ID   TRPX_ARATH              Reviewed;         621 AA.
AC   P32069; Q56XS1;
DT   01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1993, sequence version 1.
DT   02-SEP-2026, entry version 176.
DE   RecName: Full=Anthranilate synthase alpha subunit 2, chloroplastic;
DE            EC=4.1.3.27;
DE   AltName: Full=Anthranilate synthase component 1-2;
DE   AltName: Full=Anthranilate synthase component I-2;
DE   Flags: Precursor;
GN   Name=ASA2; OrderedLocusNames=At2g29690; ORFNames=T27A16.21;
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].
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=10617197; DOI=10.1038/45471;
RA   Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA   Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA   Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA   Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA   Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA   Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA   Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT   "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL   Nature 402:761-768(1999).
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;
RA   Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA   Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA   Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA   Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA   Shinozaki K.;
RT   "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL   Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
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 (By similarity). {ECO:0000250}.
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   -!- ACTIVITY REGULATION: Feedback inhibition by tryptophan. {ECO:0000250}.
CC   -!- PATHWAY: Amino-acid biosynthesis; L-tryptophan biosynthesis; L-
CC       tryptophan from chorismate: step 1/5.
CC   -!- SUBUNIT: Heterotetramer consisting of two non-identical subunits: a
CC       beta subunit and a large alpha subunit. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the anthranilate synthase component I family.
CC       {ECO:0000305}.
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DR   EMBL; M92354; AAA32739.1; -; Genomic_DNA.
DR   EMBL; AC005496; AAC35228.1; -; Genomic_DNA.
DR   EMBL; CP002685; AEC08294.1; -; Genomic_DNA.
DR   EMBL; OZ408684; CAO7036820.1; -; Genomic_DNA.
DR   EMBL; AK221602; BAD95154.1; -; mRNA.
DR   PIR; JQ1685; JQ1685.
DR   PIR; S27752; S27752.
DR   RefSeq; NP_180530.1; NM_128523.5.
DR   AlphaFoldDB; P32069; -.
DR   SMR; P32069; -.
DR   FunCoup; P32069; 1016.
DR   STRING; 3702.P32069; -.
DR   iPTMnet; P32069; -.
DR   PaxDb; 3702-P32069; -.
DR   ProteomicsDB; 234625; -.
DR   GeneID; 817519; -.
DR   KEGG; ath:AT2G29690; -.
DR   Araport; AT2G29690; -.
DR   TAIR; AT2G29690; ASA2.
DR   eggNOG; KOG1223; Eukaryota.
DR   HOGENOM; CLU_006493_9_3_1; -.
DR   InParanoid; P32069; -.
DR   OMA; GCVGYLD; -.
DR   PhylomeDB; P32069; -.
DR   BioCyc; ARA:AT2G29690-MONOMER; -.
DR   UniPathway; UPA00035; UER00040.
DR   PRO; PR:P32069; -.
DR   Proteomes; UP000006548; Chromosome 2.
DR   ExpressionAtlas; P32069; baseline and differential.
DR   GO; GO:0005950; C:anthranilate synthase complex; NAS:TAIR.
DR   GO; GO:0009507; C:chloroplast; HDA:TAIR.
DR   GO; GO:0005634; C:nucleus; ISM:TAIR.
DR   GO; GO:0004049; F:anthranilate synthase activity; IEA:UniProtKB-EC.
DR   GO; GO:0000162; P:L-tryptophan biosynthetic process; TAS:TIGR.
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:SF9; ANTHRANILATE SYNTHASE COMPONENT 1; 1.
DR   Pfam; PF00425; Chorismate_bind; 1.
DR   PRINTS; PR00095; ANTSNTHASEI.
DR   SUPFAM; SSF56322; ADC synthase; 1.
PE   2: Evidence at transcript level;
KW   Amino-acid biosynthesis; Aromatic amino acid biosynthesis; Chloroplast;
KW   Lyase; Plastid; Reference proteome; Transit peptide;
KW   Tryptophan biosynthesis.
FT   TRANSIT         1..87
FT                   /note="Chloroplast"
FT                   /evidence="ECO:0000255"
FT   CHAIN           88..621
FT                   /note="Anthranilate synthase alpha subunit 2,
FT                   chloroplastic"
FT                   /id="PRO_0000035790"
FT   CONFLICT        85
FT                   /note="F -> L (in Ref. 5; BAD95154)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   621 AA;  69816 MW;  D4039FE58A420967 CRC64;
     MSAVSISAVK SDFFTVEAIA VTHHRTPHPP HFPSLRFPLS LKSPPATSLN LVAGSKLLHF
     SRRLPSIKCS YTPSLDLSEE QFTKFKKASE KGNLVPLFRC VFSDHLTPIL AYRCLVKEDD
     RDAPSFLFES VEPGSQSSNI GRYSVVGAQP TIEIVAKGNV VTVMDHGASL RTEEEVDDPM
     MVPQKIMEEW NPQGIDELPE AFCGGWVGYF SYDTVRYVEK KKLPFSNAPE DDRSLPDVNL
     GLYDDVIVFD HVEKKAYVIH WVRIDKDRSV EENFREGMNR LESLTSRIQD QKPPKMPTGF
     IKLRTQLFGP KLEKSTMTSE AYKEAVVEAK EHILAGDIFQ IVLSQRFERR TFADPFEIYR
     ALRIVNPSPY MAYLQVRGCI LVASSPEILL RSKNRKITNR PLAGTVRRGK TPKEDLMLEK
     ELLSDEKQCA EHIMLVDLGR NDVGKVSKPG SVEVKKLKDI EWFSHVMHIS STVVGELLDH
     LTSWDALRAV LPVGTVSGAP KVKAMELIDE LEVTRRGPYS GGFGGISFNG DMDIALALRT
     MVFPTNTRYD TLYSYKHPQR RREWIAHIQA GAGIVADSNP DDEHRECENK AAALARAIDL
     AESSFLEAPE FTTITPHINN I
//