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Protein

Threonine synthase 1, chloroplastic

Gene

TS1

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

Functioni

Catalyzes the gamma-elimination of phosphate from L-phosphohomoserine and the beta-addition of water to produce L-threonine.

Catalytic activityi

O-phospho-L-homoserine + H2O = L-threonine + phosphate.

Cofactori

Enzyme regulationi

Allosterically activated by S-adenosyl-L-methionine (SAM). Activated by S-adenosyl-L-ethionine, 5'-amino-5'-deoxyadenosine, sinefungin and 5'-deoxy-5-methylthioadenosine. Inhibited by AMP.1 Publication

Kineticsi

  1. KM=30 µM for O-phospho-L-homoserine (in presence of 100 µM S-adenosyl-L-methionine)1 Publication
  2. KM=120 µM for O-phospho-L-homoserine (in absence of 100 µM S-adenosyl-L-methionine)1 Publication

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei172 – 1721S-adenosyl-L-methionine 2; shared with dimeric partner1 Publication
Binding sitei173 – 1731S-adenosyl-L-methionine 2; via amide nitrogen and carbonyl oxygen; shared with dimeric partner1 Publication
Binding sitei181 – 1811S-adenosyl-L-methionine 3; in monomer B1 Publication
Binding sitei181 – 1811S-adenosyl-L-methionine 4; in monomer A1 Publication
Binding sitei187 – 1871S-adenosyl-L-methionine 3; in monomer B1 Publication
Binding sitei472 – 4721Pyridoxal phosphateBy similarity

GO - Molecular functioni

  1. pyridoxal phosphate binding Source: GO_Central
  2. threonine synthase activity Source: TAIR

GO - Biological processi

  1. threonine biosynthetic process Source: UniProtKB-UniPathway
Complete GO annotation...

Keywords - Molecular functioni

Lyase

Keywords - Biological processi

Amino-acid biosynthesis, Threonine biosynthesis

Keywords - Ligandi

Pyridoxal phosphate, S-adenosyl-L-methionine

Enzyme and pathway databases

BRENDAi4.2.3.1. 399.
UniPathwayiUPA00050; UER00065.

Names & Taxonomyi

Protein namesi
Recommended name:
Threonine synthase 1, chloroplastic (EC:4.2.3.1)
Alternative name(s):
Protein METHIONINE OVER-ACCUMULATOR 2
Gene namesi
Name:TS1
Synonyms:MTO2
Ordered Locus Names:At4g29840
ORF Names:F27B13.80
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
ProteomesiUP000006548 Componenti: Chromosome 4

Organism-specific databases

TAIRiAT4G29840.

Subcellular locationi

GO - Cellular componenti

  1. chloroplast Source: TAIR
  2. chloroplast stroma Source: TAIR
  3. cytosol Source: TAIR
Complete GO annotation...

Keywords - Cellular componenti

Chloroplast, Plastid

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi205 – 2051L → R in mto2-1; causes a strong decrease in the concentration of soluble threonine and over-accumulation of methionine. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 4040ChloroplastAdd
BLAST
Chaini41 – 526486Threonine synthase 1, chloroplasticPRO_0000033617Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei203 – 2031N6-(pyridoxal phosphate)lysine

Proteomic databases

PaxDbiQ9S7B5.
PRIDEiQ9S7B5.

Expressioni

Gene expression databases

GenevestigatoriQ9S7B5.

Interactioni

Subunit structurei

Homodimer.2 Publications

Protein-protein interaction databases

BioGridi14393. 1 interaction.

Structurei

Secondary structure

1
526
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi60 – 645Combined sources
Beta strandi81 – 877Combined sources
Turni106 – 1083Combined sources
Beta strandi110 – 1156Combined sources
Helixi117 – 1215Combined sources
Helixi125 – 1339Combined sources
Turni134 – 1374Combined sources
Turni141 – 1444Combined sources
Helixi148 – 1536Combined sources
Helixi160 – 1623Combined sources
Beta strandi173 – 1753Combined sources
Helixi177 – 1848Combined sources
Beta strandi187 – 1937Combined sources
Beta strandi196 – 2016Combined sources
Helixi204 – 21916Combined sources
Beta strandi226 – 2294Combined sources
Helixi234 – 24613Combined sources
Beta strandi250 – 2556Combined sources
Helixi256 – 2583Combined sources
Helixi261 – 2699Combined sources
Beta strandi273 – 2797Combined sources
Helixi281 – 29414Combined sources
Beta strandi297 – 2993Combined sources
Helixi300 – 3023Combined sources
Helixi304 – 3118Combined sources
Helixi313 – 3219Combined sources
Turni322 – 3243Combined sources
Beta strandi328 – 3336Combined sources
Beta strandi335 – 3373Combined sources
Helixi338 – 35215Combined sources
Beta strandi355 – 3573Combined sources
Beta strandi361 – 3677Combined sources
Helixi368 – 3703Combined sources
Helixi373 – 3786Combined sources
Turni379 – 3835Combined sources
Helixi395 – 3973Combined sources
Helixi406 – 4149Combined sources
Beta strandi418 – 4225Combined sources
Helixi424 – 43613Combined sources
Helixi443 – 45715Combined sources
Beta strandi467 – 4715Combined sources
Helixi475 – 4784Combined sources
Helixi479 – 4868Combined sources
Beta strandi502 – 5065Combined sources
Helixi508 – 51811Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1E5XX-ray2.25A/B41-526[»]
2C2BX-ray2.60A/B/C/D/E/F41-526[»]
2C2GX-ray2.61A/B41-526[»]
ProteinModelPortaliQ9S7B5.
SMRiQ9S7B5. Positions 76-519.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9S7B5.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni142 – 1443S-adenosyl-L-methionine 1 binding; shared with dimeric partner
Regioni165 – 1673S-adenosyl-L-methionine 1 binding; shared with dimeric partner
Regioni335 – 3395Pyridoxal phosphate bindingBy similarity

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi159 – 1624Poly-Asp

Domaini

The N-terminal domain (1-77) is essential for regulation by S-adenosyl-L-methionine and AMP, but not for dimerization.

Sequence similaritiesi

Belongs to the threonine synthase family.Curated

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiCOG0498.
HOGENOMiHOG000076502.
InParanoidiQ9S7B5.
KOiK01733.
OMAiQSHHADP.
PhylomeDBiQ9S7B5.

Family and domain databases

InterProiIPR000634. Ser/Thr_deHydtase_PyrdxlP-BS.
IPR004450. Thr_synthase_like.
IPR001926. TrpB-like_PLP-dep.
[Graphical view]
PfamiPF00291. PALP. 1 hit.
[Graphical view]
SUPFAMiSSF53686. SSF53686. 1 hit.
TIGRFAMsiTIGR00260. thrC. 1 hit.
PROSITEiPS00165. DEHYDRATASE_SER_THR. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

Q9S7B5-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MASSCLFNAS VSSLNPKQDP IRRHRSTSLL RHRPVVISCT ADGNNIKAPI
60 70 80 90 100
ETAVKPPHRT EDNIRDEARR NRSNAVNPFS AKYVPFNAAP GSTESYSLDE
110 120 130 140 150
IVYRSRSGGL LDVEHDMEAL KRFDGAYWRD LFDSRVGKST WPYGSGVWSK
160 170 180 190 200
KEWVLPEIDD DDIVSAFEGN SNLFWAERFG KQFLGMNDLW VKHCGISHTG
210 220 230 240 250
SFKDLGMTVL VSQVNRLRKM KRPVVGVGCA STGDTSAALS AYCASAGIPS
260 270 280 290 300
IVFLPANKIS MAQLVQPIAN GAFVLSIDTD FDGCMKLIRE ITAELPIYLA
310 320 330 340 350
NSLNSLRLEG QKTAAIEILQ QFDWQVPDWV IVPGGNLGNI YAFYKGFKMC
360 370 380 390 400
QELGLVDRIP RMVCAQAANA NPLYLHYKSG WKDFKPMTAS TTFASAIQIG
410 420 430 440 450
DPVSIDRAVY ALKKCNGIVE EATEEELMDA MAQADSTGMF ICPHTGVALT
460 470 480 490 500
ALFKLRNQGV IAPTDRTVVV STAHGLKFTQ SKIDYHSNAI PDMACRFSNP
510 520
PVDVKADFGA VMDVLKSYLG SNTLTS
Length:526
Mass (Da):57,777
Last modified:May 1, 2000 - v1
Checksum:iB27787A57B882AD0
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti2 – 21A → L in AAB04607 (PubMed:8706836).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB027151 Genomic DNA. Translation: BAA77707.1.
AL050352 Genomic DNA. Translation: CAB43659.1.
AL161575 Genomic DNA. Translation: CAB79742.1.
CP002687 Genomic DNA. Translation: AEE85684.1.
L41666 mRNA. Translation: AAB04607.1.
PIRiT08545.
RefSeqiNP_194713.1. NM_119130.3.
UniGeneiAt.23602.
At.72983.

Genome annotation databases

EnsemblPlantsiAT4G29840.1; AT4G29840.1; AT4G29840.
GeneIDi829106.
KEGGiath:AT4G29840.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB027151 Genomic DNA. Translation: BAA77707.1.
AL050352 Genomic DNA. Translation: CAB43659.1.
AL161575 Genomic DNA. Translation: CAB79742.1.
CP002687 Genomic DNA. Translation: AEE85684.1.
L41666 mRNA. Translation: AAB04607.1.
PIRiT08545.
RefSeqiNP_194713.1. NM_119130.3.
UniGeneiAt.23602.
At.72983.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1E5XX-ray2.25A/B41-526[»]
2C2BX-ray2.60A/B/C/D/E/F41-526[»]
2C2GX-ray2.61A/B41-526[»]
ProteinModelPortaliQ9S7B5.
SMRiQ9S7B5. Positions 76-519.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi14393. 1 interaction.

Proteomic databases

PaxDbiQ9S7B5.
PRIDEiQ9S7B5.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsiAT4G29840.1; AT4G29840.1; AT4G29840.
GeneIDi829106.
KEGGiath:AT4G29840.

Organism-specific databases

TAIRiAT4G29840.

Phylogenomic databases

eggNOGiCOG0498.
HOGENOMiHOG000076502.
InParanoidiQ9S7B5.
KOiK01733.
OMAiQSHHADP.
PhylomeDBiQ9S7B5.

Enzyme and pathway databases

UniPathwayiUPA00050; UER00065.
BRENDAi4.2.3.1. 399.

Miscellaneous databases

EvolutionaryTraceiQ9S7B5.

Gene expression databases

GenevestigatoriQ9S7B5.

Family and domain databases

InterProiIPR000634. Ser/Thr_deHydtase_PyrdxlP-BS.
IPR004450. Thr_synthase_like.
IPR001926. TrpB-like_PLP-dep.
[Graphical view]
PfamiPF00291. PALP. 1 hit.
[Graphical view]
SUPFAMiSSF53686. SSF53686. 1 hit.
TIGRFAMsiTIGR00260. thrC. 1 hit.
PROSITEiPS00165. DEHYDRATASE_SER_THR. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Genomic nucleotide sequence of the Arabidopsis threonine synthase gene."
    Bartlem D., Tamaki Y., Naito S.
    Plant Gene Register PGR99-108
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: cv. Wassilewskija.
  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(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: cv. Columbia.
  3. The Arabidopsis Information Resource (TAIR)
    Submitted (MAR-2011) to the EMBL/GenBank/DDBJ databases
    Cited for: GENOME REANNOTATION.
    Strain: cv. Columbia.
  4. "Characterization of an Arabidopsis thaliana cDNA encoding an S-adenosylmethionine-sensitive threonine synthase. Threonine synthase from higher plants."
    Curien G., Dumas R., Ravanel S., Douce R.
    FEBS Lett. 390:85-90(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 2-526, CHARACTERIZATION.
    Strain: cv. Columbia.
  5. "Allosteric activation of Arabidopsis threonine synthase by S-adenosylmethionine."
    Curien G., Job D., Douce R., Dumas R.
    Biochemistry 37:13212-13221(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHARACTERIZATION.
  6. "Characterization of recombinant Arabidopsis thaliana threonine synthase."
    Laber B., Maurer W., Hanke C., Graefe S., Ehlert S., Messerschmidt A., Clausen T.
    Eur. J. Biochem. 263:212-221(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: BIOPHYSICOCHEMICAL PROPERTIES, ENZYME REGULATION, SUBUNIT, CRYSTALLIZATION.
  7. "Mutation in the threonine synthase gene results in an over-accumulation of soluble methionine in Arabidopsis."
    Bartlem D., Lambein I., Okamoto T., Itaya A., Uda Y., Kijima F., Tamaki Y., Nambara E., Naito S.
    Plant Physiol. 123:101-110(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: MUTAGENESIS OF LEU-205.
  8. "Crystal structure of threonine synthase from Arabidopsis thaliana."
    Thomazeau K., Curien G., Dumas R., Biou V.
    Protein Sci. 10:638-648(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.25 ANGSTROMS) OF 41-526, PYRIDOXAL PHOSPHATE AT LYS-203.
  9. "Allosteric threonine synthase. Reorganization of the pyridoxal phosphate site upon asymmetric activation through S-adenosylmethionine binding to a novel site."
    Mas-Droux C., Biou V., Dumas R.
    J. Biol. Chem. 281:5188-5196(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 41-526 IN COMPLEX WITH PYRIDOXAL PHOSPHATE AND S-ADENOSYL-L-METHIONINE.

Entry informationi

Entry nameiTHRC1_ARATH
AccessioniPrimary (citable) accession number: Q9S7B5
Secondary accession number(s): Q39144
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 23, 2002
Last sequence update: May 1, 2000
Last modified: April 1, 2015
This is version 123 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Miscellaneous

Binds 4 S-adenosyl-L-methionine (SAM) molecules per dimer. Although SAM3 and SAM4 have equivalent positions, their interactions with the protein are not identical. SAM3 interacts with Lys-181 and Asn-187 of monomer B, whereas SAM4 interacts only with Lys-181 of monomer A.
Much more active than TS2 at physiological concentrations of S-adenosyl-L-methionine (20 µM).

Keywords - Technical termi

3D-structure, Allosteric enzyme, Complete proteome, Reference proteome

Documents

  1. Arabidopsis thaliana
    Arabidopsis thaliana: entries and gene names
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.