TRPE_ARATH
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 03-AUG-2022, entry version 164.
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; OrderedLocusNames=At5g05730;
GN 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=10.2307/3869530;
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 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 [5]
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 [6]
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 [7]
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 [8]
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 [9]
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 [10]
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 [11]
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 + H(+) + L-glutamate +
CC pyruvate; Xref=Rhea:RHEA:21732, ChEBI:CHEBI:15361, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:16567, ChEBI:CHEBI:29748, ChEBI:CHEBI:29985,
CC 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; 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 IntAct; P32068; 2.
DR STRING; 3702.AT5G05730.2; -.
DR iPTMnet; P32068; -.
DR MetOSite; P32068; -.
DR PaxDb; P32068; -.
DR PRIDE; P32068; -.
DR ProteomicsDB; 232379; -. [P32068-1]
DR EnsemblPlants; AT5G05730.1; AT5G05730.1; AT5G05730. [P32068-1]
DR GeneID; 830457; -.
DR Gramene; AT5G05730.1; AT5G05730.1; AT5G05730. [P32068-1]
DR KEGG; ath:AT5G05730; -.
DR Araport; AT5G05730; -.
DR eggNOG; KOG1223; Eukaryota.
DR HOGENOM; CLU_006493_9_3_1; -.
DR InParanoid; P32068; -.
DR PhylomeDB; P32068; -.
DR BioCyc; ARA:AT5G05730-MON; -.
DR SABIO-RK; P32068; -.
DR UniPathway; UPA00035; UER00040.
DR PRO; PR:P32068; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; P32068; baseline and differential.
DR Genevisible; P32068; AT.
DR GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR GO; GO:0004049; F:anthranilate synthase activity; IDA:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0010600; P:regulation of auxin biosynthetic process; IMP:UniProtKB.
DR GO; GO:0000162; P:tryptophan biosynthetic process; IMP:UniProtKB.
DR Gene3D; 3.60.120.10; -; 1.
DR InterPro; IPR005801; ADC_synthase.
DR InterPro; IPR019999; Anth_synth_I-like.
DR InterPro; IPR006805; Anth_synth_I_N.
DR InterPro; IPR005256; Anth_synth_I_PabB.
DR InterPro; IPR015890; Chorismate_C.
DR PANTHER; PTHR11236; PTHR11236; 1.
DR Pfam; PF04715; Anth_synt_I_N; 1.
DR Pfam; PF00425; Chorismate_bind; 1.
DR PRINTS; PR00095; ANTSNTHASEI.
DR SUPFAM; SSF56322; SSF56322; 1.
DR TIGRFAMs; TIGR00564; trpE_most; 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 6-
FT methylanthranilate."
FT /evidence="ECO:0000269|PubMed:8587994"
FT CONFLICT 59
FT /note="P -> R (in Ref. 4; AY072013)"
FT /evidence="ECO:0000305"
FT CONFLICT 121..123
FT /note="QMS -> LLA (in Ref. 4; 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
