ID TRPE_ARATH Reviewed; 595 AA. AC P32068; DT 01-OCT-1993, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-1993, sequence version 1. DT 02-SEP-2026, entry version 180. DE RecName: Full=Anthranilate synthase alpha subunit 1, chloroplastic {ECO:0000303|PubMed:7972519}; DE EC=4.1.3.27 {ECO:0000269|PubMed:7972519}; DE AltName: Full=Anthranilate synthase component 1-1; DE AltName: Full=Anthranilate synthase component I-1; DE AltName: Full=Protein A-METHYL TRYPTOPHAN RESISTANT 1; DE AltName: Full=Protein JASMONATE-INDUCED DEFECTIVE LATERAL ROOT 1; DE AltName: Full=Protein TRYPTOPHAN BIOSYNTHESIS 5; DE AltName: Full=Protein WEAK ETHYLENE INSENSITIVE 2; DE Flags: Precursor; GN Name=ASA1; Synonyms=AMT1, JDL1, TRP5, WEI2; GN OrderedLocusNames=At5g05730; ORFNames=MJJ3.14; OS Arabidopsis thaliana (Mouse-ear cress). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae; OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis. OX NCBI_TaxID=3702; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND INDUCTION. RX PubMed=1392592; DOI=10.1105/tpc.4.6.721; RA Niyogi K.K., Fink G.R.; RT "Two anthranilate synthase genes in Arabidopsis: defense-related regulation RT of the tryptophan pathway."; RL Plant Cell 4:721-733(1992). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=cv. Columbia; RX PubMed=9330910; DOI=10.1093/dnares/4.3.215; RA Sato S., Kotani H., Nakamura Y., Kaneko T., Asamizu E., Fukami M., RA Miyajima N., Tabata S.; RT "Structural analysis of Arabidopsis thaliana chromosome 5. I. Sequence RT features of the 1.6 Mb regions covered by twenty physically assigned P1 RT clones."; RL DNA Res. 4:215-230(1997). RN [3] RP GENOME REANNOTATION. RC STRAIN=cv. Columbia; RX PubMed=27862469; DOI=10.1111/tpj.13415; RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S., RA Town C.D.; RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference RT genome."; RL Plant J. 89:789-804(2017). RN [4] RP GENOME REANNOTATION. RC STRAIN=cv. Columbia; RG The Arabidopsis Information Resource (TAIR); RT "Community-consensus reference genome of Arabidopsis thaliana Col-0."; RL Submitted (FEB-2026) to the EMBL/GenBank/DDBJ databases. RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=cv. Columbia; RX PubMed=14593172; DOI=10.1126/science.1088305; RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M., RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G., RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L., RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C., RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J., RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A., RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C., RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X., RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M., RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K., RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A., RA Ecker J.R.; RT "Empirical analysis of transcriptional activity in the Arabidopsis RT genome."; RL Science 302:842-846(2003). RN [6] RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND PATHWAY. RX PubMed=7972519; DOI=10.1104/pp.106.1.353; RA Bernasconi P., Walters E.W., Woodworth A.R., Siehl D.L., Stone T.E., RA Subramanian M.V.; RT "Functional expression of Arabidopsis thaliana anthranilate synthase RT subunit I in Escherichia coli."; RL Plant Physiol. 106:353-358(1994). RN [7] RP FUNCTION, ACTIVITY REGULATION, MUTAGENESIS OF ASP-341, AND DISRUPTION RP PHENOTYPE. RX PubMed=8587994; DOI=10.1104/pp.110.1.51; RA Li J., Last R.L.; RT "The Arabidopsis thaliana trp5 mutant has a feedback-resistant anthranilate RT synthase and elevated soluble tryptophan."; RL Plant Physiol. 110:51-59(1996). RN [8] RP FUNCTION, AND DISRUPTION PHENOTYPE. RX PubMed=8934623; DOI=10.1104/pp.110.4.1159; RA Kreps J.A., Ponappa T., Dong W., Town C.D.; RT "Molecular basis of alpha-methyltryptophan resistance in amt-1, a mutant of RT Arabidopsis thaliana with altered tryptophan metabolism."; RL Plant Physiol. 110:1159-1165(1996). RN [9] RP FUNCTION, INDUCTION BY ETHYLENE, AND DISRUPTION PHENOTYPE. RX PubMed=15980261; DOI=10.1105/tpc.105.033365; RA Stepanova A.N., Hoyt J.M., Hamilton A.A., Alonso J.M.; RT "A link between ethylene and auxin uncovered by the characterization of two RT root-specific ethylene-insensitive mutants in Arabidopsis."; RL Plant Cell 17:2230-2242(2005). RN [10] RP TISSUE SPECIFICITY. RX PubMed=18435826; DOI=10.1111/j.1365-313x.2008.03528.x; RA Ivanchenko M.G., Muday G.K., Dubrovsky J.G.; RT "Ethylene-auxin interactions regulate lateral root initiation and emergence RT in Arabidopsis thaliana."; RL Plant J. 55:335-347(2008). RN [11] RP FUNCTION, INDUCTION BY METHYL JASMONATE, AND DISRUPTION PHENOTYPE. RX PubMed=19435934; DOI=10.1105/tpc.108.064303; RA Sun J., Xu Y., Ye S., Jiang H., Chen Q., Liu F., Zhou W., Chen R., Li X., RA Tietz O., Wu X., Cohen J.D., Palme K., Li C.; RT "Arabidopsis ASA1 is important for jasmonate-mediated regulation of auxin RT biosynthesis and transport during lateral root formation."; RL Plant Cell 21:1495-1511(2009). RN [12] RP ACETYLATION [LARGE SCALE ANALYSIS] AT VAL-55, CLEAVAGE OF TRANSIT PEPTIDE RP [LARGE SCALE ANALYSIS] AFTER CYS-54, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=22223895; DOI=10.1074/mcp.m111.015131; RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., RA Giglione C.; RT "Comparative large-scale characterisation of plant vs. mammal proteins RT reveals similar and idiosyncratic N-alpha acetylation features."; RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012). CC -!- FUNCTION: Part of a heterotetrameric complex that catalyzes the two- CC step biosynthesis of anthranilate, an intermediate in the biosynthesis CC of L-tryptophan. In the first step, the glutamine-binding beta subunit CC of anthranilate synthase (AS) provides the glutamine amidotransferase CC activity which generates ammonia as a substrate that, along with CC chorismate, is used in the second step, catalyzed by the large alpha CC subunit of AS to produce anthranilate. Plays an important regulatory CC role in auxin production via the tryptophan-dependent biosynthetic CC pathway. {ECO:0000269|PubMed:15980261, ECO:0000269|PubMed:19435934, CC ECO:0000269|PubMed:7972519, ECO:0000269|PubMed:8587994, CC ECO:0000269|PubMed:8934623}. CC -!- CATALYTIC ACTIVITY: CC Reaction=chorismate + L-glutamine = anthranilate + pyruvate + L- CC glutamate + H(+); Xref=Rhea:RHEA:21732, ChEBI:CHEBI:15361, CC ChEBI:CHEBI:15378, ChEBI:CHEBI:16567, ChEBI:CHEBI:29748, CC ChEBI:CHEBI:29985, ChEBI:CHEBI:58359; EC=4.1.3.27; CC Evidence={ECO:0000269|PubMed:7972519}; CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:21734; CC Evidence={ECO:0000269|PubMed:7972519}; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000250|UniProtKB:P00897}; CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000250|UniProtKB:P00897}; CC -!- ACTIVITY REGULATION: Feedback inhibition by tryptophan. CC {ECO:0000269|PubMed:8587994}. CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Kinetic parameters: CC KM=180 uM for chorismate {ECO:0000269|PubMed:7972519}; CC Vmax=45 nmol/min/mg enzyme toward chorismate CC {ECO:0000269|PubMed:7972519}; CC -!- PATHWAY: Amino-acid biosynthesis; L-tryptophan biosynthesis; L- CC tryptophan from chorismate: step 1/5. {ECO:0000269|PubMed:7972519}. CC -!- SUBUNIT: Heterotetramer consisting of two non-identical subunits: a CC beta subunit and a large alpha subunit. {ECO:0000250}. CC -!- INTERACTION: CC P32068; Q9LEZ3: BIM1; NbExp=3; IntAct=EBI-25514634, EBI-617095; CC P32068; Q9C5K8: TIFY3B; NbExp=3; IntAct=EBI-25514634, EBI-2312231; CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000305}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=1; CC Comment=A number of isoforms are produced. According to EST CC sequences.; CC Name=1; CC IsoId=P32068-1; Sequence=Displayed; CC -!- TISSUE SPECIFICITY: Expressed in the central cylinder of mature primary CC root zones, including pericycle and early lateral root primordia, and CC vasculature of cotyledons. {ECO:0000269|PubMed:18435826}. CC -!- INDUCTION: By ethylene, methyl jasmonate (MeJa), wounding and infection CC by a virulent strain of P.syringae pv maculicola. CC {ECO:0000269|PubMed:1392592, ECO:0000269|PubMed:15980261, CC ECO:0000269|PubMed:19435934}. CC -!- DISRUPTION PHENOTYPE: No visible phenotype under normal growth CC conditions, but mutant plants are insensitive to inhibition of root CC elongation by ethylene, resistant to the herbicide and anthranilate CC analog 6-methylanthranilate, resistant to growth inhibition by the CC tryptophan analog alpha-methyltryptophan and insensitive to feedback CC inhibition by tryptophan. {ECO:0000269|PubMed:15980261, CC ECO:0000269|PubMed:19435934, ECO:0000269|PubMed:8587994, CC ECO:0000269|PubMed:8934623}. CC -!- SIMILARITY: Belongs to the anthranilate synthase component I family. CC {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=AY072013; Type=Frameshift; Evidence={ECO:0000305}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; M92353; AAA32738.1; -; Genomic_DNA. DR EMBL; AB005237; BAB09667.1; -; Genomic_DNA. DR EMBL; CP002688; AED90915.1; -; Genomic_DNA. DR EMBL; OZ408687; CAO7051189.1; -; Genomic_DNA. DR EMBL; AY072013; -; NOT_ANNOTATED_CDS; mRNA. DR PIR; JQ1684; JQ1684. DR RefSeq; NP_196192.1; NM_120655.4. [P32068-1] DR AlphaFoldDB; P32068; -. DR SMR; P32068; -. DR BioGRID; 15736; 3. DR FunCoup; P32068; 610. DR IntAct; P32068; 2. DR STRING; 3702.P32068; -. DR iPTMnet; P32068; -. DR MetOSite; P32068; -. DR PaxDb; 3702-P32068; -. DR ProteomicsDB; 232379; -. [P32068-1] DR GeneID; 830457; -. DR KEGG; ath:AT5G05730; -. DR Araport; AT5G05730; -. DR TAIR; AT5G05730; ASA1. DR eggNOG; KOG1223; Eukaryota. DR HOGENOM; CLU_006493_9_3_1; -. DR InParanoid; P32068; -. DR PhylomeDB; P32068; -. DR BioCyc; ARA:AT5G05730-MONOMER; -. DR SABIO-RK; P32068; -. DR UniPathway; UPA00035; UER00040. DR PRO; PR:P32068; -. DR Proteomes; UP000006548; Chromosome 5. DR ExpressionAtlas; P32068; baseline and differential. DR GO; GO:0005950; C:anthranilate synthase complex; NAS:TAIR. DR GO; GO:0009507; C:chloroplast; HDA:TAIR. DR GO; GO:0009570; C:chloroplast stroma; HDA:TAIR. DR GO; GO:0004049; F:anthranilate synthase activity; IDA:UniProtKB. DR GO; GO:0009851; P:auxin biosynthetic process; IGI:TAIR. DR GO; GO:0000162; P:L-tryptophan biosynthetic process; IMP:UniProtKB. DR GO; GO:0010311; P:lateral root formation; IMP:TAIR. DR GO; GO:0010600; P:regulation of auxin biosynthetic process; IMP:UniProtKB. DR GO; GO:0009617; P:response to bacterium; IEP:TIGR. DR GO; GO:0009723; P:response to ethylene; IGI:TAIR. DR GO; GO:0009611; P:response to wounding; IEP:TAIR. DR FunFam; 3.60.120.10:FF:000003; Anthranilate synthase component 1; 1. DR Gene3D; 3.60.120.10; Anthranilate synthase; 1. DR InterPro; IPR005801; ADC_synthase. DR InterPro; IPR015890; Anth_synth-like_dom. DR InterPro; IPR019999; Anth_synth_I-like. DR InterPro; IPR005256; Anth_synth_I_PabB. DR NCBIfam; TIGR00564; trpE_most; 1. DR PANTHER; PTHR11236; AMINOBENZOATE/ANTHRANILATE SYNTHASE; 1. DR PANTHER; PTHR11236:SF33; ANTHRANILATE SYNTHASE ALPHA SUBUNIT 1, CHLOROPLASTIC-RELATED; 1. DR Pfam; PF00425; Chorismate_bind; 1. DR PRINTS; PR00095; ANTSNTHASEI. DR SUPFAM; SSF56322; ADC synthase; 1. PE 1: Evidence at protein level; KW Acetylation; Alternative splicing; Amino-acid biosynthesis; KW Aromatic amino acid biosynthesis; Chloroplast; Lyase; Magnesium; KW Metal-binding; Plastid; Reference proteome; Transit peptide; KW Tryptophan biosynthesis. FT TRANSIT 1..54 FT /note="Chloroplast" FT /evidence="ECO:0007744|PubMed:22223895" FT CHAIN 55..595 FT /note="Anthranilate synthase alpha subunit 1, FT chloroplastic" FT /id="PRO_0000035789" FT BINDING 115 FT /ligand="L-tryptophan" FT /ligand_id="ChEBI:CHEBI:57912" FT /evidence="ECO:0000250|UniProtKB:P00897" FT BINDING 356..358 FT /ligand="L-tryptophan" FT /ligand_id="ChEBI:CHEBI:57912" FT /evidence="ECO:0000250|UniProtKB:P00897" FT BINDING 391..392 FT /ligand="chorismate" FT /ligand_id="ChEBI:CHEBI:29748" FT /evidence="ECO:0000250|UniProtKB:P00897" FT BINDING 418 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000250|UniProtKB:P00897" FT BINDING 506 FT /ligand="chorismate" FT /ligand_id="ChEBI:CHEBI:29748" FT /evidence="ECO:0000250|UniProtKB:P00897" FT BINDING 526 FT /ligand="chorismate" FT /ligand_id="ChEBI:CHEBI:29748" FT /evidence="ECO:0000250|UniProtKB:P00897" FT BINDING 558..560 FT /ligand="chorismate" FT /ligand_id="ChEBI:CHEBI:29748" FT /evidence="ECO:0000250|UniProtKB:P00897" FT BINDING 560 FT /ligand="chorismate" FT /ligand_id="ChEBI:CHEBI:29748" FT /evidence="ECO:0000250|UniProtKB:P00897" FT BINDING 573 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000250|UniProtKB:P00897" FT MOD_RES 55 FT /note="N-acetylvaline" FT /evidence="ECO:0007744|PubMed:22223895" FT MUTAGEN 341 FT /note="D->N: In trp5-1; insensitive to feedback inhibition FT by tryptophan and resistance to the herbicide FT 6-methylanthranilate." FT /evidence="ECO:0000269|PubMed:8587994" FT CONFLICT 59 FT /note="P -> R (in Ref. 5; AY072013)" FT /evidence="ECO:0000305" FT CONFLICT 121..123 FT /note="QMS -> LLA (in Ref. 5; AY072013)" FT /evidence="ECO:0000305" SQ SEQUENCE 595 AA; 66312 MW; 674175416A2726F0 CRC64; MSSSMNVATM QALTFSRRLL PSVASRYLSS SSVTVTGYSG RSSAYAPSFR SIKCVSVSPE ASIVSDTKKL ADASKSTNLI PIYRCIFSDQ LTPVLAYRCL VKEDDREAPS FLFESVEPGS QMSSVGRYSV VGAQPAMEIV AKENKVIVMD HNNETMTEEF VEDPMEIPRK ISEKWNPDPQ LVQDLPDAFC GGWVGFFSYD TVRYVEKRKL PFSKAPEDDR NLPDMHLGLY DDVVVFDHVE KKAYVIHWIR LDGSLPYEKA YSNGMQHLEN LVAKLHDIEP PKLAAGNVNL QTRQFGPSLD NSNVTCEEYK EAVVKAKEHI LAGDIFQIVL SQRFERRTFA DPFEVYRALR VVNPSPYMGY LQARGCILVA SSPEILTKVK QNKIVNRPLA GTSKRGKNEV EDKRLEKELL ENEKQCAEHI MLVDLGRNDV GKVTKYGSVK VEKLMNIERY SHVMHISSTV TGELQDGLTC WDVLRAALPV GTVSGAPKVK AMELIDELEP TRRGPYSGGF GGVSFTGDMD IALSLRTIVF PTACQYNTMY SYKDANKRRE WVAYLQAGAG VVADSDPQDE HCECQNKAAG LARAIDLAES AFVKK //