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Database: UniProt
Entry: I4FVW9_MICAE
LinkDB: I4FVW9_MICAE
Original site: I4FVW9_MICAE 
ID   I4FVW9_MICAE            Unreviewed;       348 AA.
AC   I4FVW9;
DT   05-SEP-2012, integrated into UniProtKB/TrEMBL.
DT   05-SEP-2012, sequence version 1.
DT   24-JAN-2024, entry version 43.
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:CCH99794.1};
GN   ORFNames=MICAB_6780009 {ECO:0000313|EMBL:CCH99794.1};
OS   Microcystis aeruginosa PCC 9717.
OC   Bacteria; Cyanobacteriota; Cyanophyceae; Oscillatoriophycideae;
OC   Chroococcales; Microcystaceae; Microcystis.
OX   NCBI_TaxID=1160286 {ECO:0000313|EMBL:CCH99794.1, ECO:0000313|Proteomes:UP000003172};
RN   [1] {ECO:0000313|EMBL:CCH99794.1, ECO:0000313|Proteomes:UP000003172}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=9717 {ECO:0000313|EMBL:CCH99794.1,
RC   ECO:0000313|Proteomes:UP000003172};
RA   Genoscope - CEA;
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:CCH99794.1}.
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DR   EMBL; CAII01000643; CCH99794.1; -; Genomic_DNA.
DR   RefSeq; WP_004266785.1; NZ_HE972764.1.
DR   AlphaFoldDB; I4FVW9; -.
DR   HOGENOM; CLU_042582_0_0_3; -.
DR   Proteomes; UP000003172; 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; 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:CCH99794.1};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00524};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_00524, ECO:0000313|EMBL:CCH99794.1}.
FT   BINDING         7..12
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00524"
SQ   SEQUENCE   348 AA;  37700 MW;  AFF0B405C73DBD31 CRC64;
     MTILLGGDIG GTKTILRLVD CQNSSDSPQP RLITLDQEIY PSEQYPDLVP IVRQFLARQT
     TIPPVAKACF GIAGPVVNNS SELTNLSWSL TGDRLSQELQ IERVKLINDF AAIGYGVLGL
     APEELHNLQS APAVPEAPIA VIGAGTGLGE GFLIPVSKGK YQVFASEGSH ADFAPRSSLE
     YQLLNYLLEL YNIERISVER VVSGPGITSI YRFLHDSNYS QSSPAMAEIY RAWLEEMGKP
     QKTVDLAAKI ASFAQDNSDH LCYQTMKIFV EAYGAEAGNL ALKLLPYGGL YIAGGIAAKN
     LPLMTEGSFM KAFRAKGRMT EILSNIPVHI VLNTQVGLMG AVYCASQL
//
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