ID A0A1Z4RSC3_9CHRO Unreviewed; 343 AA.
AC A0A1Z4RSC3;
DT 27-SEP-2017, integrated into UniProtKB/TrEMBL.
DT 27-SEP-2017, sequence version 1.
DT 24-JAN-2024, entry version 23.
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=NIES4102_23860 {ECO:0000313|EMBL:BAZ45365.1};
OS Chondrocystis sp. NIES-4102.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Oscillatoriophycideae;
OC Chroococcales; Chroococcaceae; Chondrocystis.
OX NCBI_TaxID=2005460 {ECO:0000313|EMBL:BAZ45365.1, ECO:0000313|Proteomes:UP000217698};
RN [1] {ECO:0000313|EMBL:BAZ45365.1, ECO:0000313|Proteomes:UP000217698}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NIES-4102 {ECO:0000313|EMBL:BAZ45365.1,
RC ECO:0000313|Proteomes:UP000217698};
RA Hirose Y., Shimura Y., Fujisawa T., Nakamura Y., Kawachi M.;
RT "Genome sequencing of cyanobaciteial culture collection at National
RT Institute for Environmental Studies (NIES).";
RL Submitted (JUN-2017) 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; AP018281; BAZ45365.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Z4RSC3; -.
DR KEGG; chon:NIES4102_23860; -.
DR OrthoDB; 9800595at2; -.
DR Proteomes; UP000217698; 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 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; PTHR47363; GLUCOKINASE; 1.
DR PANTHER; PTHR47363: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:BAZ45365.1};
KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00524};
KW Reference proteome {ECO:0000313|Proteomes:UP000217698};
KW Transferase {ECO:0000256|HAMAP-Rule:MF_00524}.
FT BINDING 6..11
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00524"
SQ SEQUENCE 343 AA; 37491 MW; 691DDE94DA48093F CRC64;
MFLLAGDIGG TKTILRLVEV TEVTLTEKSF RTVKEAQYIS ANFPDLVPIV KEFLGEDKKL
QPEITCLAIA GPVINNTCTL TNLKWVLDSQ RLEMELDIPK VSLINDFAAN SFGILGLKDV
DIHTLQVGEA RKKAPIAVIG AGTGLGEAFL IPQGNKYQIF ASEGGHADFA PRNDLETELL
KYLRHKLKVE HISVERVVSG QGIPSIYQFL RDSNFASESS EIAEKITAWE QETNKTIDPA
AIISQAAFKQ SDRLCEKTME IFIEAYGAET GNLALKLLSY GGIYIAGGIA AKILPLMQDG
RFLNTFKDKG RVSSLITAIP VHIVLNPQVG LVGSVLYGLQ NQD
//
