ID   THRC_SERMA              Reviewed;         429 AA.
AC   P27735;
DT   01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1992, sequence version 1.
DT   25-MAY-2022, entry version 84.
DE   RecName: Full=Threonine synthase;
DE            Short=TS;
DE            EC=4.2.3.1;
GN   Name=thrC;
OS   Serratia marcescens.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Yersiniaceae; Serratia.
OX   NCBI_TaxID=615;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=Sr41;
RX   PubMed=8423151; DOI=10.1128/jb.175.3.785-794.1993;
RA   Omori K., Suzuki S., Komatsubara S.;
RT   "Nucleotide sequence of the Serratia marcescens threonine operon and
RT   analysis of the threonine operon mutations which alter feedback inhibition
RT   of both aspartokinase I and homoserine dehydrogenase I.";
RL   J. Bacteriol. 175:785-794(1993).
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; D10387; BAA01222.1; -; Genomic_DNA.
DR   EMBL; X60821; CAA43214.1; -; Genomic_DNA.
DR   PIR; D47057; S16043.
DR   AlphaFoldDB; P27735; -.
DR   SMR; P27735; -.
DR   STRING; 273526.SMDB11_0003; -.
DR   UniPathway; UPA00050; UER00065.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0004795; F:threonine synthase activity; IEA:UniProtKB-EC.
DR   GO; GO:0009088; P:threonine biosynthetic process; IEA:UniProtKB-UniPathway.
DR   Gene3D; 3.40.50.1100; -; 2.
DR   Gene3D; 3.90.1380.10; -; 1.
DR   InterPro; IPR001926; PLP-dep.
DR   InterPro; IPR000634; Ser/Thr_deHydtase_PyrdxlP-BS.
DR   InterPro; IPR029144; Thr_synth_N.
DR   InterPro; IPR037158; Thr_synth_N_sf.
DR   InterPro; IPR004450; Thr_synthase-like.
DR   InterPro; IPR036052; Trypto_synt_PLP_dependent.
DR   Pfam; PF00291; PALP; 1.
DR   Pfam; PF14821; Thr_synth_N; 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;
KW   Threonine biosynthesis.
FT   CHAIN           1..429
FT                   /note="Threonine synthase"
FT                   /id="PRO_0000185640"
FT   MOD_RES         107
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   429 AA;  47094 MW;  B47262DE94848015 CRC64;
     MKLYNLKDHN EQVSFAQAIK QGLGKQQGLF FPLDLPEFEL TEIDHLLEQD FVTRSSRILS
     AFIGEEVPET ALKKRVQAAF EFPAPVAKVT DDVSCLELFH GPTLAFKDFG GRFMAQMLAE
     VAGEQPVTIL TATSGDTGAA VAHAFYGLKN VRVVILYPQG KISPLQEKLF CTLGGNIHTV
     AIDGDFDACQ ALVKQAFDDQ ELKDALHLNS ANSINISRLL AQICYYFEAV AQLPQEARNQ
     LVISVPSGNF GDLTAGLLAK SLGLPVKRFI AATNANDTVP RFLTSGQWQP HATVATLSNA
     MDVSQPNNWP RVEELFRRKV WQLKELGHAA VSDETTKDTM RELAELGYIS EPHAAIAYRA
     LRDQLQEGEF GLFLGTAHPA KFKESVEAIL GQELPLPKAL ALRAELPLLS HTLPASFGEL
     RKFLMGLPA