ID J0K381_HELPX Unreviewed; 336 AA.
AC J0K381;
DT 03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 03-OCT-2012, sequence version 1.
DT 24-JAN-2024, entry version 37.
DE RecName: Full=Glucokinase {ECO:0000256|HAMAP-Rule:MF_00524};
DE EC=2.7.1.2 {ECO:0000256|HAMAP-Rule:MF_00524};
DE AltName: Full=Glucose kinase {ECO:0000256|HAMAP-Rule:MF_00524};
GN Name=glk {ECO:0000256|HAMAP-Rule:MF_00524,
GN ECO:0000313|EMBL:EJB44955.1};
GN ORFNames=HPHPA9_0382 {ECO:0000313|EMBL:EJB44955.1};
OS Helicobacter pylori Hp A-9.
OC Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales;
OC Helicobacteraceae; Helicobacter.
OX NCBI_TaxID=992034 {ECO:0000313|EMBL:EJB44955.1, ECO:0000313|Proteomes:UP000005483};
RN [1] {ECO:0000313|EMBL:EJB44955.1, ECO:0000313|Proteomes:UP000005483}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Hp A-9 {ECO:0000313|EMBL:EJB44955.1,
RC ECO:0000313|Proteomes:UP000005483};
RA Blanchard T.G., Czinn S.J., McCracken C., Abolude K., Maroo A.,
RA Santana-Cruz I., Tallon L.J., Ficke F.W.F.;
RT "Genome sequence of Helicobacter pylori Hp A-9.";
RL Submitted (APR-2012) 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:0000256|HAMAP-Rule:MF_00524};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00524}.
CC -!- SIMILARITY: Belongs to the bacterial glucokinase family.
CC {ECO:0000256|HAMAP-Rule:MF_00524, ECO:0000256|RuleBase:RU004046}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EJB44955.1}.
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DR EMBL; AKOC01000004; EJB44955.1; -; Genomic_DNA.
DR RefSeq; WP_001126887.1; NZ_AKOC01000004.1.
DR AlphaFoldDB; J0K381; -.
DR PATRIC; fig|992034.3.peg.366; -.
DR Proteomes; UP000005483; Unassembled WGS sequence.
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 CDD; cd00012; NBD_sugar-kinase_HSP70_actin; 1.
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 {ECO:0000256|HAMAP-Rule:MF_00524};
KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00524};
KW Glycolysis {ECO:0000256|HAMAP-Rule:MF_00524};
KW Kinase {ECO:0000256|HAMAP-Rule:MF_00524, ECO:0000313|EMBL:EJB44955.1};
KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00524};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_00524}.
FT BINDING 12..17
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00524"
SQ SEQUENCE 336 AA; 36714 MW; AF941BE7411A5073 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 HVVLKKTPGL DGAGIALENY LLHDKI
//
