CATH Classification

Domain Context

CATH Clusters

Superfamily N-terminal domain of ligase-like
Functional Family Enterobactin synthase component E

Enzyme Information

6.3.2.14
Enterobactin synthase.
based on mapping to UniProt P0ADI4
6 ATP + 3 2,3-dihydroxybenzoate + 3 L-serine = enterobactin + 6 AMP + 6 diphosphate.
-!- This enzyme complex catalyzes the conversion of three molecules each of 2,3-dihydroxybenzoate and L-serine to form the siderophore enterobactin. -!- In Escherichia coli the complex is formed by EntB (an aryl carrier protein that has to be activated by 4'-phosphopantetheine), EntD (a phosphopantetheinyl transferase that activates EntB), EntE (catalyzes the ATP-dependent condensation of 2,3-dihydroxybenzoate and holo-EntB to form the covalently arylated form of EntB), and EntF (a four domain protein that catalyzes the activation of L-serine by ATP, the condensation of the activated L-serine with the activated 2,3- dihydroxybenzoate, and the trimerization of three such moieties to a single enterobactin molecule).
3.3.2.1
Isochorismatase.
based on mapping to UniProt P0ADI4
Isochorismate + H(2)O = (2S,3S)-2,3-dihydroxy-2,3-dihydrobenzoate + pyruvate.
2.5.1.-
Transferring alkyl or aryl groups, other than methyl groups.
based on mapping to UniProt P10378
6.3.2.14
Enterobactin synthase.
based on mapping to UniProt P10378
6 ATP + 3 2,3-dihydroxybenzoate + 3 L-serine = enterobactin + 6 AMP + 6 diphosphate.
-!- This enzyme complex catalyzes the conversion of three molecules each of 2,3-dihydroxybenzoate and L-serine to form the siderophore enterobactin. -!- In Escherichia coli the complex is formed by EntB (an aryl carrier protein that has to be activated by 4'-phosphopantetheine), EntD (a phosphopantetheinyl transferase that activates EntB), EntE (catalyzes the ATP-dependent condensation of 2,3-dihydroxybenzoate and holo-EntB to form the covalently arylated form of EntB), and EntF (a four domain protein that catalyzes the activation of L-serine by ATP, the condensation of the activated L-serine with the activated 2,3- dihydroxybenzoate, and the trimerization of three such moieties to a single enterobactin molecule).
2.7.7.58
(2,3-dihydroxybenzoyl)adenylate synthase.
based on mapping to UniProt P10378
ATP + 2,3-dihydroxybenzoate = diphosphate + (2,3- dihydroxybenzoyl)adenylate.

UniProtKB Entries (1)

P0ADI4
ENTB_ECOLI
Escherichia coli K-12
Enterobactin synthase component B

PDB Structure

PDB 4IZ6
External Links
Method X-RAY DIFFRACTION
Organism
Primary Citation
Structure determination of the functional domain interaction of a chimeric nonribosomal peptide synthetase from a challenging crystal with noncrystallographic translational symmetry.
Sundlov, J.A., Gulick, A.M.
Acta Crystallogr.,Sect.D
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