|Gene:||Psyr2584||Accession Number: G-12140 (MetaCyc)|
The subunit structure of this enzyme has not been reported.
This enzyme is a member of the NIS synthetase superfamily, a conserved group of enzymes catalyzing adenylation and condensation reactions. NIS synthetases are structurally distinct from the non-ribosomal peptide synthetases (NRPS). NIS (NRPS-independent) synthetases are involved in siderophore biosynthesis. They activate carboxylic acid substrates by forming acid adenylates in a mechanism distinct from NRPS enzymes. Based on bioinformatic analyses there are three proposed subclasses within the NIS superfamily depending upon the type of carboxylic acid substrate that is activated. Type A NIS synthetases recognize one of the pro-chiral groups of citrate. Type B NIS synthetases recognize the δ-acid group of 2-oxoglutarate (α-ketoglutarate). Type C NIS synthetases recognize esterified or amidated derivatives of carboxylic acids (in [Berti09]).
Gene Citations: [Feil05]
Unification Links: Entrez:AAY37623
Relationship Links: Entrez-Nucleotide:PART-OF:CP000075
Enzymatic reaction of: citrate:ethanolamine ligase (achromobactin synthetase protein D)
The reaction direction shown, that is, A + B ↔ C + D versus C + D ↔ A + B, is in accordance with the direction in which it was curated.
The reaction is favored in the direction shown.
In Pathways: achromobactin biosynthesis
The enzyme was assayed for activation of citrate, or 2-oxoglutarate using a method that detects hydroxamates formed from the reaction between activated carboxylic acids and hydroxylamine. For AcsD, hydroxamates were formed upon incubation with citrate [Berti09].
Feil05: Feil H, Feil WS, Chain P, Larimer F, DiBartolo G, Copeland A, Lykidis A, Trong S, Nolan M, Goltsman E, Thiel J, Malfatti S, Loper JE, Lapidus A, Detter JC, Land M, Richardson PM, Kyrpides NC, Ivanova N, Lindow SE (2005). "Comparison of the complete genome sequences of Pseudomonas syringae pv. syringae B728a and pv. tomato DC3000." Proc Natl Acad Sci U S A 102(31);11064-9. PMID: 16043691
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