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Q9SSP5

- THRC2_ARATH

UniProt

Q9SSP5 - THRC2_ARATH

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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

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
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

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-KW
Complete GO annotation...

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. 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.

Q9SSP5 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MASFSLPHSA TYFPSHSETS LKPHSAASFT VRCTSASPAV PPQTPQKPRR
60 70 80 90 100
SPDENIRDEA RRRPHQLQNL SARYVPFNAP PSSTESYSLD EIVYRSQSGA
110 120 130 140 150
LLDVQHDFAA LKRYDGEFWR NLFDSRVGKT NWPYGSGVWS KKEWVLPEID
160 170 180 190 200
DDDIVSAFEG NSNLFWAERF GKQYLQMNDL WVKHCGISHT GSFKDLGMSV
210 220 230 240 250
LVSQVNRLRK MNKPVIGVGC ASTGDTSAAL SAYCASAGIP SIVFLPADKI
260 270 280 290 300
SMAQLVQPIA NGAFVLSIDT DFDGCMHLIR EVTAELPIYL ANSLNSLRLE
310 320 330 340 350
GQKTAAIEIL QQFNWQVPDW VIVPGGNLGN IYAFYKGFHM CKELGLVDRI
360 370 380 390 400
PRLVCAQAAN ANPLYLHYKS GFKEDFNPLK ANTTFASAIQ IGDPVSIDRA
410 420 430 440 450
VYALKKSNGI VEEATEEELM DATALADSTG MFICPHTGVA LTALMKLRKS
460 470 480 490 500
GVIGANDRTV VVSTAHGLKF TQSKIDYHSK NIKEMACRLA NPPVKVKAKF
510
GSVMDVLKEY LKSNDK
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. TrpB-like_PLP-dep.
[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

« Hide 'large scale' publications
  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 29, 2014
This is version 88 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