ID   THRC_METJA              Reviewed;         405 AA.
AC   Q58860;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 124.
DE   RecName: Full=Threonine synthase;
DE            Short=TS;
DE            EC=4.2.3.1;
GN   Name=thrC; OrderedLocusNames=MJ1465;
OS   Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM
OS   10045 / NBRC 100440) (Methanococcus jannaschii).
OC   Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC   Methanocaldococcaceae; Methanocaldococcus.
OX   NCBI_TaxID=243232;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440;
RX   PubMed=8688087; DOI=10.1126/science.273.5278.1058;
RA   Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., Sutton G.G.,
RA   Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., Kerlavage A.R.,
RA   Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., Overbeek R.,
RA   Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., Scott J.L.,
RA   Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., Utterback T.R.,
RA   Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., Cotton M.D.,
RA   Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., Klenk H.-P.,
RA   Fraser C.M., Smith H.O., Woese C.R., Venter J.C.;
RT   "Complete genome sequence of the methanogenic archaeon, Methanococcus
RT   jannaschii.";
RL   Science 273:1058-1073(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=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   -!- 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; L77117; AAB99473.1; -; Genomic_DNA.
DR   PIR; H64482; H64482.
DR   RefSeq; WP_010870985.1; NC_000909.1.
DR   AlphaFoldDB; Q58860; -.
DR   SMR; Q58860; -.
DR   STRING; 243232.MJ_1465; -.
DR   EnsemblBacteria; AAB99473; AAB99473; MJ_1465.
DR   GeneID; 1452369; -.
DR   KEGG; mja:MJ_1465; -.
DR   eggNOG; arCOG01434; Archaea.
DR   HOGENOM; CLU_028142_4_1_2; -.
DR   InParanoid; Q58860; -.
DR   OMA; MWGFQAS; -.
DR   OrthoDB; 16594at2157; -.
DR   PhylomeDB; Q58860; -.
DR   BioCyc; MetaCyc:MON-14634; -.
DR   UniPathway; UPA00050; UER00065.
DR   Proteomes; UP000000805; Chromosome.
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; IPR026260; Thr_Synthase_bac/arc.
DR   InterPro; IPR036052; Trypto_synt_PLP_dependent.
DR   Pfam; PF00291; PALP; 1.
DR   PIRSF; PIRSF038945; Thr_synthase; 1.
DR   SUPFAM; SSF53686; SSF53686; 1.
DR   TIGRFAMs; TIGR00260; thrC; 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..405
FT                   /note="Threonine synthase"
FT                   /id="PRO_0000185642"
FT   BINDING         132
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000250"
FT   BINDING         233..237
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000250"
FT   BINDING         371
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         106
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   405 AA;  44601 MW;  FAD055FB041E2DF0 CRC64;
     MLQRCIKCGK TYDVDEIIYT CECGGLLEII YDYEEIKDKV SEEKLRKREI GVWRYLEYLP
     VKDESKIVSL CEGGTPLYRC NNLEKELGIK ELYVKNEGAN PTGSFKDRGM TVGVTRANEL
     GVEVVGCAST GNTSASLAAY SARSGKKCIV LLPEGKVALG KLAQAMFYGA KVIQVKGNFD
     DALDMVKQLA KEKLIYLLNS INPFRLEGQK TIAFEICDQL NWQVPDRVIV PVGNAGNISA
     IWKGFKEFEI TGIIDELPKM TGIQADGAKP IVEAFRKRAK DIIPYKNPET IATAIRIGNP
     VNAPKALDAI YSSGGYAEAV TDEEIVEAQK LLARKEGIFV EPASASSIAG LKKLLEEGII
     DRDERIVCIT TGHGLKDPDA AIRASEEPIK IECDMNVLKR ILKEL