ID   THRC_METGL              Reviewed;         475 AA.
AC   P37145;
DT   01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1994, sequence version 1.
DT   13-SEP-2023, entry version 82.
DE   RecName: Full=Threonine synthase;
DE            Short=TS;
DE            EC=4.2.3.1;
GN   Name=thrC;
OS   Methylobacillus glycogenes.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Nitrosomonadales;
OC   Methylophilaceae; Methylobacillus.
OX   NCBI_TaxID=406;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 21371 / DSM 1760 / JCM 2853 / NCIMB 1210 / M 135-7;
RX   PubMed=8117070; DOI=10.1128/aem.60.1.111-119.1994;
RA   Motoyama H., Maki K., Anazawa H., Ishino S., Teshiba S.;
RT   "Cloning and nucleotide sequences of the homoserine dehydrogenase genes
RT   (hom) and the threonine synthase genes (thrC) of the Gram-negative obligate
RT   methylotroph Methylobacillus glycogenes.";
RL   Appl. Environ. Microbiol. 60:111-119(1994).
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; D14071; BAA40416.1; -; Genomic_DNA.
DR   AlphaFoldDB; P37145; -.
DR   SMR; P37145; -.
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; cd01560; Thr-synth_2; 1.
DR   Gene3D; 3.40.50.1100; -; 2.
DR   Gene3D; 3.90.1380.10; Threonine synthase, N-terminal domain; 1.
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; IPR001926; TrpB-like_PALP.
DR   InterPro; IPR036052; TrpB-like_PALP_sf.
DR   NCBIfam; TIGR00260; thrC; 1.
DR   PANTHER; PTHR42690; THREONINE SYNTHASE FAMILY MEMBER; 1.
DR   PANTHER; PTHR42690:SF1; THREONINE SYNTHASE-LIKE 2; 1.
DR   Pfam; PF00291; PALP; 1.
DR   Pfam; PF14821; Thr_synth_N; 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..475
FT                   /note="Threonine synthase"
FT                   /id="PRO_0000185635"
FT   MOD_RES         120
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   475 AA;  52115 MW;  2520D44EAA16E831 CRC64;
     MKYISTRGQS PALSFSEILL GGLAPDGGLY LPEQYPQFSA DALSAMRGMN YRDLAFTILS
     RLIDDIPADD LRIIVDKTYR ADVYAYARPG QDAEDITPTY KLEDDLYLLS LSNGPTLAFK
     DMAMQLLGNL FEYVLAQKGE TTNILGATSG DTGSAAEYAM RGKQGVKVFM LSPHQKMSRF
     QTAQMFSLQD DNIFNIAVKG VFDDCQDIVK AVSNDHAFKA KNKIGAVNSI NWARVAAQVV
     YYFKGYFAVT ADNAQQVSFA VPSGNFGNVC AGHIARMMGL PIAKLVVATN ENDVLDEFFK
     TGVYRPRGSA NTYHTSSPSM DISKASNFER FVFDLVGRDA AKVRELWGKV DAGGSFDLND
     GGWFAKVADY GFVSGSSNHA NRMQTIKATH ERYGVTIDTH TADGLKVALE HREAGTPMLV
     LETALPAKFE DAIVEALGHK PERPHSLEGL ESLPQRFEVM EADAAVIKQF IVEHI
//