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Tryptophan synthase alpha chain, chloroplastic (EC 4.2.1.20) (Indole-3-glycerol-phosphate lyase, chloroplastic) (EC 4.1.2.8) (Protein TRYPTOPHAN-REQUIRING 3)

 TRPA2_ARATH             Reviewed;         312 AA.
Q42529; Q0WWE0; Q8LA83;
09-JAN-2013, integrated into UniProtKB/Swiss-Prot.
01-NOV-1996, sequence version 1.
25-APR-2018, entry version 133.
RecName: Full=Tryptophan synthase alpha chain, chloroplastic;
EC=4.2.1.20;
AltName: Full=Indole-3-glycerol-phosphate lyase, chloroplastic;
EC=4.1.2.8;
AltName: Full=Protein TRYPTOPHAN-REQUIRING 3;
Flags: Precursor;
Name=TSA1; Synonyms=TRP3, TSA2; OrderedLocusNames=At3g54640;
ORFNames=T14E10.210;
Arabidopsis thaliana (Mouse-ear cress).
Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae;
Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Camelineae;
Arabidopsis.
NCBI_TaxID=3702;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND CATALYTIC ACTIVITY.
STRAIN=cv. Columbia;
PubMed=7476868; DOI=10.1007/BF02191705;
Radwanski E.R., Zhao J., Last R.L.;
"Arabidopsis thaliana tryptophan synthase alpha: gene cloning,
expression, and subunit interaction.";
Mol. Gen. Genet. 248:657-667(1995).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=cv. Columbia;
PubMed=11130713; DOI=10.1038/35048706;
Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M.,
Fartmann B., Valle G., Bloecker H., Perez-Alonso M., Obermaier B.,
Delseny M., Boutry M., Grivell L.A., Mache R., Puigdomenech P.,
De Simone V., Choisne N., Artiguenave F., Robert C., Brottier P.,
Wincker P., Cattolico L., Weissenbach J., Saurin W., Quetier F.,
Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Benes V.,
Wurmbach E., Drzonek H., Erfle H., Jordan N., Bangert S.,
Wiedelmann R., Kranz H., Voss H., Holland R., Brandt P., Nyakatura G.,
Vezzi A., D'Angelo M., Pallavicini A., Toppo S., Simionati B.,
Conrad A., Hornischer K., Kauer G., Loehnert T.-H., Nordsiek G.,
Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J., Climent J.,
Navarro P., Collado C., Perez-Perez A., Ottenwaelder B., Duchemin D.,
Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
Monfort A., Argiriou A., Flores M., Liguori R., Vitale D.,
Mannhaupt G., Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W.,
Mayer K.F.X., Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J.,
Rooney T., Rizzo M., Walts A., Utterback T., Fujii C.Y., Shea T.P.,
Creasy T.H., Haas B., Maiti R., Wu D., Peterson J., Van Aken S.,
Pai G., Militscher J., Sellers P., Gill J.E., Feldblyum T.V.,
Preuss D., Lin X., Nierman W.C., Salzberg S.L., White O., Venter J.C.,
Fraser C.M., Kaneko T., Nakamura Y., Sato S., Kato T., Asamizu E.,
Sasamoto S., Kimura T., Idesawa K., Kawashima K., Kishida Y.,
Kiyokawa C., Kohara M., Matsumoto M., Matsuno A., Muraki A.,
Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
Watanabe A., Yamada M., Yasuda M., Tabata S.;
"Sequence and analysis of chromosome 3 of the plant Arabidopsis
thaliana.";
Nature 408:820-822(2000).
[3]
GENOME REANNOTATION.
STRAIN=cv. Columbia;
PubMed=27862469; DOI=10.1111/tpj.13415;
Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
Town C.D.;
"Araport11: a complete reannotation of the Arabidopsis thaliana
reference genome.";
Plant J. 89:789-804(2017).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=cv. Columbia;
Quinitio C., Chen H., Kim C.J., Shinn P., Ecker J.R.;
"Arabidopsis ORF clones.";
Submitted (JUN-2006) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=cv. Columbia;
Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J.,
Hayashizaki Y., Shinozaki K.;
"Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
Feldmann K.A.;
"Full-length cDNA from Arabidopsis thaliana.";
Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
[7]
SUBCELLULAR LOCATION, AND TRANSIT PEPTIDE CLEAVAGE SITE.
STRAIN=cv. Columbia;
PubMed=7890741; DOI=10.1074/jbc.270.11.6081;
Zhao J., Last R.L.;
"Immunological characterization and chloroplast localization of the
tryptophan biosynthetic enzymes of the flowering plant Arabidopsis
thaliana.";
J. Biol. Chem. 270:6081-6087(1995).
[8]
FUNCTION, AND CATALYTIC ACTIVITY.
PubMed=9003322; DOI=10.1007/s004380050331;
Radwanski E.R., Barczak A.J., Last R.L.;
"Characterization of tryptophan synthase alpha subunit mutants of
Arabidopsis thaliana.";
Mol. Gen. Genet. 253:353-361(1996).
[9]
FUNCTION, AND DISRUPTION PHENOTYPE.
PubMed=9839461; DOI=10.1046/j.1365-313x.1998.00279.x;
Rutherford R., Gallois P., Masson P.H.;
"Mutations in Arabidopsis thaliana genes involved in the tryptophan
biosynthesis pathway affect root waving on tilted agar surfaces.";
Plant J. 16:145-154(1998).
[10]
FUNCTION, AND DISRUPTION PHENOTYPE.
PubMed=11069706; DOI=10.1046/j.1365-313x.2000.00883.x;
Ouyang J., Shao X., Li J.;
"Indole-3-glycerol phosphate, a branchpoint of indole-3-acetic acid
biosynthesis from the tryptophan biosynthetic pathway in Arabidopsis
thaliana.";
Plant J. 24:327-333(2000).
[11]
SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
STRAIN=cv. Columbia;
PubMed=18844775; DOI=10.1111/j.1744-7909.2008.00729.x;
Zhang R., Wang B., Ouyang J., Li J., Wang Y.;
"Arabidopsis indole synthase, a homolog of tryptophan synthase alpha,
is an enzyme involved in the Trp-independent indole-containing
metabolite biosynthesis.";
J. Integr. Plant Biol. 50:1070-1077(2008).
[12]
REVIEW.
PubMed=18375600; DOI=10.1104/pp.108.115733;
Less H., Galili G.;
"Principal transcriptional programs regulating plant amino acid
metabolism in response to abiotic stresses.";
Plant Physiol. 147:316-330(2008).
[13]
IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION [LARGE
SCALE ANALYSIS].
PubMed=18431481; DOI=10.1371/journal.pone.0001994;
Zybailov B., Rutschow H., Friso G., Rudella A., Emanuelsson O.,
Sun Q., van Wijk K.J.;
"Sorting signals, N-terminal modifications and abundance of the
chloroplast proteome.";
PLoS ONE 3:E1994-E1994(2008).
-!- FUNCTION: The alpha subunit is responsible for the aldol cleavage
of indoleglycerol phosphate to indole and glyceraldehyde 3-
phosphate. Required for tryptophan biosynthesis. Contributes to
the tryptophan-independent indole biosynthesis, and possibly to
auxin production. {ECO:0000269|PubMed:11069706,
ECO:0000269|PubMed:7476868, ECO:0000269|PubMed:9003322,
ECO:0000269|PubMed:9839461}.
-!- CATALYTIC ACTIVITY: L-serine + 1-C-(indol-3-yl)glycerol 3-
phosphate = L-tryptophan + D-glyceraldehyde 3-phosphate + H(2)O.
-!- CATALYTIC ACTIVITY: (1S,2R)-1-C-(indol-3-yl)glycerol 3-phosphate =
indole + D-glyceraldehyde 3-phosphate.
-!- PATHWAY: Amino-acid biosynthesis; L-tryptophan biosynthesis; L-
tryptophan from chorismate: step 5/5.
-!- SUBUNIT: Tetramer of two alpha and two beta chains. {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Plastid, chloroplast stroma
{ECO:0000269|PubMed:18431481, ECO:0000269|PubMed:18844775,
ECO:0000269|PubMed:7890741}.
-!- TISSUE SPECIFICITY: Mostly expressed in roots, hypocotyls and
leaves, and, to a lower extent, in seedlings, cotyledons, stems,
inflorescences, flowers, siliques and seeds.
{ECO:0000269|PubMed:18844775}.
-!- DISRUPTION PHENOTYPE: Compressed root wave phenotype on tilted
agar surfaces. Reduced accumulation of tryptophan, but increased
levels of auxin. {ECO:0000269|PubMed:11069706,
ECO:0000269|PubMed:9839461}.
-!- SIMILARITY: Belongs to the TrpA family. {ECO:0000305}.
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EMBL; U18993; AAC49117.1; -; Genomic_DNA.
EMBL; AL138656; CAB77584.1; -; Genomic_DNA.
EMBL; CP002686; AEE79260.1; -; Genomic_DNA.
EMBL; BT025875; ABF85777.1; -; mRNA.
EMBL; AK226413; BAE98558.1; -; mRNA.
EMBL; AY087980; AAM65526.1; -; mRNA.
PIR; S59519; S59519.
RefSeq; NP_567004.1; NM_115321.4.
UniGene; At.24508; -.
ProteinModelPortal; Q42529; -.
SMR; Q42529; -.
STRING; 3702.AT3G54640.1; -.
iPTMnet; Q42529; -.
PaxDb; Q42529; -.
PRIDE; Q42529; -.
EnsemblPlants; AT3G54640.1; AT3G54640.1; AT3G54640.
GeneID; 824629; -.
Gramene; AT3G54640.1; AT3G54640.1; AT3G54640.
KEGG; ath:AT3G54640; -.
Araport; AT3G54640; -.
TAIR; locus:3685290; AT3G54640.
eggNOG; KOG4175; Eukaryota.
eggNOG; COG0159; LUCA.
HOGENOM; HOG000223816; -.
InParanoid; Q42529; -.
KO; K01695; -.
OMA; DYPPEEC; -.
OrthoDB; EOG09360IXC; -.
PhylomeDB; Q42529; -.
BioCyc; ARA:AT3G54640-MONOMER; -.
UniPathway; UPA00035; UER00044.
PRO; PR:Q42529; -.
Proteomes; UP000006548; Chromosome 3.
ExpressionAtlas; Q42529; baseline and differential.
Genevisible; Q42529; AT.
GO; GO:0009507; C:chloroplast; IDA:UniProtKB.
GO; GO:0009570; C:chloroplast stroma; IDA:TAIR.
GO; GO:0033984; F:indole-3-glycerol-phosphate lyase activity; IEA:UniProtKB-EC.
GO; GO:0004834; F:tryptophan synthase activity; IDA:UniProtKB.
GO; GO:0009851; P:auxin biosynthetic process; IEA:UniProtKB-KW.
GO; GO:0052544; P:defense response by callose deposition in cell wall; IMP:TAIR.
GO; GO:0042742; P:defense response to bacterium; IMP:TAIR.
GO; GO:0009630; P:gravitropism; IMP:UniProtKB.
GO; GO:0009735; P:response to cytokinin; IDA:TAIR.
GO; GO:0000162; P:tryptophan biosynthetic process; IDA:UniProtKB.
CDD; cd04724; Tryptophan_synthase_alpha; 1.
Gene3D; 3.20.20.70; -; 1.
HAMAP; MF_00131; Trp_synth_alpha; 1.
InterPro; IPR013785; Aldolase_TIM.
InterPro; IPR011060; RibuloseP-bd_barrel.
InterPro; IPR018204; Trp_synthase_alpha_AS.
InterPro; IPR002028; Trp_synthase_suA.
Pfam; PF00290; Trp_syntA; 1.
SUPFAM; SSF51366; SSF51366; 1.
TIGRFAMs; TIGR00262; trpA; 1.
PROSITE; PS00167; TRP_SYNTHASE_ALPHA; 1.
1: Evidence at protein level;
Amino-acid biosynthesis; Aromatic amino acid biosynthesis;
Auxin biosynthesis; Chloroplast; Complete proteome; Lyase; Plastid;
Reference proteome; Transit peptide; Tryptophan biosynthesis.
TRANSIT 1 40 Chloroplast.
{ECO:0000269|PubMed:7890741}.
CHAIN 41 312 Tryptophan synthase alpha chain,
chloroplastic.
/FTId=PRO_0000420605.
ACT_SITE 96 96 Proton acceptor. {ECO:0000250}.
ACT_SITE 107 107 Proton acceptor. {ECO:0000250}.
CONFLICT 66 66 F -> C (in Ref. 5; BAE98558).
{ECO:0000305}.
CONFLICT 211 211 L -> R (in Ref. 6; AAM65526).
{ECO:0000305}.
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


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