TRPA2_ARATH
ID TRPA2_ARATH Reviewed; 312 AA.
AC Q42529; Q0WWE0; Q8LA83;
DT 09-JAN-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 149.
DE RecName: Full=Tryptophan synthase alpha chain, chloroplastic;
DE EC=4.2.1.20;
DE AltName: Full=Indole-3-glycerol-phosphate lyase, chloroplastic;
DE EC=4.1.2.8 {ECO:0000250|UniProtKB:P42390};
DE AltName: Full=Protein TRYPTOPHAN-REQUIRING 3;
DE Flags: Precursor;
GN Name=TSA1; Synonyms=TRP3, TSA2; OrderedLocusNames=At3g54640;
GN ORFNames=T14E10.210;
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 FUNCTION.
RC STRAIN=cv. Columbia;
RX PubMed=7476868; DOI=10.1007/bf02191705;
RA Radwanski E.R., Zhao J., Last R.L.;
RT "Arabidopsis thaliana tryptophan synthase alpha: gene cloning, expression,
RT and subunit interaction.";
RL Mol. Gen. Genet. 248:657-667(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130713; DOI=10.1038/35048706;
RA Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL Nature 408:820-822(2000).
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;
RA Quinitio C., Chen H., Kim C.J., Shinn P., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (JUN-2006) 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 (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP SUBCELLULAR LOCATION, AND TRANSIT PEPTIDE CLEAVAGE SITE.
RC STRAIN=cv. Columbia;
RX PubMed=7890741; DOI=10.1074/jbc.270.11.6081;
RA Zhao J., Last R.L.;
RT "Immunological characterization and chloroplast localization of the
RT tryptophan biosynthetic enzymes of the flowering plant Arabidopsis
RT thaliana.";
RL J. Biol. Chem. 270:6081-6087(1995).
RN [8]
RP FUNCTION.
RX PubMed=9003322; DOI=10.1007/pl00008602;
RA Radwanski E.R., Barczak A.J., Last R.L.;
RT "Characterization of tryptophan synthase alpha subunit mutants of
RT Arabidopsis thaliana.";
RL Mol. Gen. Genet. 253:353-361(1996).
RN [9]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=9839461; DOI=10.1046/j.1365-313x.1998.00279.x;
RA Rutherford R., Gallois P., Masson P.H.;
RT "Mutations in Arabidopsis thaliana genes involved in the tryptophan
RT biosynthesis pathway affect root waving on tilted agar surfaces.";
RL Plant J. 16:145-154(1998).
RN [10]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=11069706; DOI=10.1046/j.1365-313x.2000.00883.x;
RA Ouyang J., Shao X., Li J.;
RT "Indole-3-glycerol phosphate, a branchpoint of indole-3-acetic acid
RT biosynthesis from the tryptophan biosynthetic pathway in Arabidopsis
RT thaliana.";
RL Plant J. 24:327-333(2000).
RN [11]
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RC STRAIN=cv. Columbia;
RX PubMed=18844775; DOI=10.1111/j.1744-7909.2008.00729.x;
RA Zhang R., Wang B., Ouyang J., Li J., Wang Y.;
RT "Arabidopsis indole synthase, a homolog of tryptophan synthase alpha, is an
RT enzyme involved in the Trp-independent indole-containing metabolite
RT biosynthesis.";
RL J. Integr. Plant Biol. 50:1070-1077(2008).
RN [12]
RP REVIEW.
RX PubMed=18375600; DOI=10.1104/pp.108.115733;
RA Less H., Galili G.;
RT "Principal transcriptional programs regulating plant amino acid metabolism
RT in response to abiotic stresses.";
RL Plant Physiol. 147:316-330(2008).
RN [13]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION [LARGE SCALE
RP ANALYSIS].
RX PubMed=18431481; DOI=10.1371/journal.pone.0001994;
RA Zybailov B., Rutschow H., Friso G., Rudella A., Emanuelsson O., Sun Q.,
RA van Wijk K.J.;
RT "Sorting signals, N-terminal modifications and abundance of the chloroplast
RT proteome.";
RL PLoS ONE 3:E1994-E1994(2008).
CC -!- FUNCTION: The alpha subunit is responsible for the aldol cleavage of
CC indoleglycerol phosphate to indole and glyceraldehyde 3-phosphate.
CC Required for tryptophan biosynthesis. Contributes to the tryptophan-
CC independent indole biosynthesis, and possibly to auxin production.
CC {ECO:0000269|PubMed:11069706, ECO:0000269|PubMed:7476868,
CC ECO:0000269|PubMed:9003322, ECO:0000269|PubMed:9839461}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(1S,2R)-1-C-(indol-3-yl)glycerol 3-phosphate + L-serine = D-
CC glyceraldehyde 3-phosphate + H2O + L-tryptophan;
CC Xref=Rhea:RHEA:10532, ChEBI:CHEBI:15377, ChEBI:CHEBI:33384,
CC ChEBI:CHEBI:57912, ChEBI:CHEBI:58866, ChEBI:CHEBI:59776; EC=4.2.1.20;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(1S,2R)-1-C-(indol-3-yl)glycerol 3-phosphate = D-
CC glyceraldehyde 3-phosphate + indole; Xref=Rhea:RHEA:14081,
CC ChEBI:CHEBI:16881, ChEBI:CHEBI:58866, ChEBI:CHEBI:59776; EC=4.1.2.8;
CC Evidence={ECO:0000250|UniProtKB:P42390};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:14082;
CC Evidence={ECO:0000250|UniProtKB:P42390};
CC -!- PATHWAY: Amino-acid biosynthesis; L-tryptophan biosynthesis; L-
CC tryptophan from chorismate: step 5/5.
CC -!- SUBUNIT: Tetramer of two alpha and two beta chains. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast stroma
CC {ECO:0000269|PubMed:18431481, ECO:0000269|PubMed:18844775,
CC ECO:0000269|PubMed:7890741}.
CC -!- TISSUE SPECIFICITY: Mostly expressed in roots, hypocotyls and leaves,
CC and, to a lower extent, in seedlings, cotyledons, stems,
CC inflorescences, flowers, siliques and seeds.
CC {ECO:0000269|PubMed:18844775}.
CC -!- DISRUPTION PHENOTYPE: Compressed root wave phenotype on tilted agar
CC surfaces. Reduced accumulation of tryptophan, but increased levels of
CC auxin. {ECO:0000269|PubMed:11069706, ECO:0000269|PubMed:9839461}.
CC -!- SIMILARITY: Belongs to the TrpA family. {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; U18993; AAC49117.1; -; Genomic_DNA.
DR EMBL; AL138656; CAB77584.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE79260.1; -; Genomic_DNA.
DR EMBL; BT025875; ABF85777.1; -; mRNA.
DR EMBL; AK226413; BAE98558.1; -; mRNA.
DR EMBL; AY087980; AAM65526.1; -; mRNA.
DR PIR; S59519; S59519.
DR RefSeq; NP_567004.1; NM_115321.4.
DR AlphaFoldDB; Q42529; -.
DR SMR; Q42529; -.
DR STRING; 3702.AT3G54640.1; -.
DR iPTMnet; Q42529; -.
DR PaxDb; Q42529; -.
DR PRIDE; Q42529; -.
DR ProteomicsDB; 232470; -.
DR EnsemblPlants; AT3G54640.1; AT3G54640.1; AT3G54640.
DR GeneID; 824629; -.
DR Gramene; AT3G54640.1; AT3G54640.1; AT3G54640.
DR KEGG; ath:AT3G54640; -.
DR Araport; AT3G54640; -.
DR TAIR; locus:3685290; AT3G54640.
DR eggNOG; KOG4175; Eukaryota.
DR HOGENOM; CLU_016734_0_2_1; -.
DR InParanoid; Q42529; -.
DR OMA; LVMTYWN; -.
DR OrthoDB; 1143233at2759; -.
DR PhylomeDB; Q42529; -.
DR BioCyc; ARA:AT3G54640-MON; -.
DR UniPathway; UPA00035; UER00044.
DR PRO; PR:Q42529; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q42529; baseline and differential.
DR Genevisible; Q42529; AT.
DR GO; GO:0009507; C:chloroplast; IDA:UniProtKB.
DR GO; GO:0009570; C:chloroplast stroma; HDA:TAIR.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0033984; F:indole-3-glycerol-phosphate lyase activity; IEA:UniProtKB-EC.
DR GO; GO:0004834; F:tryptophan synthase activity; IDA:UniProtKB.
DR GO; GO:0009851; P:auxin biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0052544; P:defense response by callose deposition in cell wall; IMP:TAIR.
DR GO; GO:0042742; P:defense response to bacterium; IMP:TAIR.
DR GO; GO:0009630; P:gravitropism; IMP:UniProtKB.
DR GO; GO:0000162; P:tryptophan biosynthetic process; IDA:UniProtKB.
DR CDD; cd04724; Tryptophan_synthase_alpha; 1.
DR Gene3D; 3.20.20.70; -; 1.
DR HAMAP; MF_00131; Trp_synth_alpha; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR011060; RibuloseP-bd_barrel.
DR InterPro; IPR018204; Trp_synthase_alpha_AS.
DR InterPro; IPR002028; Trp_synthase_suA.
DR PANTHER; PTHR43406; PTHR43406; 1.
DR Pfam; PF00290; Trp_syntA; 1.
DR SUPFAM; SSF51366; SSF51366; 1.
DR TIGRFAMs; TIGR00262; trpA; 1.
DR PROSITE; PS00167; TRP_SYNTHASE_ALPHA; 1.
PE 1: Evidence at protein level;
KW Amino-acid biosynthesis; Aromatic amino acid biosynthesis;
KW Auxin biosynthesis; Chloroplast; Lyase; Plastid; Reference proteome;
KW Transit peptide; Tryptophan biosynthesis.
FT TRANSIT 1..40
FT /note="Chloroplast"
FT /evidence="ECO:0000269|PubMed:7890741"
FT CHAIN 41..312
FT /note="Tryptophan synthase alpha chain, chloroplastic"
FT /id="PRO_0000420605"
FT ACT_SITE 96
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT ACT_SITE 107
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT CONFLICT 66
FT /note="F -> C (in Ref. 5; BAE98558)"
FT /evidence="ECO:0000305"
FT CONFLICT 211
FT /note="L -> R (in Ref. 6; AAM65526)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 312 AA; 33200 MW; 0B104A30219A54BF CRC64;
MAIAFKSGVF FLQSPKSQIG FRHSSPPDSS LSFKRFTPMA SLSTSSPTLG LADTFTQLKK
QGKVAFIPYI TAGDPDLSTT AEALKVLDAC GSDIIELGVP YSDPLADGPV IQAAATRSLE
RGTNLDSILE MLDKVVPQIS CPISLFTYYN PILKRGLGKF MSSIRAVGVQ GLVVPDVPLE
ETEMLRKEAL NNDIELVLLT TPTTPTERMK LIVDASEGFI YLVSSIGVTG ARSSVSGKVQ
SLLKDIKEAT DKPVAVGFGI SKPEHVKQIA GWGADGVIVG SAMVKLLGDA KSPTEGLKEL
EKLTKSLKSA LL
