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Information on EC 2.7.7.103 - L-glutamine-phosphate cytidylyltransferase
for references in articles please use BRENDA:EC2.7.7.103
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EC Tree 2 Transferases
2.7 Transferring phosphorus-containing groups
2.7.7 Nucleotidyltransferases
2.7.7.103 L-glutamine-phosphate cytidylyltransferase
IUBMB Comments
The enzyme, characterized from the bacterium Campylobacter jejuni, is involved in formation of a unique O-methyl phosphoramidate modification on specific sugar residues within the bacterium’s capsular polysaccharides.
The expected taxonomic range for this enzyme is: Campylobacter jejuni subsp. jejuni
Reaction Schemes
showSynonyms
cj1416, ctp/phosphoglutamine cytididylyltransferase, more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
Cj1416
CTP/phosphoglutamine cytididylyltransferase
phosphoglutamine cytidylyltransferase
CTP/phosphoglutamine cytididylyltransferase
-
-
CTP/phosphoglutamine cytididylyltransferase
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-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
CTP + N5-phospho-L-glutamine = diphosphate + N5-(cytidine 5'-diphosphoramidyl)-L-glutamine
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SYSTEMATIC NAME
IUBMB Comments
CTP:phosphoglutamine cytidylyltransferase
The enzyme, characterized from the bacterium Campylobacter jejuni, is involved in formation of a unique O-methyl phosphoramidate modification on specific sugar residues within the bacterium's capsular polysaccharides.
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
CTP + 3'-phosphocytidine 5'-diphosphoramidate
diphosphate + 3'-phospho-5'-cytidine diphosphoramidate
CTP + 3-phospho-D-glycerate
diphosphate + 2-hydroxy-2-oxo-1,3,2lambda5-dioxaphospholane-4-carboxylic acid
CTP + 3-phospho-D-glycerate
diphosphate + CDP-3-D-glycerate
Substrates: -
Products: -
Products: -
?
CTP + arsenate
diphosphate + ?
Substrates: -
Products: -
Products: -
?
CTP + glycerol-1-phosphate
diphosphate + 2-hydroxy-4-(hydroxymethyl)-1,3,2lambda5-dioxaphospholan-2-one + CMP
Substrates: -
Products: -
Products: -
?
CTP + glycerol-1-phosphate
diphosphate + CDP-glycerol
Substrates: -
Products: -
Products: -
?
CTP + glycerol-2-phosphate
diphosphate + 2-hydroxy-4-(hydroxymethyl)-1,3,2lambda5-dioxaphospholan-2-one + CMP
Substrates: -
Products: -
Products: -
?
CTP + glycerol-2-phosphate
diphosphate + CDP-2-glycerol
Substrates: -
Products: -
Products: -
?
CTP + L-serine phosphate
diphosphate + CDP-L-serine
Substrates: -
Products: -
Products: -
?
CTP + methyl phosphate
diphosphate + O-methyl-CDP
Substrates: -
Products: -
Products: -
?
CTP + methyl phosphonate
diphosphate + CMP methyl phosphonate
Substrates: -
Products: -
Products: -
?
CTP + phosphate
diphosphate + CDP
Substrates: -
Products: -
Products: -
?
CTP + phosphoramidate
diphosphate + cytidine 5'-diphosphoramidate
Substrates: -
Products: -
Products: -
?
CTP + serinol phosphate
diphosphate + CDP-serinol
Substrates: -
Products: -
Products: -
?
CTP + 3'-phosphocytidine 5'-diphosphoramidate
diphosphate + 3'-phospho-5'-cytidine diphosphoramidate
Substrates: -
Products: -
Products: -
?
CTP + 3'-phosphocytidine 5'-diphosphoramidate
diphosphate + 3'-phospho-5'-cytidine diphosphoramidate
Substrates: -
Products: -
Products: -
?
CTP + 3'-phosphocytidine 5'-diphosphoramidate
diphosphate + 3'-phospho-5'-cytidine diphosphoramidate
Substrates: -
Products: -
Products: -
?
CTP + 3-phospho-D-glycerate
diphosphate + 2-hydroxy-2-oxo-1,3,2lambda5-dioxaphospholane-4-carboxylic acid
Substrates: -
Products: -
Products: -
?
CTP + 3-phospho-D-glycerate
diphosphate + 2-hydroxy-2-oxo-1,3,2lambda5-dioxaphospholane-4-carboxylic acid
Substrates: -
Products: -
Products: -
?
CTP + 3-phospho-D-glycerate
diphosphate + 2-hydroxy-2-oxo-1,3,2lambda5-dioxaphospholane-4-carboxylic acid
Substrates: -
Products: -
Products: -
?
CTP + ethanolamine phosphate
diphosphate + CDP-ethanolamine
Substrates: -
Products: -
Products: -
?
CTP + ethanolamine phosphate
diphosphate + CDP-ethanolamine
Substrates: -
Products: -
Products: -
?
CTP + ethanolamine phosphate
diphosphate + CDP-ethanolamine
Substrates: -
Products: -
Products: -
?
CTP + N5-phospho-L-glutamine
diphosphate + N5-(cytidine 5'-diphosphoramidyl)-L-glutamine
Substrates: -
Products: -
Products: -
?
CTP + N5-phospho-L-glutamine
diphosphate + N5-(cytidine 5'-diphosphoramidyl)-L-glutamine
Substrates: -
Products: -
Products: -
?
CTP + N5-phospho-L-glutamine
diphosphate + N5-(cytidine 5'-diphosphoramidyl)-L-glutamine
Substrates: -
Products: -
Products: -
?
CTP + N5-phospho-L-glutamine
diphosphate + N5-(cytidine 5'-diphosphoramidyl)-L-glutamine
Campylobacter jejuni subsp. jejuni serotype O:2
Substrates: -
Products: -
Products: -
?
CTP + N5-phospho-L-glutamine
diphosphate + N5-(cytidine 5'-diphosphoramidyl)-L-glutamine
Substrates: -
Products: -
Products: -
?
additional information
?
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Substrates: in the presence of MnCTP, Cj1416 can directly catalyze the formation of cytidine diphosphoramidate from phosphoramidate and MnCTP. In addition, it catalyzes the formation of 12 different reaction products using L-glutamine phosphate, phosphoramidate, methyl phosphate, methyl phosphonate, phosphate, arsenate, ethanolamine phosphate, glycerol-1-phosphate, glycerol-2-phosphate, serinol phosphate, L-serine phosphate, or 3-phospho-D-glycerate as the nucleophile to displace pyrophosphate from CTP. No activity is detected with MgATP as a substrate. Expansion in the substrate profile of Cj1416 when the reaction is catalyzed in the presence of MnCTP, substrate specificity of Cj1416, overview. NMR product analysis
Products: -
Products: -
-
additional information
?
-
Substrates: in the presence of MnCTP, Cj1416 can directly catalyze the formation of cytidine diphosphoramidate from phosphoramidate and MnCTP. In addition, it catalyzes the formation of 12 different reaction products using L-glutamine phosphate, phosphoramidate, methyl phosphate, methyl phosphonate, phosphate, arsenate, ethanolamine phosphate, glycerol-1-phosphate, glycerol-2-phosphate, serinol phosphate, L-serine phosphate, or 3-phospho-D-glycerate as the nucleophile to displace pyrophosphate from CTP. No activity is detected with MgATP as a substrate. Expansion in the substrate profile of Cj1416 when the reaction is catalyzed in the presence of MnCTP, substrate specificity of Cj1416, overview. NMR product analysis
Products: -
Products: -
-
additional information
?
-
Substrates: in the presence of MnCTP, Cj1416 can directly catalyze the formation of cytidine diphosphoramidate from phosphoramidate and MnCTP. In addition, it catalyzes the formation of 12 different reaction products using L-glutamine phosphate, phosphoramidate, methyl phosphate, methyl phosphonate, phosphate, arsenate, ethanolamine phosphate, glycerol-1-phosphate, glycerol-2-phosphate, serinol phosphate, L-serine phosphate, or 3-phospho-D-glycerate as the nucleophile to displace pyrophosphate from CTP. No activity is detected with MgATP as a substrate. Expansion in the substrate profile of Cj1416 when the reaction is catalyzed in the presence of MnCTP, substrate specificity of Cj1416, overview. NMR product analysis
Products: -
Products: -
-
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
CTP + N5-phospho-L-glutamine
diphosphate + N5-(cytidine 5'-diphosphoramidyl)-L-glutamine
Substrates: -
Products: -
Products: -
?
CTP + N5-phospho-L-glutamine
diphosphate + N5-(cytidine 5'-diphosphoramidyl)-L-glutamine
Substrates: -
Products: -
Products: -
?
CTP + N5-phospho-L-glutamine
diphosphate + N5-(cytidine 5'-diphosphoramidyl)-L-glutamine
Substrates: -
Products: -
Products: -
?
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Mn2+
required, can replace Mg2+, manganese-induced promiscuity of Cj1416
additional information
limited activity with Mg2+, expansion in the substrate profile of Cj1416 when the reaction is catalyzed in the presence of MnCTP
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
Highest Expressing Human Cell Lines
Cell Line LinksPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
metabolism
physiological function
metabolism
Campylobacter jejuni, is a Gram-negative pathogen that contains a unique O-methyl phosphoramidate (MeOPN) on its capsular polysaccharide. Enzyme CTP/phosphoglutamine cytididylyltransferase (Cj1416) catalyzes the second step of the biosynthesis pathway, the displacement of diphosphate from MgCTP by L-glutamine phosphate to form CDP-L-glutamine
metabolism
-
Campylobacter jejuni, is a Gram-negative pathogen that contains a unique O-methyl phosphoramidate (MeOPN) on its capsular polysaccharide. Enzyme CTP/phosphoglutamine cytididylyltransferase (Cj1416) catalyzes the second step of the biosynthesis pathway, the displacement of diphosphate from MgCTP by L-glutamine phosphate to form CDP-L-glutamine
-
metabolism
-
Campylobacter jejuni, is a Gram-negative pathogen that contains a unique O-methyl phosphoramidate (MeOPN) on its capsular polysaccharide. Enzyme CTP/phosphoglutamine cytididylyltransferase (Cj1416) catalyzes the second step of the biosynthesis pathway, the displacement of diphosphate from MgCTP by L-glutamine phosphate to form CDP-L-glutamine
-
physiological function
Campylobacter jejuni, is a Gram-negative pathogen that contains a unique O-methyl phosphoramidate (MeOPN) on its capsular polysaccharide. Enzyme CTP/phosphoglutamine cytididylyltransferase (Cj1416) catalyzes the second step of the biosynthesis pathway, the displacement of diphosphate from MgCTP by L-glutamine phosphate to form CDP-L-glutamine
physiological function
-
Campylobacter jejuni, is a Gram-negative pathogen that contains a unique O-methyl phosphoramidate (MeOPN) on its capsular polysaccharide. Enzyme CTP/phosphoglutamine cytididylyltransferase (Cj1416) catalyzes the second step of the biosynthesis pathway, the displacement of diphosphate from MgCTP by L-glutamine phosphate to form CDP-L-glutamine
-
physiological function
-
Campylobacter jejuni, is a Gram-negative pathogen that contains a unique O-methyl phosphoramidate (MeOPN) on its capsular polysaccharide. Enzyme CTP/phosphoglutamine cytididylyltransferase (Cj1416) catalyzes the second step of the biosynthesis pathway, the displacement of diphosphate from MgCTP by L-glutamine phosphate to form CDP-L-glutamine
-
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UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). CTDTR_CAMJE
Campylobacter jejuni subsp. jejuni serotype O:2 (strain ATCC 700819 / NCTC 11168)
253
0
29533
Swiss-Prot
-
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant His6-tagged enzyme from Escherichia coli strain Rosetta (DE3) by nickel affinity chromatography
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
gene Cj1416, recombinant expression of His6-tagged enzyme in Escherichia coli strain Rosetta (DE3)
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Taylor, Z.; Brown, H.; Holden, H.; Raushel, F.
Biosynthesis of nucleoside diphosphoramidates in Campylobacter jejuni
Biochemistry
56
6079-6082
2017
Campylobacter jejuni subsp. jejuni serotype O:2 (Q0P8J8), Campylobacter jejuni subsp. jejuni serotype O:2 ATCC 700819 (Q0P8J8)
brenda
Taylor, Z.W.; Raushel, F.M.
Manganese-induced substrate promiscuity in the reaction catalyzed by phosphoglutamine cytidylyltransferase from Campylobacter jejuni
Biochemistry
58
2144-2151
2019
Campylobacter jejuni subsp. jejuni (Q0P8J8), Campylobacter jejuni subsp. jejuni ATCC 700819 (Q0P8J8), Campylobacter jejuni subsp. jejuni NCTC 11168 (Q0P8J8)
brenda
EXTERNAL LINKS (specific for EC-Number 2.7.7.103)
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Release 2023.1 (January 2023)
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