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MetaCyc Enzyme: achromobactin synthetase protein A

Gene: Psyr2589 Accession Number: G-12143 (MetaCyc)

Synonyms: acsA

Species: Pseudomonas syringae pv. syringae B728a

Summary:
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 [Berti09a]).

Recombinant, hexahistidine-tagged protein was overexpressed in Escherichia coli and purified [Berti09a].

The enzyme from Dickeya dadantii strain 3937 (also named Erwinia chrysanthemi strain 3937 or Pectobacterium chrysanthemi strain 3937 [Franza05, McMahon08, Schmelz09]) was proposed to be a processive, type B NIS synthetase that catalyzes more than one reaction in achromobactin synthesis (in [Schmelz09]). See UniProtKB/TrEMBL Q93AU0.

Unification Links: Entrez:AAY37628

Relationship Links: Entrez-Nucleotide:PART-OF:CP000075

Gene-Reaction Schematic: ?

Credits:
Created 13-Aug-2010 by Fulcher CA , SRI International


Enzymatic reaction of: diaminobutyryl-citryl-ethanolamino-α-ketoglutarate:α-ketoglutarate ligase (achromobactin synthetase protein A)

diaminobutyryl-citryl-ethanolamino-α-ketoglutarate + ATP + 2-oxoglutarate <=> achromobactin + AMP + diphosphate + H+

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

Summary:
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 AcsA, hydroxamates were formed only upon incubation with 2-oxoglutarate [Berti09a].

Cofactors or Prosthetic Groups: Mg2+ [Berti09a]


Enzymatic reaction of: α-ketoglutaryl-diaminobutyryl-citryl-ethanolamine:α-ketoglutarate ligase (achromobactin synthetase protein A)

α-ketoglutaryl-diaminobutyryl-citryl-ethanolamine + ATP + 2-oxoglutarate <=> achromobactin + AMP + diphosphate + H+

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

Summary:
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 AcsA, hydroxamates were formed only upon incubation with 2-oxoglutarate [Berti09a].

Cofactors or Prosthetic Groups: Mg2+ [Berti09a]


Enzymatic reaction of: diaminobutyryl-citryl-ethanolamino-α-ketoglutarate synthetase (achromobactin synthetase protein A)

diaminobutyryl-citryl-ethanolamine + ATP + 2-oxoglutarate <=> diaminobutyryl-citryl-ethanolamino-α-ketoglutarate + AMP + diphosphate + H+

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

Summary:
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 AcsA, hydroxamates were formed only upon incubation with 2-oxoglutarate [Berti09a].

Cofactors or Prosthetic Groups: Mg2+ [Berti09a]


Enzymatic reaction of: α-ketoglutaryl-diaminobutyryl-citryl-ethanolamine synthetase (achromobactin synthetase protein A)

diaminobutyryl-citryl-ethanolamine + ATP + 2-oxoglutarate <=> α-ketoglutaryl-diaminobutyryl-citryl-ethanolamine + AMP + diphosphate + H+

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

Summary:
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 AcsA, hydroxamates were formed only upon incubation with 2-oxoglutarate [Berti09a].

Cofactors or Prosthetic Groups: Mg2+ [Berti09a]


References

Berti09a: Berti AD, Thomas MG (2009). "Analysis of achromobactin biosynthesis by Pseudomonas syringae pv. syringae B728a." J Bacteriol 191(14);4594-604. PMID: 19482931

Franza05: Franza T, Mahe B, Expert D (2005). "Erwinia chrysanthemi requires a second iron transport route dependent of the siderophore achromobactin for extracellular growth and plant infection." Mol Microbiol 55(1);261-75. PMID: 15612933

McMahon08: McMahon SA, Oke M, Liu H, Johnson KA, Carter L, Kadi N, White MF, Challis GL, Naismith JH (2008). "Purification, crystallization and data collection of Pectobacterium chrysanthemi AcsD, a type A siderophore synthetase." Acta Crystallogr Sect F Struct Biol Cryst Commun 64(Pt 11);1052-5. PMID: 18997340

Schmelz09: Schmelz S, Kadi N, McMahon SA, Song L, Oves-Costales D, Oke M, Liu H, Johnson KA, Carter LG, Botting CH, White MF, Challis GL, Naismith JH (2009). "AcsD catalyzes enantioselective citrate desymmetrization in siderophore biosynthesis." Nat Chem Biol 5(3);174-82. PMID: 19182782


Report Errors or Provide Feedback
Please cite the following article in publications resulting from the use of MetaCyc: Caspi et al, Nucleic Acids Research 42:D459-D471 2014
Page generated by SRI International Pathway Tools version 18.5 on Sun Nov 23, 2014, biocyc14.