ID   THRC_METAC              Reviewed;         405 AA.
AC   Q8TQD4;
DT   23-MAR-2010, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2002, sequence version 1.
DT   03-AUG-2022, entry version 105.
DE   RecName: Full=Threonine synthase;
DE            Short=TS;
DE            EC=4.2.3.1;
GN   Name=thrC; OrderedLocusNames=MA_1610;
OS   Methanosarcina acetivorans (strain ATCC 35395 / DSM 2834 / JCM 12185 /
OS   C2A).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC   Methanosarcinales; Methanosarcinaceae; Methanosarcina.
OX   NCBI_TaxID=188937;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35395 / DSM 2834 / JCM 12185 / C2A;
RX   PubMed=11932238; DOI=10.1101/gr.223902;
RA   Galagan J.E., Nusbaum C., Roy A., Endrizzi M.G., Macdonald P., FitzHugh W.,
RA   Calvo S., Engels R., Smirnov S., Atnoor D., Brown A., Allen N., Naylor J.,
RA   Stange-Thomann N., DeArellano K., Johnson R., Linton L., McEwan P.,
RA   McKernan K., Talamas J., Tirrell A., Ye W., Zimmer A., Barber R.D.,
RA   Cann I., Graham D.E., Grahame D.A., Guss A.M., Hedderich R.,
RA   Ingram-Smith C., Kuettner H.C., Krzycki J.A., Leigh J.A., Li W., Liu J.,
RA   Mukhopadhyay B., Reeve J.N., Smith K., Springer T.A., Umayam L.A.,
RA   White O., White R.H., de Macario E.C., Ferry J.G., Jarrell K.F., Jing H.,
RA   Macario A.J.L., Paulsen I.T., Pritchett M., Sowers K.R., Swanson R.V.,
RA   Zinder S.H., Lander E., Metcalf W.W., Birren B.;
RT   "The genome of Methanosarcina acetivorans reveals extensive metabolic and
RT   physiological diversity.";
RL   Genome Res. 12:532-542(2002).
RN   [2]
RP   FUNCTION, CATALYTIC ACTIVITY, COFACTOR, DOMAIN, AND SUBUNIT.
RX   PubMed=19761441; DOI=10.1042/bj20090999;
RA   Graham D.E., Taylor S.M., Wolf R.Z., Namboori S.C.;
RT   "Convergent evolution of coenzyme M biosynthesis in the Methanosarcinales:
RT   cysteate synthase evolved from an ancestral threonine synthase.";
RL   Biochem. J. 424:467-478(2009).
CC   -!- FUNCTION: Catalyzes the gamma-elimination of phosphate from L-
CC       phosphohomoserine and the beta-addition of water to produce L-
CC       threonine. Does not catalyze the conversion of O-acetyl-L-homoserine
CC       into threonine. {ECO:0000269|PubMed:19761441}.
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         Evidence={ECO:0000269|PubMed:19761441};
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000269|PubMed:19761441};
CC   -!- PATHWAY: Amino-acid biosynthesis; L-threonine biosynthesis; L-threonine
CC       from L-aspartate: step 5/5.
CC   -!- SUBUNIT: Homotrimer. {ECO:0000269|PubMed:19761441}.
CC   -!- DOMAIN: The N-terminal 41 amino acids are required for activity.
CC       {ECO:0000269|PubMed:19761441}.
CC   -!- SIMILARITY: Belongs to the threonine synthase family. {ECO:0000305}.
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DR   EMBL; AE010299; AAM05023.1; -; Genomic_DNA.
DR   RefSeq; WP_011021620.1; NC_003552.1.
DR   AlphaFoldDB; Q8TQD4; -.
DR   SMR; Q8TQD4; -.
DR   STRING; 188937.MA_1610; -.
DR   PRIDE; Q8TQD4; -.
DR   EnsemblBacteria; AAM05023; AAM05023; MA_1610.
DR   GeneID; 1473498; -.
DR   KEGG; mac:MA_1610; -.
DR   HOGENOM; CLU_028142_4_1_2; -.
DR   InParanoid; Q8TQD4; -.
DR   OMA; MWGFQAS; -.
DR   OrthoDB; 16594at2157; -.
DR   PhylomeDB; Q8TQD4; -.
DR   UniPathway; UPA00050; UER00065.
DR   Proteomes; UP000002487; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0004795; F:threonine synthase activity; IBA:GO_Central.
DR   GO; GO:0019344; P:cysteine biosynthetic process; IBA:GO_Central.
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   1: Evidence at protein level;
KW   Amino-acid biosynthesis; Lyase; Pyridoxal phosphate; Reference proteome;
KW   Threonine biosynthesis.
FT   CHAIN           1..405
FT                   /note="Threonine synthase"
FT                   /id="PRO_0000392651"
FT   BINDING         130
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000250"
FT   BINDING         231..235
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000250"
FT   BINDING         369
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         104
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   405 AA;  43285 MW;  3D2A303B42A4D942 CRC64;
     MYHLKCIECG AEYSRDEVIY TCSKCDGLLD VIYDYSSIKI DMEKLKTECP SVWKYAKLLP
     VEREPVTIQE GGTPLYKCDR LAEKIGIKKL YVKHEGMNPT GSFKDRGMTV GVTKALELGM
     NTVACASTGN TSAALAIYGA KAGIPVVVLL PAGKVALGKV AQALMHGAKV LSIRGNFDDA
     LALVRTLCSQ EKIYLLNSIN PYRLEGQKTI GFEIADQLDF KVPDRIVLPV GNAGNITAIY
     KGFREFKILG ITDSLPKMTG IQAEGSCPIV KAIKSGAPAI TPEENPETVA TAIRIGNPVN
     ATKALSAIRE SGGTAESVTD EEILAAQKDL ARLEGIGVEP ASAASVAGLR KLVDMGVIGR
     DETVVCITTG HLLKDPQTVI DVCEEPTVVD ANIDAIREAI FGKAK