Ligases;
Forming carbon-sulfur bonds;
Acid-thiol ligases
BRITE hierarchy

L-proline:[L-prolyl-carrier protein] ligase (AMP-forming)

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]

R12056;
(other) R06746 R12057
Reaction

ATP [CPD:C00002];
L-proline [CPD:C00148];
holo-[L-prolyl-carrier protein];
(L-prolyl)adenylate [CPD:C20656]

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.

EC 6.2.1.53 created 2018

1  [PMID:11880032]

Thomas MG, Burkart MD, Walsh CT.

Conversion of L-proline to pyrrolyl-2-carboxyl-S-PCP during undecylprodigiosin and pyoluteorin biosynthesis.

Chem Biol 9:171-84 (2002)
DOI:10.1016/S1074-5521(02)00100-X

2  [PMID:15528645]

Harris AK, Williamson NR, Slater H, Cox A, Abbasi S, Foulds I, Simonsen HT, Leeper FJ, Salmond GP

The Serratia gene cluster encoding biosynthesis of the red antibiotic, prodigiosin, shows species- and strain-dependent genome context variation.

Microbiology 150:3547-60 (2004)
DOI:10.1099/mic.0.27222-0

[ag:CAH55637]

3  [PMID:15853884]

Williamson NR, Simonsen HT, Ahmed RA, Goldet G, Slater H, Woodley L, Leeper FJ, Salmond GP

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.

Mol Microbiol 56:971-89 (2005)
DOI:10.1111/j.1365-2958.2005.04602.x

[ag:CAH55637]