THRC2_ARATH
ID THRC2_ARATH Reviewed; 516 AA.
AC Q9SSP5;
DT 07-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 126.
DE RecName: Full=Threonine synthase 2, chloroplastic;
DE EC=4.2.3.1;
DE Flags: Precursor;
GN Name=TS2; OrderedLocusNames=At1g72810; ORFNames=F3N23.1;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(2000).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [4]
RP FUNCTION, AND CHARACTERIZATION.
RX PubMed=19455135; DOI=10.1038/msb.2009.29;
RA Curien G., Bastien O., Robert-Genthon M., Cornish-Bowden A., Cardenas M.L.,
RA Dumas R.;
RT "Understanding the regulation of aspartate metabolism using a model based
RT on measured kinetic parameters.";
RL Mol. Syst. Biol. 5:271-271(2009).
CC -!- FUNCTION: Catalyzes the gamma-elimination of phosphate from L-
CC phosphohomoserine and the beta-addition of water to produce L-
CC threonine. {ECO:0000269|PubMed:19455135}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + O-phospho-L-homoserine = L-threonine + phosphate;
CC Xref=Rhea:RHEA:10840, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:57590, ChEBI:CHEBI:57926; EC=4.2.3.1;
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000250};
CC -!- ACTIVITY REGULATION: Allosterically activated by S-adenosyl-methionine
CC (SAM).
CC -!- PATHWAY: Amino-acid biosynthesis; L-threonine biosynthesis; L-threonine
CC from L-aspartate: step 5/5.
CC -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000305}.
CC -!- MISCELLANEOUS: Binds 4 S-adenosyl-L-methionine (SAM) molecules per
CC dimer. Although SAM3 and SAM4 have equivalent positions, their
CC interactions with the protein are not identical. SAM3 interacts with
CC Lys-172 and Asn-178 of monomer B, whereas SAM4 interacts only with Lys-
CC 172 of monomer A (By similarity). {ECO:0000250}.
CC -!- MISCELLANEOUS: Much less active than TS1 at physiological
CC concentrations of S-adenosyl-methionine (20 uM).
CC -!- SIMILARITY: Belongs to the threonine synthase family. {ECO:0000305}.
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DR EMBL; AC008017; AAD55628.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE35375.1; -; Genomic_DNA.
DR EMBL; AY099629; AAM20480.1; -; mRNA.
DR EMBL; BT002151; AAN72162.1; -; mRNA.
DR PIR; A96753; A96753.
DR RefSeq; NP_565047.1; NM_105939.4.
DR AlphaFoldDB; Q9SSP5; -.
DR SMR; Q9SSP5; -.
DR BioGRID; 28831; 16.
DR STRING; 3702.AT1G72810.1; -.
DR PaxDb; Q9SSP5; -.
DR PRIDE; Q9SSP5; -.
DR ProteomicsDB; 234427; -.
DR EnsemblPlants; AT1G72810.1; AT1G72810.1; AT1G72810.
DR GeneID; 843612; -.
DR Gramene; AT1G72810.1; AT1G72810.1; AT1G72810.
DR KEGG; ath:AT1G72810; -.
DR Araport; AT1G72810; -.
DR TAIR; locus:2032632; AT1G72810.
DR eggNOG; ENOG502QSQC; Eukaryota.
DR HOGENOM; CLU_028142_5_0_1; -.
DR InParanoid; Q9SSP5; -.
DR OMA; MLNAICK; -.
DR OrthoDB; 1361511at2759; -.
DR PhylomeDB; Q9SSP5; -.
DR BioCyc; ARA:AT1G72810-MON; -.
DR UniPathway; UPA00050; UER00065.
DR PRO; PR:Q9SSP5; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9SSP5; baseline and differential.
DR Genevisible; Q9SSP5; AT.
DR GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0004795; F:threonine synthase activity; IBA:GO_Central.
DR GO; GO:0019344; P:cysteine biosynthetic process; IBA:GO_Central.
DR GO; GO:0009088; P:threonine biosynthetic process; IEA:UniProtKB-UniPathway.
DR Gene3D; 3.40.50.1100; -; 2.
DR InterPro; IPR001926; PLP-dep.
DR InterPro; IPR000634; Ser/Thr_deHydtase_PyrdxlP-BS.
DR InterPro; IPR004450; Thr_synthase-like.
DR InterPro; IPR036052; Trypto_synt_PLP_dependent.
DR Pfam; PF00291; PALP; 1.
DR SUPFAM; SSF53686; SSF53686; 1.
DR TIGRFAMs; TIGR00260; thrC; 1.
DR PROSITE; PS00165; DEHYDRATASE_SER_THR; 1.
PE 1: Evidence at protein level;
KW Allosteric enzyme; Amino-acid biosynthesis; Chloroplast; Lyase; Plastid;
KW Pyridoxal phosphate; Reference proteome; S-adenosyl-L-methionine;
KW Threonine biosynthesis; Transit peptide.
FT TRANSIT 1..33
FT /note="Chloroplast"
FT /evidence="ECO:0000305"
FT CHAIN 34..516
FT /note="Threonine synthase 2, chloroplastic"
FT /id="PRO_0000379516"
FT REGION 1..55
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..40
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 133..135
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /ligand_label="1"
FT /ligand_note="ligand shared between dimeric partners"
FT /evidence="ECO:0000250"
FT BINDING 156..158
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /ligand_label="1"
FT /ligand_note="ligand shared between dimeric partners"
FT /evidence="ECO:0000250"
FT BINDING 163
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /ligand_label="2"
FT /ligand_note="ligand shared between dimeric partners"
FT /evidence="ECO:0000250"
FT BINDING 164
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /ligand_label="2"
FT /ligand_note="ligand shared between dimeric partners"
FT /evidence="ECO:0000250"
FT BINDING 172
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /ligand_label="3"
FT /note="in monomer B"
FT /evidence="ECO:0000250"
FT BINDING 172
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /ligand_label="4"
FT /note="in monomer A"
FT /evidence="ECO:0000250"
FT BINDING 178
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /ligand_label="3"
FT /note="in monomer B"
FT /evidence="ECO:0000250"
FT BINDING 326..330
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250"
FT BINDING 464
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250"
FT MOD_RES 194
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 516 AA; 56925 MW; 6BB95F6CD125B1C9 CRC64;
MASFSLPHSA TYFPSHSETS LKPHSAASFT VRCTSASPAV PPQTPQKPRR SPDENIRDEA
RRRPHQLQNL SARYVPFNAP PSSTESYSLD EIVYRSQSGA LLDVQHDFAA LKRYDGEFWR
NLFDSRVGKT NWPYGSGVWS KKEWVLPEID DDDIVSAFEG NSNLFWAERF GKQYLQMNDL
WVKHCGISHT GSFKDLGMSV LVSQVNRLRK MNKPVIGVGC ASTGDTSAAL SAYCASAGIP
SIVFLPADKI SMAQLVQPIA NGAFVLSIDT DFDGCMHLIR EVTAELPIYL ANSLNSLRLE
GQKTAAIEIL QQFNWQVPDW VIVPGGNLGN IYAFYKGFHM CKELGLVDRI PRLVCAQAAN
ANPLYLHYKS GFKEDFNPLK ANTTFASAIQ IGDPVSIDRA VYALKKSNGI VEEATEEELM
DATALADSTG MFICPHTGVA LTALMKLRKS GVIGANDRTV VVSTAHGLKF TQSKIDYHSK
NIKEMACRLA NPPVKVKAKF GSVMDVLKEY LKSNDK
