Entry |
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Name |
L-proline---[L-prolyl-carrier protein] ligase;
pltF (gene name);
bmp4 (gene name);
pigI (gene name)
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Class |
Ligases;
Forming carbon-sulfur bonds;
Acid-thiol ligases
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Sysname |
L-proline:[L-prolyl-carrier protein] ligase (AMP-forming)
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Reaction(IUBMB) |
ATP + L-proline + holo-[L-prolyl-carrier protein] = AMP + diphosphate + L-prolyl-[L-prolyl-carrier protein] (overall reaction);
(1a) ATP + L-proline = diphosphate + (L-prolyl)adenylate [RN: R12056];
(1b) (L-prolyl)adenylate + holo-[L-prolyl-carrier protein] = AMP + L-prolyl-[L-prolyl-carrier protein]
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Reaction(KEGG) |
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Substrate |
ATP [CPD: C00002];
L-proline [CPD: C00148];
holo-[L-prolyl-carrier protein];
(L-prolyl)adenylate [CPD: C20656]
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Product |
AMP [CPD: C00020];
diphosphate [CPD: C00013];
L-prolyl-[L-prolyl-carrier protein];
(L-prolyl)adenylate [CPD: C20656]
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Comment |
The enzyme participates in the biosynthesis of several pyrrole-containing compounds, such as undecylprodigiosin, prodigiosin, pyoluteorin, and coumermycin A1. It catalyses the activation of L-proline to an adenylate form, followed by its transfer to the 4'-phosphopantheine moiety of an L-prolyl-carrier protein.
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History |
EC 6.2.1.53 created 2018
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Pathway |
ec01130 | Biosynthesis of antibiotics |
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Orthology |
K12719 | L-proline---[L-prolyl-carrier protein] ligase |
K21780 | L-proline---[L-prolyl-carrier protein] ligase |
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Genes |
» show all
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Reference |
|
Authors |
Thomas MG, Burkart MD, Walsh CT. |
Title |
Conversion of L-proline to pyrrolyl-2-carboxyl-S-PCP during undecylprodigiosin and pyoluteorin biosynthesis. |
Journal |
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Reference |
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Authors |
Harris AK, Williamson NR, Slater H, Cox A, Abbasi S, Foulds I, Simonsen HT, Leeper FJ, Salmond GP |
Title |
The Serratia gene cluster encoding biosynthesis of the red antibiotic, prodigiosin, shows species- and strain-dependent genome context variation. |
Journal |
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Sequence |
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Reference |
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Authors |
Williamson NR, Simonsen HT, Ahmed RA, Goldet G, Slater H, Woodley L, Leeper FJ, Salmond GP |
Title |
Biosynthesis of the red antibiotic, prodigiosin, in Serratia: identification of a novel 2-methyl-3-n-amyl-pyrrole (MAP) assembly pathway, definition of the terminal condensing enzyme, and implications for undecylprodigiosin biosynthesis in Streptomyces. |
Journal |
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Sequence |
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Other DBs |
ExplorEnz - The Enzyme Database: | 6.2.1.53 |
ExPASy - ENZYME nomenclature database: | 6.2.1.53 |
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