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Q9SSP5

- THRC2_ARATH

UniProt

Q9SSP5 - THRC2_ARATH

Protein

Threonine synthase 2, chloroplastic

Gene

TS2

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 87 (01 Oct 2014)
      Sequence version 1 (01 May 2000)
      Previous versions | rss
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    Functioni

    Catalyzes the gamma-elimination of phosphate from L-phosphohomoserine and the beta-addition of water to produce L-threonine.1 Publication

    Catalytic activityi

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

    Cofactori

    Pyridoxal phosphate.By similarity

    Enzyme regulationi

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

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei163 – 1631S-adenosyl-L-methionine 2; shared with dimeric partnerBy similarity
    Binding sitei164 – 1641S-adenosyl-L-methionine 2; via amide nitrogen and carbonyl oxygen; shared with dimeric partnerBy similarity
    Binding sitei172 – 1721S-adenosyl-L-methionine 3; in monomer BBy similarity
    Binding sitei172 – 1721S-adenosyl-L-methionine 4; in monomer ABy similarity
    Binding sitei178 – 1781S-adenosyl-L-methionine 3; in monomer BBy similarity
    Binding sitei464 – 4641Pyridoxal phosphateBy similarity

    GO - Molecular functioni

    1. pyridoxal phosphate binding Source: InterPro
    2. threonine synthase activity Source: UniProtKB-EC

    GO - Biological processi

    1. threonine biosynthetic process Source: UniProtKB-UniPathway

    Keywords - Molecular functioni

    Lyase

    Keywords - Biological processi

    Amino-acid biosynthesis, Threonine biosynthesis

    Keywords - Ligandi

    Pyridoxal phosphate, S-adenosyl-L-methionine

    Enzyme and pathway databases

    BioCyciARA:AT1G72810-MONOMER.
    UniPathwayiUPA00050; UER00065.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Threonine synthase 2, chloroplastic (EC:4.2.3.1)
    Gene namesi
    Name:TS2
    Ordered Locus Names:At1g72810
    ORF Names:F3N23.1
    OrganismiArabidopsis thaliana (Mouse-ear cress)
    Taxonomic identifieri3702 [NCBI]
    Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
    ProteomesiUP000006548: Chromosome 1

    Organism-specific databases

    TAIRiAT1G72810.

    Subcellular locationi

    Plastidchloroplast Curated

    GO - Cellular componenti

    1. chloroplast Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Chloroplast, Plastid

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transit peptidei1 – 5757ChloroplastSequence AnalysisAdd
    BLAST
    Chaini58 – 516459Threonine synthase 2, chloroplasticPRO_0000379516Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei194 – 1941N6-(pyridoxal phosphate)lysineBy similarity

    Proteomic databases

    PaxDbiQ9SSP5.
    PRIDEiQ9SSP5.

    Expressioni

    Gene expression databases

    GenevestigatoriQ9SSP5.

    Interactioni

    Subunit structurei

    Homodimer.By similarity

    Protein-protein interaction databases

    STRINGi3702.AT1G72810.1-P.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9SSP5.
    SMRiQ9SSP5. Positions 70-511.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni133 – 1353S-adenosyl-L-methionine 1 binding; shared with dimeric partnerBy similarity
    Regioni156 – 1583S-adenosyl-L-methionine 1 binding; shared with dimeric partnerBy similarity
    Regioni326 – 3305Pyridoxal phosphate bindingBy similarity

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi150 – 1534Poly-Asp

    Sequence similaritiesi

    Belongs to the threonine synthase family.Curated

    Keywords - Domaini

    Transit peptide

    Phylogenomic databases

    eggNOGiCOG0498.
    HOGENOMiHOG000076502.
    InParanoidiQ9SSP5.
    KOiK01733.
    OMAiSKAIMCA.
    PhylomeDBiQ9SSP5.

    Family and domain databases

    InterProiIPR000634. Ser/Thr_deHydtase_PyrdxlP-BS.
    IPR004450. Thr_synthase_like.
    IPR001926. Trp_syn_b_sub_like_PLP_eny_SF.
    [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.

    Q9SSP5-1 [UniParc]FASTAAdd to Basket

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    MASFSLPHSA TYFPSHSETS LKPHSAASFT VRCTSASPAV PPQTPQKPRR    50
    SPDENIRDEA RRRPHQLQNL SARYVPFNAP PSSTESYSLD EIVYRSQSGA 100
    LLDVQHDFAA LKRYDGEFWR NLFDSRVGKT NWPYGSGVWS KKEWVLPEID 150
    DDDIVSAFEG NSNLFWAERF GKQYLQMNDL WVKHCGISHT GSFKDLGMSV 200
    LVSQVNRLRK MNKPVIGVGC ASTGDTSAAL SAYCASAGIP SIVFLPADKI 250
    SMAQLVQPIA NGAFVLSIDT DFDGCMHLIR EVTAELPIYL ANSLNSLRLE 300
    GQKTAAIEIL QQFNWQVPDW VIVPGGNLGN IYAFYKGFHM CKELGLVDRI 350
    PRLVCAQAAN ANPLYLHYKS GFKEDFNPLK ANTTFASAIQ IGDPVSIDRA 400
    VYALKKSNGI VEEATEEELM DATALADSTG MFICPHTGVA LTALMKLRKS 450
    GVIGANDRTV VVSTAHGLKF TQSKIDYHSK NIKEMACRLA NPPVKVKAKF 500
    GSVMDVLKEY LKSNDK 516
    Length:516
    Mass (Da):56,925
    Last modified:May 1, 2000 - v1
    Checksum:i6BB95F6CD125B1C9
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AC008017 Genomic DNA. Translation: AAD55628.1.
    CP002684 Genomic DNA. Translation: AEE35375.1.
    AY099629 mRNA. Translation: AAM20480.1.
    BT002151 mRNA. Translation: AAN72162.1.
    PIRiA96753.
    RefSeqiNP_565047.1. NM_105939.3.
    UniGeneiAt.11666.

    Genome annotation databases

    EnsemblPlantsiAT1G72810.1; AT1G72810.1; AT1G72810.
    GeneIDi843612.
    KEGGiath:AT1G72810.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AC008017 Genomic DNA. Translation: AAD55628.1 .
    CP002684 Genomic DNA. Translation: AEE35375.1 .
    AY099629 mRNA. Translation: AAM20480.1 .
    BT002151 mRNA. Translation: AAN72162.1 .
    PIRi A96753.
    RefSeqi NP_565047.1. NM_105939.3.
    UniGenei At.11666.

    3D structure databases

    ProteinModelPortali Q9SSP5.
    SMRi Q9SSP5. Positions 70-511.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 3702.AT1G72810.1-P.

    Proteomic databases

    PaxDbi Q9SSP5.
    PRIDEi Q9SSP5.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblPlantsi AT1G72810.1 ; AT1G72810.1 ; AT1G72810 .
    GeneIDi 843612.
    KEGGi ath:AT1G72810.

    Organism-specific databases

    TAIRi AT1G72810.

    Phylogenomic databases

    eggNOGi COG0498.
    HOGENOMi HOG000076502.
    InParanoidi Q9SSP5.
    KOi K01733.
    OMAi SKAIMCA.
    PhylomeDBi Q9SSP5.

    Enzyme and pathway databases

    UniPathwayi UPA00050 ; UER00065 .
    BioCyci ARA:AT1G72810-MONOMER.

    Gene expression databases

    Genevestigatori Q9SSP5.

    Family and domain databases

    InterProi IPR000634. Ser/Thr_deHydtase_PyrdxlP-BS.
    IPR004450. Thr_synthase_like.
    IPR001926. Trp_syn_b_sub_like_PLP_eny_SF.
    [Graphical view ]
    Pfami PF00291. PALP. 1 hit.
    [Graphical view ]
    SUPFAMi SSF53686. SSF53686. 1 hit.
    TIGRFAMsi TIGR00260. thrC. 1 hit.
    PROSITEi PS00165. DEHYDRATASE_SER_THR. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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.
      , 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.
      , 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.

    Entry informationi

    Entry nameiTHRC2_ARATH
    AccessioniPrimary (citable) accession number: Q9SSP5
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 7, 2009
    Last sequence update: May 1, 2000
    Last modified: October 1, 2014
    This is version 87 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-172 and Asn-178 of monomer B, whereas SAM4 interacts only with Lys-172 of monomer A By similarity.By similarity
    Much less active than TS1 at physiological concentrations of S-adenosyl-methionine (20 µM).

    Keywords - Technical termi

    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. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3