ID Q31RR6_SYNE7 Unreviewed; 345 AA.
AC Q31RR6;
DT 06-DEC-2005, integrated into UniProtKB/TrEMBL.
DT 06-DEC-2005, sequence version 1.
DT 27-MAR-2024, entry version 93.
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 OrderedLocusNames=Synpcc7942_0221 {ECO:0000313|EMBL:ABB56253.1};
OS Synechococcus elongatus (strain ATCC 33912 / PCC 7942 / FACHB-805)
OS (Anacystis nidulans R2).
OC Bacteria; Cyanobacteriota; Cyanophyceae; Synechococcales; Synechococcaceae;
OC Synechococcus.
OX NCBI_TaxID=1140 {ECO:0000313|EMBL:ABB56253.1, ECO:0000313|Proteomes:UP000889800};
RN [1] {ECO:0000313|Proteomes:UP000889800}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33912 / PCC 7942 / FACHB-805
RC {ECO:0000313|Proteomes:UP000889800};
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA Hammon N., Israni S., Pitluck S., Schmutz J., Larimer F., Land M.,
RA Kyrpides N., Lykidis A., Richardson P.;
RT "Complete sequence of chromosome 1 of Synechococcus elongatus PCC 7942.";
RL Submitted (AUG-2005) 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; CP000100; ABB56253.1; -; Genomic_DNA.
DR RefSeq; WP_011243603.1; NZ_JACJTX010000002.1.
DR AlphaFoldDB; Q31RR6; -.
DR STRING; 1140.Synpcc7942_0221; -.
DR PaxDb; 1140-Synpcc7942_0221; -.
DR GeneID; 76398968; -.
DR KEGG; syf:Synpcc7942_0221; -.
DR eggNOG; COG0837; Bacteria.
DR HOGENOM; CLU_042582_0_0_3; -.
DR OrthoDB; 9800595at2; -.
DR BioCyc; SYNEL:SYNPCC7942_0221-MONOMER; -.
DR Proteomes; UP000889800; 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 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};
KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00524};
KW Reference proteome {ECO:0000313|Proteomes:UP000889800};
KW Transferase {ECO:0000256|HAMAP-Rule:MF_00524, ECO:0000313|EMBL:ABB56253.1}.
FT BINDING 7..12
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00524"
SQ SEQUENCE 345 AA; 35707 MW; 3F8FFEEBBEBCB14D CRC64;
MTLLLAGDIG GTKTNLMLAI ASDCDRLEPL HQASFASAAY PDLVPMVQEF LAAAPSAEVR
SPVVACFGIA GPVVHGTAKL TNLPWQLSEA RLAKELGIAQ VALINDFAAI AYGLPGLTAE
DQVVVQVGEA DPAAPIAILG AGTGLGEGFI IPTAQGRQVF GSEGSHADFA PQTELESELL
HFLRNFYAIE HISVERVVSG QGIAAIYAFL RDRHPDQENP ALGAIASAWQ TGGDQAPDLA
AAVSQAALSD RDPLALQAMQ IFVSAYGAEA GNLALKLLSY GGVYVAGGIA GKILPLLTDG
TFLQAFQAKG RVKGLLTRMP ITIVTNHEVG LIGAGLRAAA IATQP
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