ID   GLK_STRCO               Reviewed;         317 AA.
AC   P0A4E1; P40184;
DT   15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   15-MAR-2005, sequence version 1.
DT   03-AUG-2022, entry version 81.
DE   RecName: Full=Glucokinase;
DE            EC=2.7.1.2 {ECO:0000305|PubMed:1435260};
DE   AltName: Full=Glucose kinase {ECO:0000303|PubMed:1435260};
DE   AltName: Full=ORF 3 {ECO:0000303|PubMed:1435260};
GN   Name=glkA; Synonyms=glk {ECO:0000303|PubMed:1435260};
GN   OrderedLocusNames=SCO2126; ORFNames=SC6E10.20c;
OS   Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145).
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Streptomyces; Streptomyces albidoflavus group.
OX   NCBI_TaxID=100226;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, POSSIBLE SUBUNIT, AND
RP   INDUCTION.
RC   STRAIN=A3(2) / NRRL B-16638;
RX   PubMed=1435260; DOI=10.1111/j.1365-2958.1992.tb01463.x;
RA   Angell S., Schwarz E., Bibb M.J.;
RT   "The glucose kinase gene of Streptomyces coelicolor A3(2): its nucleotide
RT   sequence, transcriptional analysis and role in glucose repression.";
RL   Mol. Microbiol. 6:2833-2844(1992).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-471 / A3(2) / M145;
RX   PubMed=12000953; DOI=10.1038/417141a;
RA   Bentley S.D., Chater K.F., Cerdeno-Tarraga A.-M., Challis G.L.,
RA   Thomson N.R., James K.D., Harris D.E., Quail M.A., Kieser H., Harper D.,
RA   Bateman A., Brown S., Chandra G., Chen C.W., Collins M., Cronin A.,
RA   Fraser A., Goble A., Hidalgo J., Hornsby T., Howarth S., Huang C.-H.,
RA   Kieser T., Larke L., Murphy L.D., Oliver K., O'Neil S., Rabbinowitsch E.,
RA   Rajandream M.A., Rutherford K.M., Rutter S., Seeger K., Saunders D.,
RA   Sharp S., Squares R., Squares S., Taylor K., Warren T., Wietzorrek A.,
RA   Woodward J.R., Barrell B.G., Parkhill J., Hopwood D.A.;
RT   "Complete genome sequence of the model actinomycete Streptomyces coelicolor
RT   A3(2).";
RL   Nature 417:141-147(2002).
CC   -!- FUNCTION: A probable glucose kinase (Probable). Required for glucose
CC       repression of many different genes, restores glucose kinase activity in
CC       E.coli glk mutants (PubMed:1435260). {ECO:0000269|PubMed:1435260,
CC       ECO:0000305|PubMed:1435260}.
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:0000305|PubMed:1435260};
CC   -!- SUBUNIT: Homooligomer (possibly a homotetramer). Alternatively, it may
CC       form a heterotetramer of two glucokinase subunits with two ORF2 (AC
CC       P40182) proteins. {ECO:0000305|PubMed:1435260}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P0A6V8}.
CC   -!- INDUCTION: Transcribed from its own promoter, as well as another
CC       upstream of the preceeding gene (AC P40182). Expressed when grown on
CC       glucose or galactose, levels decrease as cells enter stationary phase.
CC       {ECO:0000269|PubMed:1435260}.
CC   -!- SIMILARITY: Belongs to the ROK (NagC/XylR) family. {ECO:0000305}.
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DR   EMBL; X65932; CAA46727.1; -; Genomic_DNA.
DR   EMBL; AL939111; CAB51974.1; -; Genomic_DNA.
DR   PIR; S26208; S26208.
DR   RefSeq; NP_626383.1; NC_003888.3.
DR   RefSeq; WP_003976689.1; NZ_VNID01000001.1.
DR   AlphaFoldDB; P0A4E1; -.
DR   SMR; P0A4E1; -.
DR   STRING; 100226.SCO2126; -.
DR   GeneID; 1097560; -.
DR   KEGG; sco:SCO2126; -.
DR   PATRIC; fig|100226.15.peg.2161; -.
DR   eggNOG; COG1940; Bacteria.
DR   HOGENOM; CLU_036604_0_0_11; -.
DR   InParanoid; P0A4E1; -.
DR   OMA; APNIDWR; -.
DR   PhylomeDB; P0A4E1; -.
DR   BRENDA; 2.7.1.2; 5998.
DR   Proteomes; UP000001973; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004340; F:glucokinase activity; IMP:CACAO.
DR   GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-KW.
DR   InterPro; IPR043129; ATPase_NBD.
DR   InterPro; IPR000600; ROK.
DR   InterPro; IPR004654; ROK_glcA.
DR   PANTHER; PTHR18964; PTHR18964; 1.
DR   Pfam; PF00480; ROK; 1.
DR   SUPFAM; SSF53067; SSF53067; 1.
DR   TIGRFAMs; TIGR00744; ROK_glcA_fam; 1.
DR   PROSITE; PS01125; ROK; 1.
PE   1: Evidence at protein level;
KW   ATP-binding; Cytoplasm; Glycolysis; Kinase; Nucleotide-binding;
KW   Reference proteome; Repressor; Transferase.
FT   CHAIN           1..317
FT                   /note="Glucokinase"
FT                   /id="PRO_0000095677"
FT   BINDING         6..12
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   317 AA;  33062 MW;  6E65A97691BA15BF CRC64;
     MGLTIGVDIG GTKIAAGVVD EEGNILSTHK VPTPTTPEAI VDAIASAVEG ARVGHEIVAV
     GIGAAGYVNR QRSTVYFAPN IDWRQEPLKE KVEARVGLPV VVENDANAAA WGEYKFGGGK
     GHRNVICITL GTGLGGGIII GNKLRRGHFG VAAEFGHIRM VPDGLLCGCG SQGCWEQYAS
     GRALVRYAKQ RANATPERAE VLLALGDGTP DGIEGKHISV AARQGCPVAV DSYRELARWA
     GAGLADLASL FDPSAFIVGG GLSDEGDLVL DPIRKSYKRW LVGGNWRPVA DVIAAQLGNK
     AGLVGAADLA REPDPIM