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Information on EC 2.7.3.13 - glutamine kinase
for references in articles please use BRENDA:EC2.7.3.13
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EC Tree 2 Transferases
2.7 Transferring phosphorus-containing groups
2.7.3 Phosphotransferases with a nitrogenous group as acceptor
2.7.3.13 glutamine kinase
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
showSynonyms
cj1418, glutamine kinase, l-glutamine kinase, more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
Cj1418
L-glutamine kinase
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
ATP + L-glutamine + H2O = AMP + phosphate + N5-phospho-L-glutamine
-
-
-
-
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SYSTEMATIC NAME
IUBMB Comments
ATP:L-glutamine N5-phosphotransferase
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
ATP + beta-L-aspartyl hydroxamate + H2O
AMP + phosphate + N4-phospho-beta-L-aspartyl hydroxamate
ATP + gamma-L-glutamyl hydrazide + H2O
AMP + phosphate + N5-phospho-gamma-L-glutamyl hydrazide
ATP + gamma-L-glutamyl hydroxamate + H2O
AMP + phosphate + N5-phospho-gamma-L-glutamyl hydroxamate
ATP + beta-L-aspartyl hydroxamate + H2O
AMP + phosphate + N4-phospho-beta-L-aspartyl hydroxamate
Substrates: -
Products: -
Products: -
?
ATP + beta-L-aspartyl hydroxamate + H2O
AMP + phosphate + N4-phospho-beta-L-aspartyl hydroxamate
Campylobacter jejuni ATCC 700819
Substrates: -
Products: -
Products: -
?
ATP + D-glutamine + H2O
AMP + phosphate + N5-phospho-D-glutamine
Substrates: -
Products: -
Products: -
?
ATP + D-glutamine + H2O
AMP + phosphate + N5-phospho-D-glutamine
Campylobacter jejuni ATCC 700819
Substrates: -
Products: -
Products: -
?
ATP + gamma-L-glutamyl hydrazide + H2O
AMP + phosphate + N5-phospho-gamma-L-glutamyl hydrazide
Substrates: -
Products: -
Products: -
?
ATP + gamma-L-glutamyl hydrazide + H2O
AMP + phosphate + N5-phospho-gamma-L-glutamyl hydrazide
Campylobacter jejuni ATCC 700819
Substrates: -
Products: -
Products: -
?
ATP + gamma-L-glutamyl hydroxamate + H2O
AMP + phosphate + N5-phospho-gamma-L-glutamyl hydroxamate
Substrates: second best substrate
Products: -
Products: -
?
ATP + gamma-L-glutamyl hydroxamate + H2O
AMP + phosphate + N5-phospho-gamma-L-glutamyl hydroxamate
Campylobacter jejuni ATCC 700819
Substrates: second best substrate
Products: -
Products: -
?
ATP + L-glutamine + H2O
AMP + phosphate + N5-phospho-L-glutamine
-
Substrates: -
Products: -
Products: -
?
ATP + L-glutamine + H2O
AMP + phosphate + N5-phospho-L-glutamine
Substrates: -
Products: -
Products: -
r
ATP + L-glutamine + H2O
AMP + phosphate + N5-phospho-L-glutamine
-
Substrates: -
Products: -
Products: -
r
ATP + L-glutamine + H2O
AMP + phosphate + N5-phospho-L-glutamine
Substrates: best substrate
Products: -
Products: -
r
ATP + L-glutamine + H2O
AMP + phosphate + N5-phospho-L-glutamine
Campylobacter jejuni ATCC 700819
Substrates: -
Products: -
Products: -
r
ATP + L-glutamine + H2O
AMP + phosphate + N5-phospho-L-glutamine
-
Substrates: -
Products: -
Products: -
?
additional information
?
-
-
Substrates: no activity with ammonia, L-glutamate, or L-asparagine
Products: -
Products: -
?
additional information
?
-
Substrates: no activity with L-glutamate and L-asparagine
Products: -
Products: -
?
additional information
?
-
-
Substrates: no activity with L-glutamate and L-asparagine
Products: -
Products: -
?
additional information
?
-
-
Substrates: no activity with ammonia, L-glutamate, or L-asparagine
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
ATP + L-glutamine + H2O
AMP + phosphate + N5-phospho-L-glutamine
-
Substrates: -
Products: -
Products: -
?
ATP + L-glutamine + H2O
AMP + phosphate + N5-phospho-L-glutamine
Substrates: -
Products: -
Products: -
r
ATP + L-glutamine + H2O
AMP + phosphate + N5-phospho-L-glutamine
-
Substrates: -
Products: -
Products: -
r
ATP + L-glutamine + H2O
AMP + phosphate + N5-phospho-L-glutamine
Campylobacter jejuni ATCC 700819
Substrates: -
Products: -
Products: -
r
ATP + L-glutamine + H2O
AMP + phosphate + N5-phospho-L-glutamine
-
Substrates: -
Products: -
Products: -
?
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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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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
-
the enzyme is required for the biosynthesis of the phosphoramidate group of O-methyl phosphoramidate
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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). GLKIN_CAMJE
Campylobacter jejuni subsp. jejuni serotype O:2 (strain ATCC 700819 / NCTC 11168)
779
0
90325
Swiss-Prot
-
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
H737N
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli Rosetta (DE3) cells
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Taylor, Z.W.; Brown, H.A.; Narindoshvili, T.; Wenzel, C.Q.; Szymanski, C.M.; Holden, H.M.; Raushel, F.M.
Discovery of a glutamine kinase required for the biosynthesis of the O-methyl phosphoramidate modifications found in the capsular polysaccharides of Campylobacter jejuni
J. Am. Chem. Soc.
139
9463-9466
2017
Campylobacter jejuni, Campylobacter jejuni NCTC11168
brenda
Taylor, Z.W.; Raushel, F.M.
Cytidine diphosphoramidate kinase an enzyme required for the biosynthesis of the O-methyl phosphoramidate modification in the capsular polysaccharides of Campylobacter jejuni
Biochemistry
57
2238-2244
2018
Campylobacter jejuni
brenda
Taylor, Z.W.; Chamberlain, A.R.; Raushel, F.M.
Substrate specificity and chemical mechanism for the reaction catalyzed by glutamine kinase
Biochemistry
57
5447-5455
2018
Campylobacter jejuni (Q0P8J6), Campylobacter jejuni, Campylobacter jejuni ATCC 700819 (Q0P8J6)
brenda
EXTERNAL LINKS (specific for EC-Number 2.7.3.13)
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Release 2026.1 (March 2026)
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