ID   THRC_ALKHC              Reviewed;         354 AA.
AC   Q9K7E3;
DT   11-JUL-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   03-AUG-2022, entry version 117.
DE   RecName: Full=Threonine synthase;
DE            Short=TS;
DE            EC=4.2.3.1;
GN   Name=thrC; OrderedLocusNames=BH3421;
OS   Alkalihalobacillus halodurans (strain ATCC BAA-125 / DSM 18197 / FERM 7344
OS   / JCM 9153 / C-125) (Bacillus halodurans).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Alkalihalobacillus.
OX   NCBI_TaxID=272558;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-125 / DSM 18197 / FERM 7344 / JCM 9153 / C-125;
RX   PubMed=11058132; DOI=10.1093/nar/28.21.4317;
RA   Takami H., Nakasone K., Takaki Y., Maeno G., Sasaki R., Masui N., Fuji F.,
RA   Hirama C., Nakamura Y., Ogasawara N., Kuhara S., Horikoshi K.;
RT   "Complete genome sequence of the alkaliphilic bacterium Bacillus halodurans
RT   and genomic sequence comparison with Bacillus subtilis.";
RL   Nucleic Acids Res. 28:4317-4331(2000).
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; BA000004; BAB07140.1; -; Genomic_DNA.
DR   PIR; E84077; E84077.
DR   RefSeq; WP_010899559.1; NC_002570.2.
DR   AlphaFoldDB; Q9K7E3; -.
DR   SMR; Q9K7E3; -.
DR   STRING; 272558.10176044; -.
DR   PRIDE; Q9K7E3; -.
DR   EnsemblBacteria; BAB07140; BAB07140; BAB07140.
DR   KEGG; bha:BH3421; -.
DR   eggNOG; COG0498; Bacteria.
DR   HOGENOM; CLU_028142_0_0_9; -.
DR   OMA; MWGFQAS; -.
DR   OrthoDB; 428821at2; -.
DR   UniPathway; UPA00050; UER00065.
DR   Proteomes; UP000001258; 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..354
FT                   /note="Threonine synthase"
FT                   /id="PRO_0000185624"
FT   BINDING         87
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000250"
FT   BINDING         187..191
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000250"
FT   BINDING         316
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         61
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   354 AA;  37665 MW;  D25EABAB4952C691 CRC64;
     MSQWRGLLQE YKEFLPVTEE TPLLTLGEGN TPLIPLENLS KEWGVKAYVK YEGANPTGSF
     KDRGMVMAVA KAKEEGSRTI ICASTGNTSA AAAAYGARAG LRCIVVIPEG KIALGKLAQA
     VMYGAEVLEI KGNFDHALDI VRSISEKEPI TLVNSVNPYR IEGQKTSAFE ICDALGQAPD
     VLAIPVGNAG NITAYWKGFK EYHEKKGTGL PQMRGFEAEG AAAIVRNQVI EEPETIATAI
     RIGNPASWTY AVEAAAESNG KIDEVTDEEI LAAYQLLAQK EGVFAEPASC ASIAGLRKQI
     ASGEIKKGST VVCVLTGNGL KDPNTAMSTI DVNPAVLPND EQAFLDHIKG GVPK