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Q9SSP5 (THRC2_ARATH) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 86. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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 2, chloroplastic

EC=4.2.3.1
Gene names
Name:TS2
Ordered Locus Names:At1g72810
ORF Names:F3N23.1
OrganismArabidopsis thaliana (Mouse-ear cress) [Reference proteome]
Taxonomic identifier3702 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis

Protein attributes

Sequence length516 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. Ref.4

Catalytic activity

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

Cofactor

Pyridoxal phosphate By similarity.

Enzyme regulation

Allosterically activated by S-adenosyl-methionine (SAM).

Pathway

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

Subunit structure

Homodimer By similarity.

Subcellular location

Plastidchloroplast Potential.

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-172 and Asn-178 of monomer B, whereas SAM4 interacts only with Lys-172 of monomer A By similarity.

Much less active than TS1 at physiological concentrations of S-adenosyl-methionine (20 µM).

Sequence similarities

Belongs to the threonine synthase family.

Ontologies

Keywords
   Biological processAmino-acid biosynthesis
Threonine biosynthesis
   Cellular componentChloroplast
Plastid
   DomainTransit peptide
   LigandPyridoxal phosphate
S-adenosyl-L-methionine
   Molecular functionLyase
   Technical termAllosteric enzyme
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processthreonine biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-UniPathway

   Cellular_componentchloroplast

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionpyridoxal phosphate binding

Inferred from electronic annotation. Source: InterPro

threonine synthase activity

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 5757Chloroplast Potential
Chain58 – 516459Threonine synthase 2, chloroplastic
PRO_0000379516

Regions

Region133 – 1353S-adenosyl-L-methionine 1 binding; shared with dimeric partner By similarity
Region156 – 1583S-adenosyl-L-methionine 1 binding; shared with dimeric partner By similarity
Region326 – 3305Pyridoxal phosphate binding By similarity
Compositional bias150 – 1534Poly-Asp

Sites

Binding site1631S-adenosyl-L-methionine 2; shared with dimeric partner By similarity
Binding site1641S-adenosyl-L-methionine 2; via amide nitrogen and carbonyl oxygen; shared with dimeric partner By similarity
Binding site1721S-adenosyl-L-methionine 3; in monomer B By similarity
Binding site1721S-adenosyl-L-methionine 4; in monomer A By similarity
Binding site1781S-adenosyl-L-methionine 3; in monomer B By similarity
Binding site4641Pyridoxal phosphate By similarity

Amino acid modifications

Modified residue1941N6-(pyridoxal phosphate)lysine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q9SSP5 [UniParc].

Last modified May 1, 2000. Version 1.
Checksum: 6BB95F6CD125B1C9

FASTA51656,925
        10         20         30         40         50         60 
MASFSLPHSA TYFPSHSETS LKPHSAASFT VRCTSASPAV PPQTPQKPRR SPDENIRDEA 

        70         80         90        100        110        120 
RRRPHQLQNL SARYVPFNAP PSSTESYSLD EIVYRSQSGA LLDVQHDFAA LKRYDGEFWR 

       130        140        150        160        170        180 
NLFDSRVGKT NWPYGSGVWS KKEWVLPEID DDDIVSAFEG NSNLFWAERF GKQYLQMNDL 

       190        200        210        220        230        240 
WVKHCGISHT GSFKDLGMSV LVSQVNRLRK MNKPVIGVGC ASTGDTSAAL SAYCASAGIP 

       250        260        270        280        290        300 
SIVFLPADKI SMAQLVQPIA NGAFVLSIDT DFDGCMHLIR EVTAELPIYL ANSLNSLRLE 

       310        320        330        340        350        360 
GQKTAAIEIL QQFNWQVPDW VIVPGGNLGN IYAFYKGFHM CKELGLVDRI PRLVCAQAAN 

       370        380        390        400        410        420 
ANPLYLHYKS GFKEDFNPLK ANTTFASAIQ IGDPVSIDRA VYALKKSNGI VEEATEEELM 

       430        440        450        460        470        480 
DATALADSTG MFICPHTGVA LTALMKLRKS GVIGANDRTV VVSTAHGLKF TQSKIDYHSK 

       490        500        510 
NIKEMACRLA NPPVKVKAKF GSVMDVLKEY LKSNDK 

« Hide

References

« Hide 'large scale' references
[1]"Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana."
Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O., Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E., Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K. expand/collapse author list , Conn L., Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P., Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D., Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J., Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L., Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A., Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A., Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M., Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M., Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P., Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D., Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D., Yu G., Fraser C.M., Venter J.C., Davis R.W.
Nature 408:816-820(2000) [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]"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. expand/collapse author list , 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.
[4]"Understanding the regulation of aspartate metabolism using a model based on measured kinetic parameters."
Curien G., Bastien O., Robert-Genthon M., Cornish-Bowden A., Cardenas M.L., Dumas R.
Mol. Syst. Biol. 5:271-271(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, CHARACTERIZATION.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AC008017 Genomic DNA. Translation: AAD55628.1.
CP002684 Genomic DNA. Translation: AEE35375.1.
AY099629 mRNA. Translation: AAM20480.1.
BT002151 mRNA. Translation: AAN72162.1.
PIRA96753.
RefSeqNP_565047.1. NM_105939.3.
UniGeneAt.11666.

3D structure databases

ProteinModelPortalQ9SSP5.
SMRQ9SSP5. Positions 70-511.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING3702.AT1G72810.1-P.

Proteomic databases

PaxDbQ9SSP5.
PRIDEQ9SSP5.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsAT1G72810.1; AT1G72810.1; AT1G72810.
GeneID843612.
KEGGath:AT1G72810.

Organism-specific databases

TAIRAT1G72810.

Phylogenomic databases

eggNOGCOG0498.
HOGENOMHOG000076502.
InParanoidQ9SSP5.
KOK01733.
OMASKAIMCA.
PhylomeDBQ9SSP5.

Enzyme and pathway databases

BioCycARA:AT1G72810-MONOMER.
UniPathwayUPA00050; UER00065.

Gene expression databases

GenevestigatorQ9SSP5.

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...

Entry information

Entry nameTHRC2_ARATH
AccessionPrimary (citable) accession number: Q9SSP5
Entry history
Integrated into UniProtKB/Swiss-Prot: July 7, 2009
Last sequence update: May 1, 2000
Last modified: May 14, 2014
This is version 86 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

PATHWAY comments

Index of metabolic and biosynthesis pathways

Arabidopsis thaliana

Arabidopsis thaliana: entries and gene names