GLK_ECOLI
ID GLK_ECOLI Reviewed; 321 AA.
AC P0A6V8; P46880; P78276;
DT 29-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 29-MAR-2005, sequence version 1.
DT 03-AUG-2022, entry version 125.
DE RecName: Full=Glucokinase {ECO:0000303|PubMed:9023215};
DE EC=2.7.1.2 {ECO:0000269|PubMed:9023215};
DE AltName: Full=Glucose kinase;
GN Name=glk {ECO:0000303|PubMed:9023215}; OrderedLocusNames=b2388, JW2385;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY,
RP BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR LOCATION, INDUCTION, AND
RP DISRUPTION PHENOTYPE.
RC STRAIN=K12 / MC4100 / ATCC 35695 / DSM 6574;
RX PubMed=9023215; DOI=10.1128/jb.179.4.1298-1306.1997;
RA Meyer D., Schneider-Fresenius C., Horlacher R., Peist R., Boos W.W.;
RT "Molecular characterization of glucokinase from Escherichia coli K-12.";
RL J. Bacteriol. 179:1298-1306(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=9205837; DOI=10.1093/dnares/4.2.91;
RA Yamamoto Y., Aiba H., Baba T., Hayashi K., Inada T., Isono K., Itoh T.,
RA Kimura S., Kitagawa M., Makino K., Miki T., Mitsuhashi N., Mizobuchi K.,
RA Mori H., Nakade S., Nakamura Y., Nashimoto H., Oshima T., Oyama S.,
RA Saito N., Sampei G., Satoh Y., Sivasundaram S., Tagami H., Takahashi H.,
RA Takeda J., Takemoto K., Uehara K., Wada C., Yamagata S., Horiuchi T.;
RT "Construction of a contiguous 874-kb sequence of the Escherichia coli-K12
RT genome corresponding to 50.0-68.8 min on the linkage map and analysis of
RT its sequence features.";
RL DNA Res. 4:91-113(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
CC -!- FUNCTION: An ATP-dependent kinase that phosphorylates glucose to make
CC glucose-6-phosphate, not active on fructose, galactose or mannose. Not
CC highly important in wild-type E.coli as glucose is transported into the
CC cell by the PTS system as glucose 6-phosphate.
CC {ECO:0000269|PubMed:9023215}.
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:0000269|PubMed:9023215};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:17826;
CC Evidence={ECO:0000269|PubMed:9023215};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.78 mM for glucose {ECO:0000269|PubMed:9023215};
CC KM=3.76 mM for ATP {ECO:0000269|PubMed:9023215};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:9023215}.
CC -!- INDUCTION: Constitutively expressed, weakly repressed by growth on
CC glucose, repression may be partially controlled by cra (fruR).
CC {ECO:0000269|PubMed:9023215}.
CC -!- DISRUPTION PHENOTYPE: No glucokinase activity, no growth phenotype in
CC an otherwise wild-type cell. {ECO:0000269|PubMed:9023215}.
CC -!- SIMILARITY: Belongs to the bacterial glucokinase family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; U22490; AAA64506.1; -; Genomic_DNA.
DR EMBL; U00096; AAC75447.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA16258.1; -; Genomic_DNA.
DR PIR; A65013; A65013.
DR RefSeq; NP_416889.1; NC_000913.3.
DR RefSeq; WP_000170346.1; NZ_LN832404.1.
DR AlphaFoldDB; P0A6V8; -.
DR SMR; P0A6V8; -.
DR BioGRID; 4260563; 10.
DR IntAct; P0A6V8; 5.
DR STRING; 511145.b2388; -.
DR DrugBank; DB02379; Beta-D-Glucose.
DR jPOST; P0A6V8; -.
DR PaxDb; P0A6V8; -.
DR PRIDE; P0A6V8; -.
DR EnsemblBacteria; AAC75447; AAC75447; b2388.
DR EnsemblBacteria; BAA16258; BAA16258; BAA16258.
DR GeneID; 946858; -.
DR KEGG; ecj:JW2385; -.
DR KEGG; eco:b2388; -.
DR PATRIC; fig|1411691.4.peg.4340; -.
DR EchoBASE; EB2791; -.
DR eggNOG; COG0837; Bacteria.
DR HOGENOM; CLU_042582_1_0_6; -.
DR InParanoid; P0A6V8; -.
DR OMA; NNHWRLS; -.
DR PhylomeDB; P0A6V8; -.
DR BioCyc; EcoCyc:GLUCOKIN-MON; -.
DR BioCyc; MetaCyc:GLUCOKIN-MON; -.
DR SABIO-RK; P0A6V8; -.
DR PRO; PR:P0A6V8; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005829; C:cytosol; IDA:EcoCyc.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004340; F:glucokinase activity; IDA:EcoCyc.
DR GO; GO:0005536; F:glucose binding; IEA:InterPro.
DR GO; GO:0006096; P:glycolytic process; IBA:GO_Central.
DR HAMAP; MF_00524; Glucokinase; 1.
DR InterPro; IPR043129; ATPase_NBD.
DR InterPro; IPR003836; Glucokinase.
DR Pfam; PF02685; Glucokinase; 1.
DR SUPFAM; SSF53067; SSF53067; 1.
DR TIGRFAMs; TIGR00749; glk; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Cytoplasm; Glycolysis; Kinase; Nucleotide-binding;
KW Reference proteome; Transferase.
FT CHAIN 1..321
FT /note="Glucokinase"
FT /id="PRO_0000215124"
FT BINDING 8..13
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT CONFLICT 108
FT /note="I -> N (in Ref. 1; AAA64506)"
FT /evidence="ECO:0000305"
FT CONFLICT 188..189
FT /note="RV -> AC (in Ref. 1; AAA64506)"
FT /evidence="ECO:0000305"
FT CONFLICT 274
FT /note="A -> G (in Ref. 1; AAA64506)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 321 AA; 34723 MW; 2D6CD956641A3823 CRC64;
MTKYALVGDV GGTNARLALC DIASGEISQA KTYSGLDYPS LEAVIRVYLE EHKVEVKDGC
IAIACPITGD WVAMTNHTWA FSIAEMKKNL GFSHLEIIND FTAVSMAIPM LKKEHLIQFG
GAEPVEGKPI AVYGAGTGLG VAHLVHVDKR WVSLPGEGGH VDFAPNSEEE AIILEILRAE
IGHVSAERVL SGPGLVNLYR AIVKADNRLP ENLKPKDITE RALADSCTDC RRALSLFCVI
MGRFGGNLAL NLGTFGGVFI AGGIVPRFLE FFKASGFRAA FEDKGRFKEY VHDIPVYLIV
HDNPGLLGSG AHLRQTLGHI L
