ID A0A1I5EXE1_9BRAD Unreviewed; 339 AA.
AC A0A1I5EXE1;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 24.
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 ORFNames=SAMN05216330_10234 {ECO:0000313|EMBL:SFO16185.1};
OS Bradyrhizobium sp. Ghvi.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Nitrobacteraceae; Bradyrhizobium.
OX NCBI_TaxID=1855319 {ECO:0000313|EMBL:SFO16185.1, ECO:0000313|Proteomes:UP000198509};
RN [1] {ECO:0000313|EMBL:SFO16185.1, ECO:0000313|Proteomes:UP000198509}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ghvi {ECO:0000313|EMBL:SFO16185.1,
RC ECO:0000313|Proteomes:UP000198509};
RA de Groot N.N.;
RL Submitted (OCT-2016) 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}.
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DR EMBL; FOVU01000002; SFO16185.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I5EXE1; -.
DR STRING; 1855319.SAMN05216330_10234; -.
DR Proteomes; UP000198509; 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 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:SFO16185.1};
KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00524};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_00524}.
FT BINDING 29..34
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00524"
SQ SEQUENCE 339 AA; 35936 MW; 86A6D525AAA347C4 CRC64;
MEEEGSRSLQ GNGSQMDMSI GKTGNILLAD IGGTNARFAL SNGEQIGTID YVKVADHPTV
REAIADVLRR ANSEKPIRAV LAVAGPVTNN RCVMTNSPWV IDGNELQPAL GFDSVHVLND
FEVVAWSLPA LQPADLIPLG GQDGMPGEPL LVVGPGTGFG VSCLVERHGS RLAVVTEAGH
ATLPAENERE ERVIASMRRR FGHVSIERGA LSGSGLQSLY EALAEVDEAQ VPQRDAAGIT
KAALEGTCEV SRATLEMFCA ILGSVAGNLA VTFGARGGAY IAGGIVPRFP EFLAASAFRA
RFEAKGRFQD YLRNIPTRLV VKPDASFVGL KMFADHIAD
//
