ID   THRC_BACSL              Reviewed;         352 AA.
AC   P09123;
DT   01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1989, sequence version 1.
DT   13-SEP-2023, entry version 94.
DE   RecName: Full=Threonine synthase;
DE            Short=TS;
DE            EC=4.2.3.1;
GN   Name=thrC;
OS   Bacillus sp. (strain ULM1).
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=231717;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=3186450; DOI=10.1093/nar/16.20.9859;
RA   Malumbres M., Mateos L.M., Guerrero C., Martin J.F.;
RT   "Nucleotide sequence of the threonine synthase (thrC) gene of
RT   Brevibacterium lactofermentum.";
RL   Nucleic Acids Res. 16:9859-9859(1988).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=8768250; DOI=10.1007/bf02818515;
RA   Malumbres M., Mateos L.M., Guerrero C., Martin J.F.;
RT   "Molecular cloning of the hom-thrC-thrB cluster from Bacillus sp. ULM1:
RT   expression of the thrC gene in Escherichia coli and corynebacteria, and
RT   evolutionary relationships of the threonine genes.";
RL   Folia Microbiol. (Praha) 40:595-606(1995).
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}.
CC   -!- CAUTION: Was originally thought to originate from
CC       B.lactofermentum=C.glutamicum. {ECO:0000305|PubMed:3186450}.
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DR   EMBL; Z29562; CAA82669.1; -; Genomic_DNA.
DR   AlphaFoldDB; P09123; -.
DR   SMR; P09123; -.
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   CDD; cd01563; Thr-synth_1; 1.
DR   Gene3D; 3.40.50.1100; -; 2.
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; ACT DOMAIN-CONTAINING PROTEIN; 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;
KW   Threonine biosynthesis.
FT   CHAIN           1..352
FT                   /note="Threonine synthase"
FT                   /id="PRO_0000185625"
FT   BINDING         85
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000250"
FT   BINDING         185..189
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000250"
FT   BINDING         314
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         59
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   352 AA;  37458 MW;  192550176FAD7930 CRC64;
     MYKGLLKQYA SYLPVNEKTP DVSLMEGNTP LIPLLNISKQ LGVQLYGKYE GANPTGSFKD
     RGMVMAVAKA KEEGSEAIIC ASTGNTSASA AAYAARLGMK CIIVIPEGKI AHGKLAQAVA
     YGAEIISIEG NFDDALKAVR NIAAEEPITL VNSVNPYRIE GQKTAAFEIC DQLQNAPDVL
     AIPVGNAGNI TAYWKGFCEY EKEKGYKKPR IHGFEAEGAA AIVKGHVIEE PETIATAIRI
     GNPASWSYAV EAAEQSHGEI DMVSDEEILH AYRLLAKTEG VFAEPGSNAS LAGVIKHVES
     GKIKKGETVV AVLTGNGLKD PDIAISSNQL DIASVSNDIE QIKDHIKGVI MS
//