FEATURES

FAMILY

class-I pyridoxal-phosphate-dependent aminotransferase family

DESCRIPTION

Also known as ALD1_ARATH, ALD1. Aminotransferase involved in local and systemic acquired resistance (SAR) to the bacterial pathogen P.syringae. Required for salicylic acid (SA) and camalexin accumulation upon pathogen infection. Possesses aminotransferase activity in vitro and may generate amino-acid-derived defense signals in vivo. May be involved in ethylene-induced senescence signaling. Involved in the biosynthesis of pipecolate (Pip), a metabolite that orchestrates defense amplification, positive regulation of SA biosynthesis, and priming to guarantee effective local resistance induction and the establishment of SAR (PubMed:23221596, PubMed:27758894). Converts lysine to alpha-keto-epsilon-aminocaproate, which then can spontaneously cyclize to form delta-(1)-piperideine-2-carboxylate (P2C). P2C is converted to Pip by SARD4 (PubMed:27758894). May produce non-Pip metabolites that play roles in immunity. Involved in the synthesis of distinct metabolite signals that affect basal and early defenses, and later defense responses (PubMed:25372120).

EXTERNAL LINKS

ALD1

Mutations

Mutation(s) distribution

Mutations table