| Entry |
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| Symbol |
cmaA
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| Name |
coronamic acid synthetase CmaA, adenylation and thiolation didomain protein [EC: 6.2.1.46]
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| Reaction |
| R11084 | L-allo-isoleucine:[peptidyl-carrier protein] ligase (AMP-forming) |
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| Brite |
KEGG Orthology (KO) [BR:ko00001]
09180 Brite Hierarchies
09181 Protein families: metabolism
01008 Polyketide biosynthesis proteins
K15646 cmaA; coronamic acid synthetase CmaA, adenylation and thiolation didomain protein
Enzymes [BR:ko01000]
6. Ligases
6.2 Forming carbon-sulfur bonds
6.2.1 Acid-thiol ligases
6.2.1.46 L-allo-isoleucine---holo-[CmaA peptidyl-carrier protein] ligase
K15646 cmaA; coronamic acid synthetase CmaA, adenylation and thiolation didomain protein
Polyketide biosynthesis proteins [BR:ko01008]
Polyketide synthase (PKS)
PKS-NRPS hybrid
Bacterial type (modular)
Coronatine hybrid PKS-NRPS
K15646 cmaA; coronamic acid synthetase CmaA, adenylation and thiolation didomain protein
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| Genes |
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| Reference |
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| Authors |
Vaillancourt FH, Yeh E, Vosburg DA, O'Connor SE, Walsh CT |
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| Title |
Cryptic chlorination by a non-haem iron enzyme during cyclopropyl amino acid biosynthesis. |
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| Journal |
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| Reference |
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| Authors |
Couch R, O'Connor SE, Seidle H, Walsh CT, Parry R |
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| Title |
Characterization of CmaA, an adenylation-thiolation didomain enzyme involved in the biosynthesis of coronatine. |
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| Journal |
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| Sequence |
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| LinkDB |
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