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Q9S7B5 (THRC1_ARATH) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 117. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Threonine synthase 1, chloroplastic

EC=4.2.3.1
Alternative name(s):
Protein METHIONINE OVER-ACCUMULATOR 2
Gene names
Name:TS1
Synonyms:MTO2
Ordered Locus Names:At4g29840
ORF Names:F27B13.80
OrganismArabidopsis thaliana (Mouse-ear cress) [Reference proteome]
Taxonomic identifier3702 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis

Protein attributes

Sequence length526 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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

Catalytic activity

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

Cofactor

Pyridoxal phosphate.

Enzyme regulation

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. Ref.6

Pathway

Amino-acid biosynthesis; L-threonine biosynthesis; L-threonine from L-aspartate: step 5/5.

Subunit structure

Homodimer. Ref.6

Subcellular location

Plastidchloroplast.

Domain

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

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).

Sequence similarities

Belongs to the threonine synthase family.

Biophysicochemical properties

Kinetic parameters:

KM=30 µM for O-phospho-L-homoserine (in presence of 100 µM S-adenosyl-L-methionine) Ref.6

KM=120 µM for O-phospho-L-homoserine (in absence of 100 µM S-adenosyl-L-methionine)

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 4040Chloroplast
Chain41 – 526486Threonine synthase 1, chloroplastic
PRO_0000033617

Regions

Region142 – 1443S-adenosyl-L-methionine 1 binding; shared with dimeric partner
Region165 – 1673S-adenosyl-L-methionine 1 binding; shared with dimeric partner
Region335 – 3395Pyridoxal phosphate binding By similarity
Compositional bias159 – 1624Poly-Asp

Sites

Binding site1721S-adenosyl-L-methionine 2; shared with dimeric partner
Binding site1731S-adenosyl-L-methionine 2; via amide nitrogen and carbonyl oxygen; shared with dimeric partner
Binding site1811S-adenosyl-L-methionine 3; in monomer B
Binding site1811S-adenosyl-L-methionine 4; in monomer A
Binding site1871S-adenosyl-L-methionine 3; in monomer B
Binding site4721Pyridoxal phosphate By similarity

Amino acid modifications

Modified residue2031N6-(pyridoxal phosphate)lysine

Experimental info

Mutagenesis2051L → R in mto2-1; causes a strong decrease in the concentration of soluble threonine and over-accumulation of methionine. Ref.7
Sequence conflict21A → L in AAB04607. Ref.4

Secondary structure

................................................................................... 526
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q9S7B5 [UniParc].

Last modified May 1, 2000. Version 1.
Checksum: B27787A57B882AD0

FASTA52657,777
        10         20         30         40         50         60 
MASSCLFNAS VSSLNPKQDP IRRHRSTSLL RHRPVVISCT ADGNNIKAPI ETAVKPPHRT 

        70         80         90        100        110        120 
EDNIRDEARR NRSNAVNPFS AKYVPFNAAP GSTESYSLDE IVYRSRSGGL LDVEHDMEAL 

       130        140        150        160        170        180 
KRFDGAYWRD LFDSRVGKST WPYGSGVWSK KEWVLPEIDD DDIVSAFEGN SNLFWAERFG 

       190        200        210        220        230        240 
KQFLGMNDLW VKHCGISHTG SFKDLGMTVL VSQVNRLRKM KRPVVGVGCA STGDTSAALS 

       250        260        270        280        290        300 
AYCASAGIPS IVFLPANKIS MAQLVQPIAN GAFVLSIDTD FDGCMKLIRE ITAELPIYLA 

       310        320        330        340        350        360 
NSLNSLRLEG QKTAAIEILQ QFDWQVPDWV IVPGGNLGNI YAFYKGFKMC QELGLVDRIP 

       370        380        390        400        410        420 
RMVCAQAANA NPLYLHYKSG WKDFKPMTAS TTFASAIQIG DPVSIDRAVY ALKKCNGIVE 

       430        440        450        460        470        480 
EATEEELMDA MAQADSTGMF ICPHTGVALT ALFKLRNQGV IAPTDRTVVV STAHGLKFTQ 

       490        500        510        520 
SKIDYHSNAI PDMACRFSNP PVDVKADFGA VMDVLKSYLG SNTLTS 

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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]"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(1996) [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(1998) [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(1999) [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(2000) [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(2001) [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(2006) [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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
PIRT08545.
RefSeqNP_194713.1. NM_119130.3.
UniGeneAt.23602.
At.72983.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1E5XX-ray2.25A/B41-526[»]
2C2BX-ray2.60A/B/C/D/E/F41-526[»]
2C2GX-ray2.61A/B41-526[»]
ProteinModelPortalQ9S7B5.
SMRQ9S7B5. Positions 76-519.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid14393. 1 interaction.

Proteomic databases

PaxDbQ9S7B5.
PRIDEQ9S7B5.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsAT4G29840.1; AT4G29840.1; AT4G29840.
GeneID829106.
KEGGath:AT4G29840.

Organism-specific databases

TAIRAT4G29840.

Phylogenomic databases

eggNOGCOG0498.
HOGENOMHOG000076502.
KOK01733.
OMALAQAMFH.
PhylomeDBQ9S7B5.

Enzyme and pathway databases

UniPathwayUPA00050; UER00065.

Gene expression databases

GenevestigatorQ9S7B5.

Family and domain databases

InterProIPR000634. Ser/Thr_deHydtase_PyrdxlP-BS.
IPR004450. Thr_synthase_like.
IPR001926. Trp_syn_b_sub_like_PLP_eny_SF.
[Graphical view]
PfamPF00291. PALP. 1 hit.
[Graphical view]
SUPFAMSSF53686. SSF53686. 1 hit.
TIGRFAMsTIGR00260. thrC. 1 hit.
PROSITEPS00165. DEHYDRATASE_SER_THR. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceQ9S7B5.

Entry information

Entry nameTHRC1_ARATH
AccessionPrimary (citable) accession number: Q9S7B5
Secondary accession number(s): Q39144
Entry history
Integrated into UniProtKB/Swiss-Prot: January 23, 2002
Last sequence update: May 1, 2000
Last modified: May 14, 2014
This is version 117 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways

Arabidopsis thaliana

Arabidopsis thaliana: entries and gene names