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Information on EC 6.2.1.46 - L-allo-isoleucine-holo-[CmaA peptidyl-carrier protein] ligase
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6.2.1.46 L-allo-isoleucine-holo-[CmaA peptidyl-carrier protein] ligaseIUBMB Comments
This two-domain protein from the bacterium Pseudomonas syringae contains an adenylation domain (A domain) and a thiolation domain (T domain). It catalyses the adenylation of L-allo-isoleucine and its attachment to the T domain. The enzyme is involved in the biosynthesis of the toxin coronatine, which mimics the plant hormone jasmonic acid isoleucine. Coronatine promotes opening of the plant stomata allowing bacterial invasion, which is followed by bacterial growth in the apoplast, systemic susceptibility, and disease.
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The expected taxonomic range for this enzyme is: Pseudomonas syringae group
Reaction Schemes
Synonyms
CmaA, CmaE, L-allo-isoleucine:holo-[CmaA peptidyl-carrier protein] ligase, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
CmaA
L-allo-isoleucine:holo-[CmaA peptidyl-carrier protein] ligase
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-
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-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
ATP + L-allo-isoleucine + holo-[CmaA peptidyl-carrier protein] = AMP + diphosphate + L-allo-isoleucyl-[CmaA peptidyl-carrier protein]
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SYSTEMATIC NAME
IUBMB Comments
L-allo-isoleucine:holo-[CmaA peptidyl-carrier protein] ligase (AMP-forming)
This two-domain protein from the bacterium Pseudomonas syringae contains an adenylation domain (A domain) and a thiolation domain (T domain). It catalyses the adenylation of L-allo-isoleucine and its attachment to the T domain. The enzyme is involved in the biosynthesis of the toxin coronatine, which mimics the plant hormone jasmonic acid isoleucine. Coronatine promotes opening of the plant stomata allowing bacterial invasion, which is followed by bacterial growth in the apoplast, systemic susceptibility, and disease.
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
ATP + L-allo-isoleucine + holo-[CmaA peptidyl-carrier protein]
AMP + diphosphate + L-allo-isoleucyl-S-[CmaA peptidyl-carrier protein]
ATP + L-allo-isoleucine + [CmaA -protein-T-domain]-4'-phosphopantetheine
AMP + diphosphate + S-L-allo-isoleucyl-[CmaA-protein-T-domain]-4'-phosphopantetheine
ATP + L-allo-isoleucine + [CmaA-protein-T-domain]-4'-phosphopantetheine
AMP + diphosphate + S-L-allo-isoleucyl-[CmaA-protein-T-domain]-4'-phosphopantetheine
ATP + L-isoleucine + [CmaA-protein-T-domain]-4'-phosphopantetheine
AMP + diphosphate + S-L-isoleucyl-[CmaA-protein-T-domain]-4'-phosphopantetheine
ATP + L-leucine + [CmaA-protein-T-domain]-4'-phosphopantetheine
AMP + diphosphate + S-L-leucyl-[CmaA-protein-T-domain]-4'-phosphopantetheine
ATP + L-valine + [CmaA-protein-T-domain]-4'-phosphopantetheine
AMP + diphosphate + S-L-valyl-[CmaA-protein-T-domain]-4'-phosphopantetheine
additional information
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aminoacylated-S-CmaE will transfer the L-Val moiety to the HS-pantetheinyl arm of other T domains, including CytC2, BarA, and ArfA C2-A2-T2 but not to free HS-pantetheine. CmaD can be loaded with other amino acids, for example, L-Leu and L-Thr, by the action of heterologous donor T domains containing alternative aminoacyl groups. Additionally, CmaE is able to accept L-Phe as a substrate when presented on CmaD and is able to load this aminoacyl moiety onto heterologous T domains
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?
ATP + L-allo-isoleucine + holo-[CmaA peptidyl-carrier protein]
AMP + diphosphate + L-allo-isoleucyl-S-[CmaA peptidyl-carrier protein]
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during the biosynthesis of the cyclopropyl amino acid coronamic acid from L-allo-Ile by the phytotoxic Pseudomonas syringae, the aminoacyl group covalently attached to the pantetheinyl arm of CmaA is shuttled to the HS-pantetheinyl arm of the protein CmaD by the aminoacyltransferase CmaE, reversible shuttling process
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r
ATP + L-allo-isoleucine + holo-[CmaA peptidyl-carrier protein]
AMP + diphosphate + L-allo-isoleucyl-S-[CmaA peptidyl-carrier protein]
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CmaE will only recognize deacylated CmaA for initial complexation. The aminoacyl group becomes covalently attached to the active site Cys of CmaE and can then be transferred out to the holo pantetheinylated form of CmaD, reversible shuttling process
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r
ATP + L-allo-isoleucine + [CmaA -protein-T-domain]-4'-phosphopantetheine
AMP + diphosphate + S-L-allo-isoleucyl-[CmaA-protein-T-domain]-4'-phosphopantetheine
the didomain protein contains an adenylation domain (A domain) and a thiolation domain (T domain). It catalyzes the adenylation of L-allo-isoleucine and the attachment of L-allo-isoleucine to the CmaA T domain. The enzyme-bound L-allo-isoleucine serves as the substrate for the later stages of the biosdynthesis of the toxin coronatine. This toxin mimics the plant hormone jasmonic acid isoleucine and promotes opening of stomata for bacterial entry, bacterial growth in the apoplast, systemic susceptibility, and disease
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-
?
ATP + L-allo-isoleucine + [CmaA -protein-T-domain]-4'-phosphopantetheine
AMP + diphosphate + S-L-allo-isoleucyl-[CmaA-protein-T-domain]-4'-phosphopantetheine
the didomain protein contains an adenylation domain (A domain) and a thiolation domain (T domain). It catalyzes the adenylation of L-allo-isoleucine and the attachment of L-allo-isoleucine to the CmaA T domain. The enzyme-bound L-allo-isoleucine serves as the substrate for the later stages of the biosdynthesis of the toxin coronatine. This toxin mimics the plant hormone jasmonic acid isoleucine and promotes opening of stomata for bacterial entry, bacterial growth in the apoplast, systemic susceptibility, and disease
-
-
?
ATP + L-allo-isoleucine + [CmaA-protein-T-domain]-4'-phosphopantetheine
AMP + diphosphate + S-L-allo-isoleucyl-[CmaA-protein-T-domain]-4'-phosphopantetheine
the enzyme catalyzes the adenylation of L-isoleucine, L-leucine and L-valine with about 40% of the activity compared to L-allo-isoleucine
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-
?
ATP + L-allo-isoleucine + [CmaA-protein-T-domain]-4'-phosphopantetheine
AMP + diphosphate + S-L-allo-isoleucyl-[CmaA-protein-T-domain]-4'-phosphopantetheine
the enzyme catalyzes the adenylation of L-isoleucine, L-leucine and L-valine with about 40% of the activity compared to L-allo-isoleucine
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-
?
ATP + L-isoleucine + [CmaA-protein-T-domain]-4'-phosphopantetheine
AMP + diphosphate + S-L-isoleucyl-[CmaA-protein-T-domain]-4'-phosphopantetheine
the enzyme catalyzes the adenylation of L-isoleucine, L-leucine and L-valine with about 40% of the activity compared to L-allo-isoleucine
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-
?
ATP + L-isoleucine + [CmaA-protein-T-domain]-4'-phosphopantetheine
AMP + diphosphate + S-L-isoleucyl-[CmaA-protein-T-domain]-4'-phosphopantetheine
the enzyme catalyzes the adenylation of L-isoleucine, L-leucine and L-valine with about 40% of the activity compared to L-allo-isoleucine
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-
?
ATP + L-leucine + [CmaA-protein-T-domain]-4'-phosphopantetheine
AMP + diphosphate + S-L-leucyl-[CmaA-protein-T-domain]-4'-phosphopantetheine
the enzyme catalyzes the adenylation of L-isoleucine, L-leucine and L-valine with about 40% of the activity compared to L-allo-isoleucine
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-
?
ATP + L-leucine + [CmaA-protein-T-domain]-4'-phosphopantetheine
AMP + diphosphate + S-L-leucyl-[CmaA-protein-T-domain]-4'-phosphopantetheine
the enzyme catalyzes the adenylation of L-isoleucine, L-leucine and L-valine with about 40% of the activity compared to L-allo-isoleucine
-
-
?
ATP + L-valine + [CmaA-protein-T-domain]-4'-phosphopantetheine
AMP + diphosphate + S-L-valyl-[CmaA-protein-T-domain]-4'-phosphopantetheine
the enzyme catalyzes the adenylation of L-isoleucine, L-leucine and L-valine with about 40% of the activity compared to L-allo-isoleucine
-
-
?
ATP + L-valine + [CmaA-protein-T-domain]-4'-phosphopantetheine
AMP + diphosphate + S-L-valyl-[CmaA-protein-T-domain]-4'-phosphopantetheine
the enzyme catalyzes the adenylation of L-isoleucine, L-leucine and L-valine with about 40% of the activity compared to L-allo-isoleucine
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-
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
ATP + L-allo-isoleucine + holo-[CmaA peptidyl-carrier protein]
AMP + diphosphate + L-allo-isoleucyl-S-[CmaA peptidyl-carrier protein]
-
during the biosynthesis of the cyclopropyl amino acid coronamic acid from L-allo-Ile by the phytotoxic Pseudomonas syringae, the aminoacyl group covalently attached to the pantetheinyl arm of CmaA is shuttled to the HS-pantetheinyl arm of the protein CmaD by the aminoacyltransferase CmaE, reversible shuttling process
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-
r
ATP + L-allo-isoleucine + [CmaA -protein-T-domain]-4'-phosphopantetheine
AMP + diphosphate + S-L-allo-isoleucyl-[CmaA-protein-T-domain]-4'-phosphopantetheine
ATP + L-allo-isoleucine + [CmaA -protein-T-domain]-4'-phosphopantetheine
AMP + diphosphate + S-L-allo-isoleucyl-[CmaA-protein-T-domain]-4'-phosphopantetheine
the didomain protein contains an adenylation domain (A domain) and a thiolation domain (T domain). It catalyzes the adenylation of L-allo-isoleucine and the attachment of L-allo-isoleucine to the CmaA T domain. The enzyme-bound L-allo-isoleucine serves as the substrate for the later stages of the biosdynthesis of the toxin coronatine. This toxin mimics the plant hormone jasmonic acid isoleucine and promotes opening of stomata for bacterial entry, bacterial growth in the apoplast, systemic susceptibility, and disease
-
-
?
ATP + L-allo-isoleucine + [CmaA -protein-T-domain]-4'-phosphopantetheine
AMP + diphosphate + S-L-allo-isoleucyl-[CmaA-protein-T-domain]-4'-phosphopantetheine
the didomain protein contains an adenylation domain (A domain) and a thiolation domain (T domain). It catalyzes the adenylation of L-allo-isoleucine and the attachment of L-allo-isoleucine to the CmaA T domain. The enzyme-bound L-allo-isoleucine serves as the substrate for the later stages of the biosdynthesis of the toxin coronatine. This toxin mimics the plant hormone jasmonic acid isoleucine and promotes opening of stomata for bacterial entry, bacterial growth in the apoplast, systemic susceptibility, and disease
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-
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.04
L-allo-isoleucine
pH 7.5, 25°C, the assay measures the release of diphosphate by means of a coupled enzyme system in which diphosphate drives the reduction of NAD+ to NADH
0.5
L-isoleucine
pH 7.5, 25°C, the assay measures the release of diphosphate by means of a coupled enzyme system in which diphosphate drives the reduction of NAD+ to NADH
1.5
L-leucine
pH 7.5, 25°C, the assay measures the release of diphosphate by means of a coupled enzyme system in which diphosphate drives the reduction of NAD+ to NADH
1.2
L-valine
pH 7.5, 25°C, the assay measures the release of diphosphate by means of a coupled enzyme system in which diphosphate drives the reduction of NAD+ to NADH
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0015
L-allo-isoleucine
pH 7.5, 25°C, the assay measures the release of diphosphate by means of a coupled enzyme system in which diphosphate drives the reduction of NAD+ to NADH
0.012
L-isoleucine
pH 7.5, 25°C, the assay measures the release of diphosphate by means of a coupled enzyme system in which diphosphate drives the reduction of NAD+ to NADH
0.03
L-leucine
pH 7.5, 25°C, the assay measures the release of diphosphate by means of a coupled enzyme system in which diphosphate drives the reduction of NAD+ to NADH
0.023
L-valine
pH 7.5, 25°C, the assay measures the release of diphosphate by means of a coupled enzyme system in which diphosphate drives the reduction of NAD+ to NADH
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0375
L-allo-isoleucine
pH 7.5, 25°C, the assay measures the release of diphosphate by means of a coupled enzyme system in which diphosphate drives the reduction of NAD+ to NADH
0.024
L-isoleucine
pH 7.5, 25°C, the assay measures the release of diphosphate by means of a coupled enzyme system in which diphosphate drives the reduction of NAD+ to NADH
0.02
L-leucine
pH 7.5, 25°C, the assay measures the release of diphosphate by means of a coupled enzyme system in which diphosphate drives the reduction of NAD+ to NADH
0.019
L-valine
pH 7.5, 25°C, the assay measures the release of diphosphate by means of a coupled enzyme system in which diphosphate drives the reduction of NAD+ to NADH
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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
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
physiological function
physiological function
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the enzyme is involved in the biosynthesis of the toxin coronatine. This toxin mimics the plant hormone jasmonic acid isoleucine and promotes opening of stomata for bacterial entry, bacterial growth in the apoplast, systemic susceptibility, and disease symptoms
physiological function
the enzyme is involved in the biosynthesis of the toxin coronatine. This toxin mimics the plant hormone jasmonic acid isoleucine and promotes opening of stomata for bacterial entry, bacterial growth in the apoplast, systemic susceptibility, and disease symptoms
physiological function
-
the transferase shuttles aminoacyl groups between carrier protein domains in the coronamic acid biosynthetic pathway, overview
physiological function
-
the enzyme is involved in the biosynthesis of the toxin coronatine. This toxin mimics the plant hormone jasmonic acid isoleucine and promotes opening of stomata for bacterial entry, bacterial growth in the apoplast, systemic susceptibility, and disease symptoms
-
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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). Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Pseudomonas syringae pv. syringae FF5 as a FLAG-tagged protein
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Strieter, E.R.; Vaillancourt, F.H.; Walsh, C.T.
CmaE: a transferase shuttling aminoacyl groups between carrier protein domains in the coronamic acid biosynthetic pathway
Biochemistry
46
7549-7557
2007
Pseudomonas syringae
brenda
Couch, R.; O'Connor, S.E.; Seidle, H.; Walsh, C.T.; Parry, R.
Characterization of CmaA, an adenylation-thiolation didomain enzyme involved in the biosynthesis of coronatine
J. Bacteriol.
186
35-42
2004
Pseudomonas syringae (Q6TNA5), Pseudomonas syringae pv. glycinea PG4180 (Q6TNA5)
brenda
Vaillancourt, F.H.; Yeh, E.; Vosburg, D.A.; O'Connor, S.E.; Walsh, C.T.
Cryptic chlorination by a non-haem iron enzyme during cyclopropyl amino acid biosynthesis
Nature
436
1191-1194
2005
Pseudomonas syringae
brenda
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Release 2023.1 (January 2023)
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