Enterobactin synthetase-like, component D (IPR003542)

Short name: Enbac_synth_compD-like

Overlapping homologous superfamilies

Family relationships



Iron is essential for growth in both bacteria and mammals. Controlling the amount of free iron in solution is often used as a tactic by hosts to limit invasion of pathogenic microbes; binding iron tightly within protein molecules can accomplish this. Such iron-protein complexes include haem in blood, lactoferrin in tears/saliva and transferrin in blood plasma. Some bacteria express surface receptors to capture eukaryotic iron-binding compounds, while others have evolved siderophores to scavenge iron from iron-binding host proteins [PMID: 8057905].

The absence of free iron molecules in the surrounding environment triggers transcription of gene clusters that encode both siderophore-synthesis enzymes, and receptors that recognise iron-bound siderophores [PMID: 2521621]. Classic examples are the enterobactin/enterochelin clusters found in Escherichia coli and Salmonella, although similar moieties in other pathogens have been identified. The enzymic machinery that produces vibrionectin in Vibrio cholerae is such a homologue [PMID: 9371453].

EntD forms part of the enterobactin-synthetase enzyme complex. It is involved in the final stage of enterobactin biosynthesis, converting 2,3-dihydroxybenzoic acid (DHBA) and L-serine to enterobactin. Deletion studies involving EntD- mutants have shown that it is essential for virulence [PMID: 2521622].

This entry also identifies some 4'-phosphopantetheinyl transferase proteins.

GO terms

Biological Process

GO:0009239 enterobactin biosynthetic process

Molecular Function

GO:0016780 phosphotransferase activity, for other substituted phosphate groups

Cellular Component

GO:0009366 enterobactin synthetase complex

Contributing signatures

Signatures from InterPro member databases are used to construct an entry.