ID   THRC_SYNY3              Reviewed;         382 AA.
AC   P74193;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1997, sequence version 1.
DT   02-SEP-2026, entry version 152.
DE   RecName: Full=Threonine synthase;
DE            Short=TS;
DE            EC=4.2.3.1;
GN   Name=thrC; OrderedLocusNames=sll1172;
OS   Synechocystis sp. (strain ATCC 27184 / PCC 6803 / Kazusa).
OC   Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae; Synechococcales;
OC   Merismopediaceae; Synechocystis.
OX   NCBI_TaxID=1111708;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 27184 / PCC 6803 / Kazusa;
RX   PubMed=8905231; DOI=10.1093/dnares/3.3.109;
RA   Kaneko T., Sato S., Kotani H., Tanaka A., Asamizu E., Nakamura Y.,
RA   Miyajima N., Hirosawa M., Sugiura M., Sasamoto S., Kimura T., Hosouchi T.,
RA   Matsuno A., Muraki A., Nakazaki N., Naruo K., Okumura S., Shimpo S.,
RA   Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT   "Sequence analysis of the genome of the unicellular cyanobacterium
RT   Synechocystis sp. strain PCC6803. II. Sequence determination of the entire
RT   genome and assignment of potential protein-coding regions.";
RL   DNA Res. 3:109-136(1996).
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=O-phospho-L-homoserine + H2O = 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   -!- PATHWAY: Amino-acid biosynthesis; L-threonine biosynthesis; L-threonine
CC       from L-aspartate: step 5/5.
CC   -!- SIMILARITY: Belongs to the threonine synthase family. {ECO:0000305}.
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DR   EMBL; BA000022; BAA18282.1; -; Genomic_DNA.
DR   PIR; S75823; S75823.
DR   AlphaFoldDB; P74193; -.
DR   SMR; P74193; -.
DR   FunCoup; P74193; 179.
DR   IntAct; P74193; 1.
DR   STRING; 1148.gene:10499158; -.
DR   PaxDb; 1148-gene:10499158; -.
DR   EnsemblBacteria; BAA18282; BAA18282; BAA18282.
DR   KEGG; syn:sll1172; -.
DR   eggNOG; COG0498; Bacteria.
DR   InParanoid; P74193; -.
DR   PhylomeDB; P74193; -.
DR   UniPathway; UPA00050; UER00065.
DR   Proteomes; UP000001425; Chromosome.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0004795; F:threonine synthase activity; IBA:GO_Central.
DR   GO; GO:0009088; P:L-threonine biosynthetic process; IEA:UniProtKB-UniPathway.
DR   CDD; cd01563; Thr-synth_1; 1.
DR   FunFam; 3.40.50.1100:FF:000013; Threonine synthase; 1.
DR   FunFam; 3.40.50.1100:FF:000014; Threonine synthase; 1.
DR   Gene3D; 3.40.50.1100; -; 2.
DR   InterPro; IPR001763; Rhodanese-like_dom.
DR   InterPro; IPR050147; Ser/Thr_Dehydratase.
DR   InterPro; IPR000634; Ser/Thr_deHydtase_PyrdxlP-BS.
DR   InterPro; IPR004450; Thr_synthase-like.
DR   InterPro; IPR026260; Thr_Synthase_bac/arc.
DR   InterPro; IPR001926; TrpB-like_PALP.
DR   InterPro; IPR036052; TrpB-like_PALP_sf.
DR   NCBIfam; TIGR00260; thrC; 1.
DR   PANTHER; PTHR48078:SF6; L-THREONINE DEHYDRATASE CATABOLIC TDCB; 1.
DR   PANTHER; PTHR48078; THREONINE DEHYDRATASE, MITOCHONDRIAL-RELATED; 1.
DR   Pfam; PF00291; PALP; 1.
DR   PIRSF; PIRSF038945; Thr_synthase; 1.
DR   SUPFAM; SSF53686; Tryptophan synthase beta subunit-like PLP-dependent enzymes; 1.
DR   PROSITE; PS00165; DEHYDRATASE_SER_THR; 1.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis; Lyase; Pyridoxal phosphate; Reference proteome;
KW   Threonine biosynthesis.
FT   CHAIN           1..382
FT                   /note="Threonine synthase"
FT                   /id="PRO_0000185641"
FT   BINDING         119
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000250"
FT   BINDING         219..223
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000250"
FT   BINDING         347
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         93
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   382 AA;  40414 MW;  FBC9AEEC2B7F6F35 CRC64;
     MISCHSFTMT PSAPNSTVLP SATPVCPQSS ACRWRGLIET YRPYLPVSDQ TPVVTLLEGN
     TPLIPAPAIA KRIGKDVRVF VKYDGLNPTG SFKDRGMTMA ISKAKEAGAK AVICASTGNT
     SAAAAAYARR AGLRAFVIIP DGYVALGKLG QALIYGAEVI AIDGNFDDAL TTVRQLSEHY
     PVTLVNSVNP YRLEGQKTAA FEIVDVLGQA PDWLCIPVGN AGNITAYWMG FCQYKELGKG
     DRLPRMMGFQ AAGSAPFIQG QPISHPETLA TAIRIGNPAN WDKAWAASRE SNGEFHPVTD
     AEILEAYRIL AAEEGVFCEP ASAASVAGLL KQKDQVPAGA TVVCVLTGNG LKDPDCAVQN
     SGNQVKAGLK PDLEIVAKAM GF
//