TRPA1_ARATH
ID TRPA1_ARATH Reviewed; 275 AA.
AC O22765; Q43290;
DT 09-JAN-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1999, sequence version 2.
DT 03-AUG-2022, entry version 148.
DE RecName: Full=Tryptophan synthase alpha chain;
DE EC=4.2.1.20;
DE AltName: Full=Indole synthase;
DE AltName: Full=Indole-3-glycerol-phosphate lyase;
DE EC=4.1.2.8;
GN Name=TRPA1; Synonyms=INS, TSA; OrderedLocusNames=At4g02610;
GN ORFNames=T10P11.11;
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617198; DOI=10.1038/47134;
RA Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA Martienssen R., McCombie W.R.;
RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL Nature 402:769-777(1999).
RN [2]
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=11910074; DOI=10.1126/science.1071006;
RA Seki M., Narusaka M., Kamiya A., Ishida J., Satou M., Sakurai T.,
RA Nakajima M., Enju A., Akiyama K., Oono Y., Muramatsu M., Hayashizaki Y.,
RA Kawai J., Carninci P., Itoh M., Ishii Y., Arakawa T., Shibata K.,
RA Shinagawa A., Shinozaki K.;
RT "Functional annotation of a full-length Arabidopsis cDNA collection.";
RL Science 296:141-145(2002).
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-87.
RC STRAIN=cv. Columbia; TISSUE=Protoplast;
RA Cooke R., Laudie M., Raynal M., Delseny M.;
RT "The Arabidopsis thaliana transcribed genome: the GDR cDNA program.";
RL Submitted (MAR-1996) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND
RP DEVELOPMENTAL STAGE.
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 [7]
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).
CC -!- FUNCTION: The alpha subunit is responsible for the aldol cleavage of
CC indoleglycerol phosphate to indole and glyceraldehyde 3-phosphate (By
CC similarity). Contributes to the tryptophan-independent indole
CC biosynthesis, and possibly to auxin production. {ECO:0000250,
CC ECO:0000269|PubMed:18844775}.
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 Evidence={ECO:0000269|PubMed:18844775};
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:0000269|PubMed:18844775};
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: Cytoplasm {ECO:0000269|PubMed:18844775}.
CC -!- TISSUE SPECIFICITY: Ubiquitously expressed at low levels in seedlings,
CC roots, hypocotyls, cotyledons, stems, leaves, inflorescences, flowers,
CC siliques and seeds. {ECO:0000269|PubMed:18844775}.
CC -!- DEVELOPMENTAL STAGE: Mostly present in vascular tissues. In flowers,
CC expressed in carpels, stamens and pollen.
CC {ECO:0000269|PubMed:18844775}.
CC -!- SIMILARITY: Belongs to the TrpA family. {ECO:0000305}.
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DR EMBL; AC002330; AAC78257.1; -; Genomic_DNA.
DR EMBL; AL161494; CAB80754.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE82204.1; -; Genomic_DNA.
DR EMBL; AK117668; BAC42321.1; -; mRNA.
DR EMBL; BT006097; AAP04082.1; -; mRNA.
DR EMBL; F20005; CAA23378.1; -; mRNA.
DR PIR; T01088; T01088.
DR RefSeq; NP_192170.1; NM_116495.4.
DR AlphaFoldDB; O22765; -.
DR SMR; O22765; -.
DR STRING; 3702.AT4G02610.1; -.
DR PaxDb; O22765; -.
DR PRIDE; O22765; -.
DR ProMEX; O22765; -.
DR ProteomicsDB; 232445; -.
DR EnsemblPlants; AT4G02610.1; AT4G02610.1; AT4G02610.
DR GeneID; 828226; -.
DR Gramene; AT4G02610.1; AT4G02610.1; AT4G02610.
DR KEGG; ath:AT4G02610; -.
DR Araport; AT4G02610; -.
DR TAIR; locus:2132328; AT4G02610.
DR eggNOG; KOG4175; Eukaryota.
DR HOGENOM; CLU_016734_0_2_1; -.
DR InParanoid; O22765; -.
DR OMA; IGCMPAG; -.
DR OrthoDB; 1143233at2759; -.
DR PhylomeDB; O22765; -.
DR BioCyc; ARA:AT4G02610-MON; -.
DR BRENDA; 4.1.2.8; 399.
DR UniPathway; UPA00035; UER00044.
DR PRO; PR:O22765; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; O22765; baseline and differential.
DR Genevisible; O22765; AT.
DR GO; GO:0009507; C:chloroplast; IBA:GO_Central.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0033984; F:indole-3-glycerol-phosphate lyase activity; IDA:UniProtKB.
DR GO; GO:0004834; F:tryptophan synthase activity; IDA:UniProtKB.
DR GO; GO:0009851; P:auxin biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0000162; P:tryptophan biosynthetic process; IBA:GO_Central.
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; Cytoplasm; Lyase; Reference proteome;
KW Tryptophan biosynthesis.
FT CHAIN 1..275
FT /note="Tryptophan synthase alpha chain"
FT /id="PRO_0000420604"
FT ACT_SITE 58
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT ACT_SITE 69
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT CONFLICT 79..80
FT /note="RS -> VP (in Ref. 5; CAA23378)"
FT /evidence="ECO:0000305"
FT CONFLICT 86..87
FT /note="NF -> KL (in Ref. 5; CAA23378)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 275 AA; 29579 MW; BC1A027A1A53FA6A CRC64;
MDLLKTPSST VGLSETFARL KSQGKVALIP YITAGDPDLS TTAKALKVLD SCGSDIIELG
VPYSDPLADG PAIQAAARRS LLKGTNFNSI ISMLKEVIPQ LSCPIALFTY YNPILRRGVE
NYMTVIKNAG VHGLLVPDVP LEETETLRNE ARKHQIELVL LTTPTTPKER MNAIVEASEG
FIYLVSSVGV TGTRESVNEK VQSLLQQIKE ATSKPVAVGF GISKPEHVKQ VAEWGADGVI
VGSAMVKILG ESESPEQGLK ELEFFTKSLK SALVS
