ID   THRC_SCHPO              Reviewed;         514 AA.
AC   Q42598; P78841;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   27-MAR-2024, entry version 151.
DE   RecName: Full=Threonine synthase;
DE            Short=TS;
DE            EC=4.2.3.1;
GN   Name=thrc; ORFNames=SPAC9E9.06c;
OS   Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC   Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC   Schizosaccharomyces.
OX   NCBI_TaxID=284812;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=972 / ATCC 24843;
RA   Aas S.F., Rognes S.E.;
RT   "Isolation of cDNA encoding threonine synthase from Schizosaccharomyces
RT   pombe by functional expression in Saccharomyces cerevisiae.";
RL   Submitted (OCT-1997) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=972 / ATCC 24843;
RX   PubMed=11859360; DOI=10.1038/nature724;
RA   Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA   Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA   Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA   Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA   Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA   Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA   Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA   Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA   O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA   Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA   Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA   Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA   Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA   Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA   Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA   Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA   Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA   Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA   Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA   Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA   del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA   Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA   Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA   Nurse P.;
RT   "The genome sequence of Schizosaccharomyces pombe.";
RL   Nature 415:871-880(2002).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 147-514.
RC   STRAIN=PR745;
RX   PubMed=9501991; DOI=10.1093/dnares/4.6.363;
RA   Yoshioka S., Kato K., Nakai K., Okayama H., Nojima H.;
RT   "Identification of open reading frames in Schizosaccharomyces pombe
RT   cDNAs.";
RL   DNA Res. 4:363-369(1997).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-319 AND SER-321, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY.
RX   PubMed=18257517; DOI=10.1021/pr7006335;
RA   Wilson-Grady J.T., Villen J., Gygi S.P.;
RT   "Phosphoproteome analysis of fission yeast.";
RL   J. Proteome Res. 7:1088-1097(2008).
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 (Ref.1) thought to originate from A.thaliana.
CC       {ECO:0000305}.
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DR   EMBL; Z46263; CAA86405.1; -; mRNA.
DR   EMBL; CU329670; CAB16415.1; -; Genomic_DNA.
DR   EMBL; D89190; BAA13852.1; -; mRNA.
DR   PIR; T39213; T39213.
DR   PIR; T42748; T42748.
DR   RefSeq; NP_594579.1; NM_001020008.2.
DR   AlphaFoldDB; Q42598; -.
DR   SMR; Q42598; -.
DR   BioGRID; 279107; 1.
DR   STRING; 284812.Q42598; -.
DR   iPTMnet; Q42598; -.
DR   MaxQB; Q42598; -.
DR   PaxDb; 4896-SPAC9E9-06c-1; -.
DR   EnsemblFungi; SPAC9E9.06c.1; SPAC9E9.06c.1:pep; SPAC9E9.06c.
DR   GeneID; 2542653; -.
DR   KEGG; spo:SPAC9E9.06c; -.
DR   PomBase; SPAC9E9.06c; -.
DR   VEuPathDB; FungiDB:SPAC9E9.06c; -.
DR   eggNOG; KOG2616; Eukaryota.
DR   HOGENOM; CLU_015170_1_0_1; -.
DR   InParanoid; Q42598; -.
DR   OMA; FDDCQDM; -.
DR   PhylomeDB; Q42598; -.
DR   UniPathway; UPA00050; UER00065.
DR   PRO; PR:Q42598; -.
DR   Proteomes; UP000002485; Chromosome I.
DR   GO; GO:0005829; C:cytosol; HDA:PomBase.
DR   GO; GO:0005634; C:nucleus; HDA:PomBase.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0004795; F:threonine synthase activity; IBA:GO_Central.
DR   GO; GO:0009088; P:threonine biosynthetic process; IBA:GO_Central.
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   1: Evidence at protein level;
KW   Amino-acid biosynthesis; Lyase; Phosphoprotein; Pyridoxal phosphate;
KW   Reference proteome; Threonine biosynthesis.
FT   CHAIN           1..514
FT                   /note="Threonine synthase"
FT                   /id="PRO_0000185644"
FT   MOD_RES         117
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         319
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:18257517"
FT   MOD_RES         321
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:18257517"
FT   CONFLICT        253..254
FT                   /note="SV -> PA (in Ref. 3; BAA13852)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        446
FT                   /note="C -> W (in Ref. 3; BAA13852)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        456
FT                   /note="D -> G (in Ref. 3; BAA13852)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        459
FT                   /note="V -> G (in Ref. 3; BAA13852)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   514 AA;  57632 MW;  1C61AEFBB5F961C4 CRC64;
     MSSQVSYLST RGGSSNFSFE EAVLKGLAND GGLFIPSEIP QLPSGWIEAW KDKSFPEIAF
     EVMSLYIPRS EISADELKKL VDRSYSTFRH PETTPLKSLK NGLNVLELFH GPTFAFKDVA
     LQFLGNLFEF FLTRKNGNKP EDERDHLTVV GATSGDTGSA AIYGLRGKKD VSVFILFPNG
     RVSPIQEAQM TTVTDPNVHC ITVNGVFDDC QDLVKQIFGD VEFNKKHHIG AVNSINWARI
     LSQITYYLYS YLSVYKQGKA DDVRFIVPTG NFGDILAGYY AKRMGLPTKQ LVIATNENDI
     LNRFFKTGRY EKADSTQVSP SGPISAKETY SPAMDILVSS NFERYLWYLA LATEAPNHTP
     AEASEILSRW MNEFKRDGTV TVRPEVLEAA RRDFVSERVS NDETIDAIKK IYESDHYIID
     PHTAVGVETG LRCLEKTKDQ DITYICLSTA HPAKFDKAVN LALSSYSDYN FNTQVLPIEF
     DGLLDEERTC IFSGKPNIDI LKQIIEVTLS REKA
//