THRC_SCHPO
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 03-AUG-2022, entry version 144.
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; 4896.SPAC9E9.06c.1; -.
DR iPTMnet; Q42598; -.
DR MaxQB; Q42598; -.
DR PaxDb; Q42598; -.
DR PRIDE; Q42598; -.
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; FGRIAFQ; -.
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; ISO:PomBase.
DR GO; GO:0009088; P:threonine biosynthetic process; ISS:PomBase.
DR Gene3D; 3.40.50.1100; -; 2.
DR Gene3D; 3.90.1380.10; -; 1.
DR InterPro; IPR001926; PLP-dep.
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; IPR036052; Trypto_synt_PLP_dependent.
DR Pfam; PF00291; PALP; 1.
DR Pfam; PF14821; Thr_synth_N; 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; 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
