; 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_1000127709"
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; 36732 MW; EE941BE7411A51A8 CRC64;
MPKTETYPRL LADIGGTNAR FGLEVAPRQI ECIEVLRCED FESLSDAVRF YLSKCKESLK
LHPIYGSFAV ATPIMGDFVQ MTNNHWTFSI ETTRQCLTLK KLLVINDFVA QAYAISAMQE
NDLAQIGGIK CEINAPKAIL GPGTGLGVST LIQNSDGSLK VLPGEGGHVS FAPFDDLEIL
VWQYARSKFN HVSAERFLSG SGLVLIYEAL SKRKGLEKVA KLSKAELTPQ IISERALNGD
YPICRLTLDT FCSMLGTLAA DVALTLGARG GVYLCGGIIP RFIDYFKTSP FRARFETKGR
MGAFLASIPV HVVMKKTPGL DGAGIALENY LLHDKI