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Information on EC 6.3.4.2 - CTP synthase (glutamine hydrolysing) and Organism(s) Saccharolobus solfataricus and UniProt Accession Q980S6

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EC Tree
     6 Ligases
         6.3 Forming carbon-nitrogen bonds
             6.3.4 Other carbon-nitrogen ligases
                6.3.4.2 CTP synthase (glutamine hydrolysing)
IUBMB Comments
The enzyme contains three functionally distinct sites: an allosteric GTP-binding site, a glutaminase site where glutamine hydrolysis occurs (cf. EC 3.5.1.2, glutaminase), and the active site where CTP synthesis takes place. The reaction proceeds via phosphorylation of UTP by ATP to give an activated intermediate 4-phosphoryl UTP and ADP [4,5]. Ammonia then reacts with this intermediate generating CTP and a phosphate. The enzyme can also use ammonia from the surrounding solution [3,6].
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Saccharolobus solfataricus
UNIPROT: Q980S6
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The taxonomic range for the selected organisms is: Saccharolobus solfataricus
The enzyme appears in selected viruses and cellular organisms
Reaction Schemes
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ATP
+
UTP
+
L-glutamine
=
ADP
+
phosphate
+
CTP
+
L-glutamate
+
+
=
+
+
+
Synonyms
ctps, ctp synthetase, ctp synthase, ctps1, ctpsyn, ctps2, cytidine triphosphate synthetase, ctp synthetase 1, cytidine 5'-triphosphate synthase, ecctps, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
CTP synthetase
-
-
-
-
CTPS
-
-
-
-
cytidine 5'-triphosphate synthetase
-
-
-
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cytidine triphosphate synthetase
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-
-
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synthetase, cytidine triphosphate
-
-
-
-
uridine triphosphate aminase
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-
-
-
UTP-ammonia ligase
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-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
amination
-
-
-
-
PATHWAY SOURCE
PATHWAYS
-
-, -, -
SYSTEMATIC NAME
IUBMB Comments
UTP:ammonia ligase (ADP-forming)
The enzyme contains three functionally distinct sites: an allosteric GTP-binding site, a glutaminase site where glutamine hydrolysis occurs (cf. EC 3.5.1.2, glutaminase), and the active site where CTP synthesis takes place. The reaction proceeds via phosphorylation of UTP by ATP to give an activated intermediate 4-phosphoryl UTP and ADP [4,5]. Ammonia then reacts with this intermediate generating CTP and a phosphate. The enzyme can also use ammonia from the surrounding solution [3,6].
CAS REGISTRY NUMBER
COMMENTARY hide
9023-56-7
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dimer
crystallization data and sedimentation-ultracentrifugation experiments
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
dimeric form of CTP synthase at 2.5 A resolution. A comparison of the dimeric interface with the intermolecular interfaces in the tetrameric structures of Thermus thermophilus CTP synthase and Escherichia coli CTP synthase shows that the dimeric interfaces are almost identical in the three systems. Residues that are involved in the tetramerization of Sulfolobus solfataricus CTP synthase all have large thermal parameters in the dimeric form and undergo substantial movement upon tetramerization
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Lauritsen, I.; Willemoes, M.; Jensen, K.F.; Johansson, E.; Harris, P.
Structure of the dimeric form of CTP synthase from Sulfolobus solfataricus
Acta Crystallogr. Sect. F
67
201-208
2011
Saccharolobus solfataricus (Q980S6), Saccharolobus solfataricus
Manually annotated by BRENDA team