D
IPR041354

4'-phosphopantetheinyl transferase, N-terminal domain

InterPro entry
Short name4PPT_N

Description

This entry represents the N-terminal domain from 4'- phosphopantetheinyl transferase enzymes. This domain is structurally related to the 4'-phosphopantetheinyl transferase domain (
IPR008278
) with which it forms a pseudodimeric arrangement
[1]
.

This domain can also be found in enterobactin synthase component D (EntD), which forms part of the enterobactin-synthetase enzyme complex. It plays an essential role in the assembly of the enterobactin by catalyzing the transfer of the 4'-phosphopantetheine (Ppant) moiety from coenzyme A to the apo-domains of both EntB (ArCP domain) and EntF (PCP domain) to yield their holo-forms which make them competent for the activation of 2,3-dihydroxybenzoate (DHB) and L-serine, respectively
[2]
. Deletion studies involving EntD- mutants have shown that it is essential for virulence
[3]
.

References

1.Structure, biochemistry, and inhibition of essential 4'-phosphopantetheinyl transferases from two species of Mycobacteria. Vickery CR, Kosa NM, Casavant EP, Duan S, Noel JP, Burkart MD. ACS Chem. Biol. 9, 1939-44, (2014). View articlePMID: 24963544

2.Enterobactin biosynthesis in Escherichia coli: isochorismate lyase (EntB) is a bifunctional enzyme that is phosphopantetheinylated by EntD and then acylated by EntE using ATP and 2,3-dihydroxybenzoate. Gehring AM, Bradley KA, Walsh CT. Biochemistry 36, 8495-503, (1997). View articlePMID: 9214294

3.Nucleotide sequence of a cluster of Escherichia coli enterobactin biosynthesis genes: identification of entA and purification of its product 2,3-dihydro-2,3-dihydroxybenzoate dehydrogenase. Liu J, Duncan K, Walsh CT. J. Bacteriol. 171, 791-8, (1989). View articlePMID: 2521622

Cross References

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