ID   THRC_SOLTU              Reviewed;         519 AA.
AC   Q9MT28;
DT   23-JAN-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   03-AUG-2022, entry version 93.
DE   RecName: Full=Threonine synthase, chloroplastic;
DE            Short=TS;
DE            EC=4.2.3.1;
DE   Flags: Precursor;
OS   Solanum tuberosum (Potato).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; lamiids; Solanales; Solanaceae; Solanoideae; Solaneae; Solanum.
OX   NCBI_TaxID=4113;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Leaf;
RX   PubMed=10940468; DOI=10.1016/s0168-9452(00)00265-x;
RA   Casazza A.P., Basner A., Hoefgen R., Hesse H.;
RT   "Expression of threonine synthase from Solanum tuberosum L. is not
RT   metabolically regulated by photosynthesis-related signals or by nitrogenous
RT   compounds.";
RL   Plant Sci. 157:43-50(2000).
CC   -!- FUNCTION: Catalyzes the gamma-elimination of phosphate from L-
CC       phosphohomoserine and the beta-addition of water to produce L-
CC       threonine. {ECO:0000250}.
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). {ECO:0000250}.
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:0000250}.
CC   -!- SIMILARITY: Belongs to the threonine synthase family. {ECO:0000305}.
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DR   EMBL; AF082894; AAF74984.1; -; mRNA.
DR   RefSeq; NP_001274994.1; NM_001288065.1.
DR   AlphaFoldDB; Q9MT28; -.
DR   SMR; Q9MT28; -.
DR   STRING; 4113.PGSC0003DMT400006366; -.
DR   EnsemblPlants; RHC03H1G2400.2.1; RHC03H1G2400.2.1.cds.1; RHC03H1G2400.2.
DR   GeneID; 102577745; -.
DR   Gramene; RHC03H1G2400.2.1; RHC03H1G2400.2.1.cds.1; RHC03H1G2400.2.
DR   KEGG; sot:102577745; -.
DR   eggNOG; ENOG502QSQC; Eukaryota.
DR   UniPathway; UPA00050; UER00065.
DR   Proteomes; UP000011115; Unassembled WGS sequence.
DR   ExpressionAtlas; Q9MT28; baseline and differential.
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   2: Evidence at transcript 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..40
FT                   /note="Chloroplast"
FT                   /evidence="ECO:0000250"
FT   CHAIN           41..519
FT                   /note="Threonine synthase, chloroplastic"
FT                   /id="PRO_0000033618"
FT   BINDING         328..332
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000250"
FT   BINDING         465
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         196
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   519 AA;  57412 MW;  114C0979CD231464 CRC64;
     MAASCMLRSS FISPGLPQLH HQSTSKPNNG IHFFTPIKAT ATNDAISQQK HRRPADENIR
     EEARRHCSSH NFSARYVPFN AGPNSDEWYS LDEIVYRSRS GGLLDVQHDM DALKKFDGQY
     WRSLFDSRVG KTTWPYGSGV WSKKEWVLPE IDSDDIVSAF EGNSNLFWAE RFGKQFLGMT
     DLWVKHCGIS HTGSFKDLGM TVLVSQVNRL RKMHKPVVGV GCASTGDTSA ALSAYCASAG
     IPSIVFLPAN KISMAQLVQP IANGAFVLSI DTDFDGCMQL IREVTAELPI YLANSLNSLR
     LEGQKTAAIE ILQQFDWEVP EWVIVPGGNL GNIYAFYKGF QMCKELGLVD RIPRLVCAQA
     ANANPLYLHY KSGWKDFKPV KANTTFASAI QIGDPVSIDR AVFALQQCNG IVEEATEEEL
     MDAMAQADST GMFICPHTGV ALTALFKLRN SGVIAPTDRT VVVSTAHGLK FTQSKIDYHS
     KEIKDMECRF ANPPVEVKAD FGSVMDVLKS YLLSQNSKL