ID   THRC_MYCLE              Reviewed;         360 AA.
AC   P45837;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, 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=ML1130;
OS   Mycobacterium leprae (strain TN).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium.
OX   NCBI_TaxID=272631;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Smith D.R., Robison K.;
RL   Submitted (SEP-1994) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TN;
RX   PubMed=11234002; DOI=10.1038/35059006;
RA   Cole S.T., Eiglmeier K., Parkhill J., James K.D., Thomson N.R.,
RA   Wheeler P.R., Honore N., Garnier T., Churcher C.M., Harris D.E.,
RA   Mungall K.L., Basham D., Brown D., Chillingworth T., Connor R.,
RA   Davies R.M., Devlin K., Duthoy S., Feltwell T., Fraser A., Hamlin N.,
RA   Holroyd S., Hornsby T., Jagels K., Lacroix C., Maclean J., Moule S.,
RA   Murphy L.D., Oliver K., Quail M.A., Rajandream M.A., Rutherford K.M.,
RA   Rutter S., Seeger K., Simon S., Simmonds M., Skelton J., Squares R.,
RA   Squares S., Stevens K., Taylor K., Whitehead S., Woodward J.R.,
RA   Barrell B.G.;
RT   "Massive gene decay in the leprosy bacillus.";
RL   Nature 409:1007-1011(2001).
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   -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the threonine synthase family. {ECO:0000305}.
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DR   EMBL; U15186; AAA63090.1; -; Genomic_DNA.
DR   EMBL; AL583920; CAC31511.1; -; Genomic_DNA.
DR   PIR; T09991; T09991.
DR   RefSeq; NP_301824.1; NC_002677.1.
DR   RefSeq; WP_010908148.1; NC_002677.1.
DR   AlphaFoldDB; P45837; -.
DR   SMR; P45837; -.
DR   STRING; 272631.ML1130; -.
DR   EnsemblBacteria; CAC31511; CAC31511; CAC31511.
DR   KEGG; mle:ML1130; -.
DR   PATRIC; fig|272631.5.peg.2052; -.
DR   Leproma; ML1130; -.
DR   eggNOG; COG0498; Bacteria.
DR   HOGENOM; CLU_028142_0_0_11; -.
DR   OMA; MWGFQAS; -.
DR   UniPathway; UPA00050; UER00065.
DR   Proteomes; UP000000806; Chromosome.
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   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..360
FT                   /note="Threonine synthase"
FT                   /id="PRO_0000185636"
FT   BINDING         95
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000250"
FT   BINDING         196..200
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000250"
FT   BINDING         326
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         69
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   360 AA;  37385 MW;  96A06F7B17B2688B CRC64;
     MSGQQTTTHQ PWPGVIAAYR DRLPVGDDWT PVTLLEGGTP LIAAPRLSEQ TGCTIHLKVE
     GLNPTGSFKD RGMTMAVTDA LARGQRAVLC ASTGNTSASA AAYAARAGIT CAVLIPQGKI
     AMGKLAQAVM HGAKIIQIDG NFDDCLELAR KMAADFPMIS LVNSVNPVRI EGQKTAVFEI
     VDALGTAPHV HALPVGNAGN ITAYWKGYTE YHADGLIDRL PRMLGTQAAG AAPLVLGEPV
     SHPETIATAI RIGSPASWTS AVEAQQQSKG RFLAATDEEI LAAYHLVARA EGVFVEPASA
     ASIAGLLKAI DGGWVARGST VVCTITGNGL KDPDTALKDM PSVSPVPVDA VAVVEQLGLV