Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Tryptophan synthase beta chain 2, chloroplastic

Gene

TSB2

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

Functioni

The beta subunit is responsible for the synthesis of L-tryptophan from indole and L-serine.

Catalytic activityi

L-serine + 1-C-(indol-3-yl)glycerol 3-phosphate = L-tryptophan + D-glyceraldehyde 3-phosphate + H2O.

Cofactori

Pathwayi: L-tryptophan biosynthesis

This protein is involved in step 5 of the subpathway that synthesizes L-tryptophan from chorismate.
Proteins known to be involved in the 5 steps of the subpathway in this organism are:
  1. Anthranilate synthase beta subunit 2, chloroplastic (ASB2), Anthranilate synthase beta subunit 1, chloroplastic (ASB1), Anthranilate synthase alpha subunit 1, chloroplastic (ASA1), Anthranilate synthase alpha subunit 2, chloroplastic (ASA2)
  2. Anthranilate phosphoribosyltransferase, chloroplastic (PAT1)
  3. N-(5'-phosphoribosyl)anthranilate isomerase 2, chloroplastic (PAI2), N-(5'-phosphoribosyl)anthranilate isomerase 3, chloroplastic (PAI3), N-(5'-phosphoribosyl)anthranilate isomerase 1, chloroplastic (PAI1)
  4. Indole-3-glycerol phosphate synthase, chloroplastic (IGPS)
  5. Tryptophan synthase alpha chain (TRPA1), Tryptophan synthase alpha chain, chloroplastic (TSA1), Tryptophan synthase beta chain 1, chloroplastic (TSB1), Tryptophan synthase beta chain 2, chloroplastic (TSB2)
This subpathway is part of the pathway L-tryptophan biosynthesis, which is itself part of Amino-acid biosynthesis.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes L-tryptophan from chorismate, the pathway L-tryptophan biosynthesis and in Amino-acid biosynthesis.

GO - Molecular functioni

  • pyridoxal phosphate binding Source: GO_Central
  • tryptophan synthase activity Source: TAIR

GO - Biological processi

  • tryptophan biosynthetic process Source: TAIR
Complete GO annotation...

Keywords - Molecular functioni

Lyase

Keywords - Biological processi

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

Keywords - Ligandi

Pyridoxal phosphate

Enzyme and pathway databases

BioCyciARA:AT4G27070-MONOMER.
UniPathwayiUPA00035; UER00044.

Names & Taxonomyi

Protein namesi
Recommended name:
Tryptophan synthase beta chain 2, chloroplastic (EC:4.2.1.20)
Gene namesi
Name:TSB2
Ordered Locus Names:At4g27070
ORF Names:T24A18.20
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
Proteomesi
  • UP000006548 Componenti: Chromosome 4

Organism-specific databases

TAIRiAT4G27070.

Subcellular locationi

GO - Cellular componenti

  • chloroplast envelope Source: TAIR
  • chloroplast stroma Source: TAIR
Complete GO annotation...

Keywords - Cellular componenti

Chloroplast, Plastid

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 5151ChloroplastCombined sourcesAdd
BLAST
Chaini52 – 475424Tryptophan synthase beta chain 2, chloroplasticPRO_0000035784Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei52 – 521N-acetylthreonineCombined sources
Modified residuei170 – 1701N6-(pyridoxal phosphate)lysineBy similarity

Keywords - PTMi

Acetylation

Proteomic databases

PaxDbiP25269.
PRIDEiP25269.

Expressioni

Gene expression databases

ExpressionAtlasiP25269. baseline and differential.
GenevisibleiP25269. AT.

Interactioni

Subunit structurei

Tetramer of two alpha and two beta chains.

Protein-protein interaction databases

BioGridi14102. 1 interaction.
STRINGi3702.AT4G27070.1.

Structurei

3D structure databases

ProteinModelPortaliP25269.
SMRiP25269. Positions 86-471.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the TrpB family.Curated

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiKOG1395. Eukaryota.
COG0133. LUCA.
HOGENOMiHOG000161710.
InParanoidiP25269.
KOiK01696.
OMAiNVYRMRM.
PhylomeDBiP25269.

Family and domain databases

HAMAPiMF_00133. Trp_synth_beta.
InterProiIPR006653. Trp_synth_b_CS.
IPR006654. Trp_synth_beta.
IPR023026. Trp_synth_beta/beta-like.
IPR001926. TrpB-like_PLP-dep.
[Graphical view]
PfamiPF00291. PALP. 1 hit.
[Graphical view]
PIRSFiPIRSF001413. Trp_syn_beta. 1 hit.
SUPFAMiSSF53686. SSF53686. 1 hit.
TIGRFAMsiTIGR00263. trpB. 1 hit.
PROSITEiPS00168. TRP_SYNTHASE_BETA. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P25269-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MATASTAATF RPSSVSASSE LTHLRSPSKL PKFTPLPSAR SRSSSSFSVS
60 70 80 90 100
CTIAKDPAVV MADSEKIKAA GSDPTMWQRP DSFGRFGKFG GKYVPETLMH
110 120 130 140 150
ALSELETAFY SLATDEDFQR ELAEILKDYV GRESPLYFAE RLTEHYRREN
160 170 180 190 200
GEGPLIYLKR EDLNHTGAHK INNAVAQALL AKRLGKKRII AETGAGQHGV
210 220 230 240 250
ATATVCARFG LQCIIYMGAQ DMERQALNVF RMRLLGAEVR GVHSGTATLK
260 270 280 290 300
DATSEAIRDW VTNVETTHYI LGSVAGPHPY PMMVRDFHAV IGKETRKQAM
310 320 330 340 350
EKWGGKPDVL VACVGGGSNA MGLFHEFVDD TEVRMIGVEA AGFGLDSGKH
360 370 380 390 400
AATLTKGDVG VLHGAMSYLL QDDDGQIIEP HSISAGLDYP GVGPEHSFLK
410 420 430 440 450
DVGRAEYFSV TDEEALEAFK RVSRLEGIIP ALETSHALAH LEKLCPTLPD
460 470
GARVVLNFSG RGDKDVQTAI KYLEV
Length:475
Mass (Da):51,601
Last modified:November 1, 1995 - v2
Checksum:i1222EDA3B4CDBEEB
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M81620 Genomic DNA. Translation: AAA32879.1.
AL035680 Genomic DNA. Translation: CAB38837.1.
AL161566 Genomic DNA. Translation: CAB79562.1.
CP002687 Genomic DNA. Translation: AEE85296.1.
BT003144 mRNA. Translation: AAO24576.1.
AY084334 mRNA. Translation: AAM60917.1.
PIRiJQ1073.
T06037.
RefSeqiNP_194437.1. NM_118841.4.
UniGeneiAt.327.

Genome annotation databases

EnsemblPlantsiAT4G27070.1; AT4G27070.1; AT4G27070.
GeneIDi828815.
GrameneiAT4G27070.1; AT4G27070.1; AT4G27070.
KEGGiath:AT4G27070.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M81620 Genomic DNA. Translation: AAA32879.1.
AL035680 Genomic DNA. Translation: CAB38837.1.
AL161566 Genomic DNA. Translation: CAB79562.1.
CP002687 Genomic DNA. Translation: AEE85296.1.
BT003144 mRNA. Translation: AAO24576.1.
AY084334 mRNA. Translation: AAM60917.1.
PIRiJQ1073.
T06037.
RefSeqiNP_194437.1. NM_118841.4.
UniGeneiAt.327.

3D structure databases

ProteinModelPortaliP25269.
SMRiP25269. Positions 86-471.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi14102. 1 interaction.
STRINGi3702.AT4G27070.1.

Proteomic databases

PaxDbiP25269.
PRIDEiP25269.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsiAT4G27070.1; AT4G27070.1; AT4G27070.
GeneIDi828815.
GrameneiAT4G27070.1; AT4G27070.1; AT4G27070.
KEGGiath:AT4G27070.

Organism-specific databases

TAIRiAT4G27070.

Phylogenomic databases

eggNOGiKOG1395. Eukaryota.
COG0133. LUCA.
HOGENOMiHOG000161710.
InParanoidiP25269.
KOiK01696.
OMAiNVYRMRM.
PhylomeDBiP25269.

Enzyme and pathway databases

UniPathwayiUPA00035; UER00044.
BioCyciARA:AT4G27070-MONOMER.

Miscellaneous databases

PROiP25269.

Gene expression databases

ExpressionAtlasiP25269. baseline and differential.
GenevisibleiP25269. AT.

Family and domain databases

HAMAPiMF_00133. Trp_synth_beta.
InterProiIPR006653. Trp_synth_b_CS.
IPR006654. Trp_synth_beta.
IPR023026. Trp_synth_beta/beta-like.
IPR001926. TrpB-like_PLP-dep.
[Graphical view]
PfamiPF00291. PALP. 1 hit.
[Graphical view]
PIRSFiPIRSF001413. Trp_syn_beta. 1 hit.
SUPFAMiSSF53686. SSF53686. 1 hit.
TIGRFAMsiTIGR00263. trpB. 1 hit.
PROSITEiPS00168. TRP_SYNTHASE_BETA. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Tryptophan mutants in Arabidopsis: the consequences of duplicated tryptophan synthase beta genes."
    Last R.L., Bissinger P.H., Mahoney D.J., Radwanski E.R., Fink G.R.
    Plant Cell 3:345-358(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: cv. Columbia.
  2. "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.
  3. The Arabidopsis Information Resource (TAIR)
    Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
    Cited for: GENOME REANNOTATION.
    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. "Full-length cDNA from Arabidopsis thaliana."
    Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B., Feldmann K.A.
    Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  6. "Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
    Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
    Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT THR-52, CLEAVAGE OF TRANSIT PEPTIDE [LARGE SCALE ANALYSIS] AFTER CYS-51, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiTRBP2_ARATH
AccessioniPrimary (citable) accession number: P25269
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 1, 1992
Last sequence update: November 1, 1995
Last modified: February 17, 2016
This is version 131 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.