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Information on EC 2.7.1.2 - glucokinase and Organism(s) Bacillus subtilis and UniProt Accession P54495

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IUBMB Comments
A group of enzymes found in invertebrates and microorganisms that are highly specific for glucose.
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Bacillus subtilis
UNIPROT: P54495
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The taxonomic range for the selected organisms is: Bacillus subtilis
The expected taxonomic range for this enzyme is: Bacteria, Archaea, Eukaryota
Synonyms
glucokinase, atp-dependent glucokinase, tcglck, atp-glk, sgglka, tte0090, klglk1, sw2155, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
glucokinase (phosphorylating)
-
-
-
-
kinase, gluco- (phosphorylating)
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-
-
-
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
ATP + D-glucose = ADP + D-glucose 6-phosphate
show the reaction diagram
the enzyme activity requires 3 cysteine residues C175, C177, and C182 within the motif CXCGX(2)GCXE that discriminates microbial glucokinases into two lineages
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
phospho group transfer
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-
-
-
SYSTEMATIC NAME
IUBMB Comments
ATP:D-glucose 6-phosphotransferase
A group of enzymes found in invertebrates and microorganisms that are highly specific for glucose.
CAS REGISTRY NUMBER
COMMENTARY hide
9001-36-9
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
ATP + D-glucose
ADP + D-glucose 6-phosphate
show the reaction diagram
-
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
ATP + D-glucose
ADP + D-glucose 6-phosphate
show the reaction diagram
-
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
ATP
dependent on
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
SwissProt
Manually annotated by BRENDA team
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
35000
recombinant enzyme, oxidative conditions, PAGE, the wild-type and mutant enzymes occur as both monomer and homodimer
35200
recombinant enzyme, about, mass spectrometry, 2 peaks
70000
recombinant enzyme, oxidative conditions, PAGE, the wild-type and mutant enzymes occur as both monomer and homodimer
70400
recombinant enzyme, about, mass spectrometry, 2 peaks
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dimer
2 * 35200, about, mass spectrometry, 2 * 35000, recombinant enzyme, PAGE under oxidative conditions or SDS-PAGE in absence of reductants, the wild-type and mutant enzymes occur as both monomer and homodimer
monomer
1 * 35200, about, mass spectrometry, 1 * 35000, recombinant enzyme, PAGE under reducing conditions or SDS-PAGE in absence of reductants, the wild-type and mutant enzymes occur as both monomer and homodimer
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
C166A
site-directed mutagenesis, mutant shows activity similar to the wild-type enzyme
C175A
site-directed mutagenesis, inactive active site residue mutant
C177A
site-directed mutagenesis, inactive active site residue mutant
C182A
site-directed mutagenesis, inactive active site residue mutant
C282A
site-directed mutagenesis, mutant shows slightly increased enzyme activity compared to the wild-type enzyme, conformational changes different from the wild-type enzyme, overview
C321A
site-directed mutagenesis, mutant shows 5fold increased enzyme activity compared to the wild-type enzyme, conformational changes different from the wild-type enzyme, overview
D10K
site-directed mutagenesis, ATP binding site mutant, inactive mutant
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant His-tagged wild-type and mutant enzymes from Escherichia coli strain RB791 by nickel affinity chromatography
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
gene glcK, phylogenetic analysis and tree, functional complementation of enzyme-deficient Escherichia coli strain UE26, overexpression of His-tagged wild-type and mutant enzymes in Escherichia coli strain RB791 as soluble proteins
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Mesak, L.R.; Mesak, F.M.; Dahl, M.K.
Bacillus subtilis GlcK activity requires cysteines within a motif that discriminates microbial glucokinases into two lineages
BMC Microbiol.
4
6-13
2004
Bacillus subtilis (P54495), Bacillus subtilis
Manually annotated by BRENDA team