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phosphopantetheine-binding protein
A 4'-phosphopantetheine prosthetic group is attached through a serine. This prosthetic group acts as a a 'swinging arm' for the attachment of activated fatty acid and amino-acid groups. This domain forms a four helix bundle. This family includes members not included in Prosite. The inclusion of these members is supported by sequence analysis and functional evidence. The related domain of Swiss:P19828 has the attachment serine replaced by an alanine. (from Pfam)
condensation domain-containing protein
This domain is found in many multi-domain enzymes which synthesise peptide antibiotics. This domain catalyses a condensation reaction to form peptide bonds in non- ribosomal peptide biosynthesis. It is usually found to the carboxy side of a phosphopantetheine binding domain (Pfam:PF00550). It has been shown that mutations in the HHXXXDG motif abolish activity suggesting this is part of the active site [1]. [1]. 9712910. Peptide bond formation in nonribosomal peptide biosynthesis.. Catalytic role of the condensation domain.. Stachelhaus T, Mootz HD, Bergendahl V, Marahiel MA;. J Biol Chem 1998;273:22773-22781. (from Pfam)
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