Literature summary for 6.2.1.25 extracted from

Crosby, H.A.; Heiniger, E.K.; Harwood, C.S.; Escalante-Semerena, J.C.
Reversible N(E)-lysine acetylation regulates the activity of acyl-CoA synthetases involved in anaerobic benzoate catabolism in Rhodopseudomonas palustris (2010), Mol. Microbiol., 76, 874-888.

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Organism

Organism	UniProt	Comment	Textmining
Rhodopseudomonas palustris	-	-	-

Posttranslational Modification

Posttranslational Modification	Comment	Organism
additional information	acetylation of residue Lys512 inactivates BadA, deacetylation reactivates BadA. Acetyltransferase RpPat modifies BadA, and also modifies acetyl-CoA synthetase. At least two deacetylases reactivate BadAAc. One is SrtN, a sirtuintype NAD+-dependent deacetylase, the other deacetylase is lysine deacetylase LdaA, an acetate-forming protein deacetylase. LdaA reactivates HbaAc and AliAAc in vitro	Rhodopseudomonas palustris

Renatured (Commentary)

Renatured (Comment)	Organism
acetylation of residue Lys512 inactivates BadA, deacetylation reactivates BadA	Rhodopseudomonas palustris

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
ATP + benzoate + CoA	-	Rhodopseudomonas palustris	AMP + diphosphate + benzoyl-CoA	-	?

Synonyms

Synonyms	Comment	Organism
BadA	-	Rhodopseudomonas palustris

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Release 2023.1 (January 2023)