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Protein

Tryptophan synthase alpha chain

Gene

TRPA1

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

The alpha subunit is responsible for the aldol cleavage of indoleglycerol phosphate to indole and glyceraldehyde 3-phosphate (By similarity). Contributes to the tryptophan-independent indole biosynthesis, and possibly to auxin production.By similarity1 Publication

Catalytic activityi

L-serine + 1-C-(indol-3-yl)glycerol 3-phosphate = L-tryptophan + D-glyceraldehyde 3-phosphate + H2O.1 Publication
(1S,2R)-1-C-(indol-3-yl)glycerol 3-phosphate = indole + D-glyceraldehyde 3-phosphate.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei58 – 581Proton acceptorBy similarity
Active sitei69 – 691Proton acceptorBy similarity

GO - Molecular functioni

  • indole-3-glycerol-phosphate lyase activity Source: UniProtKB
  • tryptophan synthase activity Source: UniProtKB

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Lyase

Keywords - Biological processi

Amino-acid biosynthesis, Aromatic amino acid biosynthesis, Auxin biosynthesis, Tryptophan biosynthesis

Enzyme and pathway databases

BioCyciARA:AT4G02610-MONOMER.
BRENDAi4.1.2.8. 399.
UniPathwayiUPA00035; UER00044.

Names & Taxonomyi

Protein namesi
Recommended name:
Tryptophan synthase alpha chain (EC:4.2.1.20)
Alternative name(s):
Indole synthase
Indole-3-glycerol-phosphate lyase (EC:4.1.2.8)
Gene namesi
Name:TRPA1
Synonyms:INS, TSA
Ordered Locus Names:At4g02610
ORF Names:T10P11.11
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
Proteomesi
  • UP000006548 Componenti: Chromosome 4

Organism-specific databases

TAIRiAT4G02610.

Subcellular locationi

  • Cytoplasm 1 Publication

GO - Cellular componenti

  • cytoplasm Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 275275Tryptophan synthase alpha chainPRO_0000420604Add
BLAST

Proteomic databases

PaxDbiO22765.
PRIDEiO22765.
ProMEXiO22765.

Expressioni

Tissue specificityi

Ubiquitously expressed at low levels in seedlings, roots, hypocotyls, cotyledons, stems, leaves, inflorescences, flowers, siliques and seeds.1 Publication

Developmental stagei

Mostly present in vascular tissues. In flowers, expressed in carpels, stamens and pollen.1 Publication

Gene expression databases

GenevisibleiO22765. AT.

Interactioni

Subunit structurei

Tetramer of two alpha and two beta chains.By similarity

Protein-protein interaction databases

STRINGi3702.AT4G02610.1.

Structurei

3D structure databases

ProteinModelPortaliO22765.
SMRiO22765. Positions 13-273.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the TrpA family.Curated

Phylogenomic databases

eggNOGiKOG4175. Eukaryota.
COG0159. LUCA.
HOGENOMiHOG000223816.
InParanoidiO22765.
KOiK01695.
OMAiDYNPHIP.
PhylomeDBiO22765.

Family and domain databases

Gene3Di3.20.20.70. 1 hit.
HAMAPiMF_00131. Trp_synth_alpha.
InterProiIPR013785. Aldolase_TIM.
IPR011060. RibuloseP-bd_barrel.
IPR018204. Trp_synthase_alpha_AS.
IPR002028. Trp_synthase_suA.
[Graphical view]
PfamiPF00290. Trp_syntA. 1 hit.
[Graphical view]
SUPFAMiSSF51366. SSF51366. 1 hit.
TIGRFAMsiTIGR00262. trpA. 1 hit.
PROSITEiPS00167. TRP_SYNTHASE_ALPHA. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

O22765-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MDLLKTPSST VGLSETFARL KSQGKVALIP YITAGDPDLS TTAKALKVLD
60 70 80 90 100
SCGSDIIELG VPYSDPLADG PAIQAAARRS LLKGTNFNSI ISMLKEVIPQ
110 120 130 140 150
LSCPIALFTY YNPILRRGVE NYMTVIKNAG VHGLLVPDVP LEETETLRNE
160 170 180 190 200
ARKHQIELVL LTTPTTPKER MNAIVEASEG FIYLVSSVGV TGTRESVNEK
210 220 230 240 250
VQSLLQQIKE ATSKPVAVGF GISKPEHVKQ VAEWGADGVI VGSAMVKILG
260 270
ESESPEQGLK ELEFFTKSLK SALVS
Length:275
Mass (Da):29,579
Last modified:January 1, 1999 - v2
Checksum:iBC1A027A1A53FA6A
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti79 – 802RS → VP in CAA23378 (Ref. 5) Curated
Sequence conflicti86 – 872NF → KL in CAA23378 (Ref. 5) Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AC002330 Genomic DNA. Translation: AAC78257.1.
AL161494 Genomic DNA. Translation: CAB80754.1.
CP002687 Genomic DNA. Translation: AEE82204.1.
AK117668 mRNA. Translation: BAC42321.1.
BT006097 mRNA. Translation: AAP04082.1.
F20005 mRNA. Translation: CAA23378.1.
PIRiT01088.
RefSeqiNP_192170.1. NM_116495.3.
UniGeneiAt.48825.
At.68477.

Genome annotation databases

EnsemblPlantsiAT4G02610.1; AT4G02610.1; AT4G02610.
GeneIDi828226.
GrameneiAT4G02610.1; AT4G02610.1; AT4G02610.
KEGGiath:AT4G02610.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AC002330 Genomic DNA. Translation: AAC78257.1.
AL161494 Genomic DNA. Translation: CAB80754.1.
CP002687 Genomic DNA. Translation: AEE82204.1.
AK117668 mRNA. Translation: BAC42321.1.
BT006097 mRNA. Translation: AAP04082.1.
F20005 mRNA. Translation: CAA23378.1.
PIRiT01088.
RefSeqiNP_192170.1. NM_116495.3.
UniGeneiAt.48825.
At.68477.

3D structure databases

ProteinModelPortaliO22765.
SMRiO22765. Positions 13-273.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi3702.AT4G02610.1.

Proteomic databases

PaxDbiO22765.
PRIDEiO22765.
ProMEXiO22765.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsiAT4G02610.1; AT4G02610.1; AT4G02610.
GeneIDi828226.
GrameneiAT4G02610.1; AT4G02610.1; AT4G02610.
KEGGiath:AT4G02610.

Organism-specific databases

TAIRiAT4G02610.

Phylogenomic databases

eggNOGiKOG4175. Eukaryota.
COG0159. LUCA.
HOGENOMiHOG000223816.
InParanoidiO22765.
KOiK01695.
OMAiDYNPHIP.
PhylomeDBiO22765.

Enzyme and pathway databases

UniPathwayiUPA00035; UER00044.
BioCyciARA:AT4G02610-MONOMER.
BRENDAi4.1.2.8. 399.

Miscellaneous databases

PROiO22765.

Gene expression databases

GenevisibleiO22765. AT.

Family and domain databases

Gene3Di3.20.20.70. 1 hit.
HAMAPiMF_00131. Trp_synth_alpha.
InterProiIPR013785. Aldolase_TIM.
IPR011060. RibuloseP-bd_barrel.
IPR018204. Trp_synthase_alpha_AS.
IPR002028. Trp_synthase_suA.
[Graphical view]
PfamiPF00290. Trp_syntA. 1 hit.
[Graphical view]
SUPFAMiSSF51366. SSF51366. 1 hit.
TIGRFAMsiTIGR00262. trpA. 1 hit.
PROSITEiPS00167. TRP_SYNTHASE_ALPHA. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana."
    Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T., Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B., Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M., de Simone V., Obermaier B.
    , Mache R., Mueller M., Kreis M., Delseny M., Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D., Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J., Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B., Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J., Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R., Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M., Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P., Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S., Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C., Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J., Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S., Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A., Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M., Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D., Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E., Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S., Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R., Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M., Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E., Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P., Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K., Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K., de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K., Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M., Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G., Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K., Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K., Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W., Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H., Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B., Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J., Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K., O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N., Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A., Martienssen R., McCombie W.R.
    Nature 402:769-777(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: cv. Columbia.
  2. The Arabidopsis Information Resource (TAIR)
    Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
    Cited for: GENOME REANNOTATION.
    Strain: cv. Columbia.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: cv. Columbia.
  4. "Empirical analysis of transcriptional activity in the Arabidopsis genome."
    Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G.
    , Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.
    Science 302:842-846(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: cv. Columbia.
  5. "The Arabidopsis thaliana transcribed genome: the GDR cDNA program."
    Cooke R., Laudie M., Raynal M., Delseny M.
    Submitted (MAR-1996) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-87.
    Strain: cv. Columbia.
    Tissue: Protoplast.
  6. "Arabidopsis indole synthase, a homolog of tryptophan synthase alpha, is an enzyme involved in the Trp-independent indole-containing metabolite biosynthesis."
    Zhang R., Wang B., Ouyang J., Li J., Wang Y.
    J. Integr. Plant Biol. 50:1070-1077(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
    Strain: cv. Columbia.
  7. "Principal transcriptional programs regulating plant amino acid metabolism in response to abiotic stresses."
    Less H., Galili G.
    Plant Physiol. 147:316-330(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVIEW.

Entry informationi

Entry nameiTRPA1_ARATH
AccessioniPrimary (citable) accession number: O22765
Secondary accession number(s): Q43290
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 9, 2013
Last sequence update: January 1, 1999
Last modified: February 17, 2016
This is version 122 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Arabidopsis thaliana
    Arabidopsis thaliana: entries and gene names
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.