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Information on EC 2.7.7.74 - 1L-myo-inositol 1-phosphate cytidylyltransferase and Organism(s) Archaeoglobus fulgidus and UniProt Accession O29976

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IUBMB Comments
In many organisms this activity is catalysed by a bifunctional enzyme. The cytidylyltransferase domain of the bifunctional EC 2.7.7.74/EC 2.7.8.34 (CTP:inositol-1-phosphate cytidylyltransferase/CDP-inositol:inositol-1-phosphate transferase) is absolutely specific for CTP and 1L-myo-inositol 1-phosphate. The enzyme is involved in biosynthesis of bis(1L-myo-inositol) 1,3'-phosphate, a widespread organic solute in microorganisms adapted to hot environments.
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Archaeoglobus fulgidus
UNIPROT: O29976
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The taxonomic range for the selected organisms is: Archaeoglobus fulgidus
The expected taxonomic range for this enzyme is: Bacteria, Archaea, Eukaryota
Synonyms
ctp:inositol-1-phosphate cytidylyltransferase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
CTP:inositol-1-phosphate cytidylyltransferase
PATHWAY SOURCE
PATHWAYS
-
-
SYSTEMATIC NAME
IUBMB Comments
CTP:1L-myo-inositol 1-phosphate cytidylyltransferase
In many organisms this activity is catalysed by a bifunctional enzyme. The cytidylyltransferase domain of the bifunctional EC 2.7.7.74/EC 2.7.8.34 (CTP:inositol-1-phosphate cytidylyltransferase/CDP-inositol:inositol-1-phosphate transferase) is absolutely specific for CTP and 1L-myo-inositol 1-phosphate. The enzyme is involved in biosynthesis of bis(1L-myo-inositol) 1,3'-phosphate, a widespread organic solute in microorganisms adapted to hot environments.
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
CDP-glycerol + 1L-myo-inositol 1-phosphate
CMP + 1-(1X-glyceryl) myo-inosityl phosphate 3-phosphate
show the reaction diagram
-
-
-
?
CTP + 1D-myo-inositol 3-phosphate
diphosphate + CDP-L-myo-inositol
show the reaction diagram
CTP + 1L-myo-inositol 1-phosphate
diphosphate + CDP-1L-myo-inositol
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
CTP + 1D-myo-inositol 3-phosphate
diphosphate + CDP-L-myo-inositol
show the reaction diagram
the enzyme is involved in the synthesis of di-myo-inositol phosphate. Archaeoglobus fulgidus accumulates di-myo-inositol phosphate and diglycerol phosphate in response to heat and osmotic stresses, respectively, and the level of glycero-phospho-myo-inositol increases primarily when the two stresses are combined
-
-
?
CTP + 1L-myo-inositol 1-phosphate
diphosphate + CDP-1L-myo-inositol
show the reaction diagram
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.87
1D-myo-inositol 3-phosphate
pH and temperature not specified in the publication
0.87
1L-myo-inositol 1-phosphate
90°C, pH 7.0, cytoplasmic CTP:inositol-1-phosphate cytidylyltransferase domain of the bifunctional enzyme (EC 2.7.7.74/EC 2.7.8.34)
0.58
CTP
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
62.9
90°C, pH 7.0, cytoplasmic CTP:inositol-1-phosphate cytidylyltransferase domain of the bifunctional enzyme (EC 2.7.7.74/EC 2.7.8.34)
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.5 - 8.5
pH 5.5: about 30% of maximal activity, pH 8.5: about 65% of maximal activity
6.5 - 7.5
maximal activity
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
60 - 100
activity of the enzyme is undetectable at temperatures below 60°C, and maximal activity is reached between 90 and 95°C, at 100°C about 25% of maximal activity
90 - 95
maximal activity
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
crystal structure of the enzyme in the apo form is solved to a 1.9 A resolution. The structure of IPCT is composed of a central seven-stranded mixed beta-sheet, of which six beta-strands are parallel, surrounded by six alpha-helices, a fold reminiscent of the dinucleotide-binding Rossmann fold
crystallization of the CTP:inositol-1-phosphate cytidylyltransferase domain in the apo form. The crystals diffracted to 2.4 A resolution using a synchrotron source and belong to the orthorhombic space group P2(1)2(1)2, with unit-cell parameters a = 154.7, b = 83.9, c = 127.7 A
hanging-drop vapor diffusion method at 20°C, X-ray structure of the cytoplasmic CTP:inositol-1-phosphate cytidylyltransferase domain of the bifunctional enzyme (EC 2.7.7.74/EC 2.7.8.34). The structure of the enzyme in the apo form was solved to a 1.9 A resolution. The structure of CTP:inositol-1-phosphate cytidylyltransferase is composed of a central seven-stranded mixed beta-sheet, of which six beta-strands are parallel, surrounded by six alpha-helices, a fold reminiscent of the dinucleotide-binding Rossmann fold
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
purification CTP:inositol-1-phosphate cytidylyltransferase domain
the cytoplasmic domain of the bifunctional enzyme (EC 2.7.7.74/EC 2.7.8.34) is produced in Escherichia coli
using metal affinity chromatography and gel filtration
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
cytoplasmic domain of IPCT is expressed in Escherichia coli as a His-tagged fusion protein
expression in Escherichia coli
the CTP:inositol-1-phosphate cytidylyltransferase domain of the bifunctional CTP:inositol-1-phosphate cytidylyltransferase/CDP-inositol:inositol-1-phosphate transferase (EC 2.7.7.74/EC 2.7.8.34) is cloned and expressed in Escherichia coli
the cytoplasmic domain of the bifunctional enzyme (EC 2.7.7.74/EC 2.7.8.34) is produced in Escherichia coli
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Borges, N.; Goncalves, L.G.; Rodrigues, M.V.; Siopa, F.; Ventura, R.; Maycock, C.; Lamosa, P.; Santos, H.
Biosynthetic pathways of inositol and glycerol phosphodiesters used by the hyperthermophile Archaeoglobus fulgidus in stress adaptation
J. Bacteriol.
188
8128-8135
2006
Archaeoglobus fulgidus (O29976)
Manually annotated by BRENDA team
Rodrigues, M.V.; Borges, N.; Henriques, M.; Lamosa, P.; Ventura, R.; Fernandes, C.; Empadinhas, N.; Maycock, C.; da Costa, M.S.; Santos, H.
Bifunctional CTP:inositol-1-phosphate cytidylyltransferase/CDP-inositol:inositol-1-phosphate transferase, the key enzyme for di-myo-inositol-phosphate synthesis in several (hyper)thermophiles
J. Bacteriol.
189
5405-5412
2007
Aquifex aeolicus (O67379), Archaeoglobus fulgidus (O29976), Pyrococcus furiosus (Q8U1Z6), Rubrobacter xylanophilus (Q1AWQ0), Thermococcus kodakarensis (Q5JDA9)
Manually annotated by BRENDA team
Brito, J.A.; Borges, N.; Santos, H.; Archer, M.
Production, crystallization and preliminary X-ray analysis of CTP:inositol-1-phosphate cytidylyltransferase from Archaeoglobus fulgidus
Acta Crystallogr. Sect. F
66
1463-1465
2010
Archaeoglobus fulgidus (O29976), Archaeoglobus fulgidus
Manually annotated by BRENDA team
Brito, J.A.; Borges, N.; Vonrhein, C.; Santos, H.; Archer, M.
Crystal structure of Archaeoglobus fulgidus CTP:inositol-1-phosphate cytidylyltransferase, a key enzyme for di-myo-inositol-phosphate synthesis in (hyper)thermophiles
J. Bacteriol.
193
2177-2185
2011
Archaeoglobus fulgidus (O29976), Archaeoglobus fulgidus
Manually annotated by BRENDA team