Species	Reference gene ID	Possible function	Papers / DOI
Arabidopsis	At5g05730	Part of a heterotetrameric complex that catalyzes the two- step biosynthesis of anthranilate, an intermediate in the biosynthesis of L-tryptophan.	A Link between ethylene and auxin uncovered by the characterization of two root-specific ethylene-insensitive mutants in Arabidopsis.; 2005; DOI: 10.1105/tpc.105.033365; PMID: 15980261; https://pubmed.ncbi.nlm.nih.gov/15980261/ | Arabidopsis ASA1 is important for jasmonate-mediated regulation of auxin biosynthesis and transport during lateral root formation.; 2009; DOI: 10.1105/tpc.108.064303; PMID: 19435934; https://pubmed.ncbi.nlm.nih.gov/19435934/
Arabidopsis	At2g29690	Part of a heterotetrameric complex that catalyzes the two-step biosynthesis of anthranilate, an intermediate in the biosynthesis of L-tryptophan.	No verified direct reference in this release
Rice	UniProt: A2XNK3	Part of a heterotetrameric complex that catalyzes the two-step biosynthesis of anthranilate, an intermediate in the biosynthesis of L-tryptophan.	No verified direct reference in this release
Rice	Os03g0826500	Part of a heterotetrameric complex that catalyzes the two- step biosynthesis of anthranilate, an intermediate in the biosynthesis of L-tryptophan.	Characterization of rice anthranilate synthase alpha-subunit genes OASA1 and OASA2. Tryptophan accumulation in transgenic rice expressing a feedback-insensitive mutant of OASA1.; 2001; DOI: 10.1104/pp.126.4.1493; PMID: 11500548; https://pubmed.ncbi.nlm.nih.gov/11500548/ | In vitro reconstitution of rice anthranilate synthase: distinct functional properties of the alpha subunits OASA1 and OASA2.; 2004; DOI: 10.1023/b:plan.0000028729.79034.07; PMID: 15159631; https://pubmed.ncbi.nlm.nih.gov/15159631/
Rice	Os03g0264400	Part of a heterotetrameric complex that catalyzes the two- step biosynthesis of anthranilate, an intermediate in the biosynthesis of L-tryptophan.	In vitro reconstitution of rice anthranilate synthase: distinct functional properties of the alpha subunits OASA1 and OASA2.; 2004; DOI: 10.1023/b:plan.0000028729.79034.07; PMID: 15159631; https://pubmed.ncbi.nlm.nih.gov/15159631/