ID   THRC_EREGS              Reviewed;         512 AA.
AC   Q00063;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   24-JAN-2024, entry version 133.
DE   RecName: Full=Threonine synthase;
DE            Short=TS;
DE            EC=4.2.3.1;
GN   Name=THR4; OrderedLocusNames=AAR059C;
OS   Eremothecium gossypii (strain ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL
OS   Y-1056) (Yeast) (Ashbya gossypii).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Eremothecium.
OX   NCBI_TaxID=284811;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX   PubMed=8569689; DOI=10.1007/bf02191826;
RA   Altmann-Joehl R., Philippsen P.;
RT   "AgTHR4, a new selection marker for transformation of the filamentous
RT   fungus Ashbya gossypii, maps in a four-gene cluster that is conserved
RT   between A. gossypii and Saccharomyces cerevisiae.";
RL   Mol. Gen. Genet. 250:69-80(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX   PubMed=15001715; DOI=10.1126/science.1095781;
RA   Dietrich F.S., Voegeli S., Brachat S., Lerch A., Gates K., Steiner S.,
RA   Mohr C., Poehlmann R., Luedi P., Choi S., Wing R.A., Flavier A.,
RA   Gaffney T.D., Philippsen P.;
RT   "The Ashbya gossypii genome as a tool for mapping the ancient Saccharomyces
RT   cerevisiae genome.";
RL   Science 304:304-307(2004).
RN   [3]
RP   GENOME REANNOTATION.
RC   STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX   PubMed=23749448; DOI=10.1534/g3.112.002881;
RA   Dietrich F.S., Voegeli S., Kuo S., Philippsen P.;
RT   "Genomes of Ashbya fungi isolated from insects reveal four mating-type
RT   loci, numerous translocations, lack of transposons, and distinct gene
RT   duplications.";
RL   G3 (Bethesda) 3:1225-1239(2013).
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; X91046; CAA62506.1; -; Genomic_DNA.
DR   EMBL; AE016814; AAS50424.1; -; Genomic_DNA.
DR   PIR; S61905; S61905.
DR   RefSeq; NP_982600.1; NM_207953.1.
DR   AlphaFoldDB; Q00063; -.
DR   SMR; Q00063; -.
DR   STRING; 284811.Q00063; -.
DR   EnsemblFungi; AAS50424; AAS50424; AGOS_AAR059C.
DR   GeneID; 4618427; -.
DR   KEGG; ago:AGOS_AAR059C; -.
DR   eggNOG; KOG2616; Eukaryota.
DR   HOGENOM; CLU_015170_1_0_1; -.
DR   InParanoid; Q00063; -.
DR   OMA; FDDCQDM; -.
DR   OrthoDB; 275600at2759; -.
DR   UniPathway; UPA00050; UER00065.
DR   Proteomes; UP000000591; Chromosome I.
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   3: Inferred from homology;
KW   Amino-acid biosynthesis; Lyase; Pyridoxal phosphate; Reference proteome;
KW   Threonine biosynthesis.
FT   CHAIN           1..512
FT                   /note="Threonine synthase"
FT                   /id="PRO_0000185643"
FT   MOD_RES         121
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   512 AA;  58925 MW;  E527C4E449881671 CRC64;
     MSQVYRSTRS SSEDTKSFEE AVIQGLAEDG GLFLPAVIPR LREETLFEHW AHLSFQDLAM
     EIMKFYIADW EIPAPELREL IERSYSSFRS EEVTPLRKNV TGDDENLHIL ELFHGPTYAF
     KDVALQFVGN LFEYFLERKN RDVSEEERTH LTVVGATSGD TGSAAIYGLR GKQDVSVFIL
     YPHGRISPIQ EEQMTTVEDE NVHTMAIEGS FDNCQDIVKS IFVDEEFNRK HNIAAVNSIN
     WARILAQITY YFYSYFRATD GQPGRVKFIV PSGNFGDILA GFYAKQMGLP IEKLVIATNE
     NDILDRFLRE GVYERSEDVT ATHSPAMDIL VSSNFERLLW FFAREQLAQG DDQEAGSIVN
     RWFEQLREER RFDVPEHLLD AIRYHFDSER VDNYNTLASI RHIYEHAQNP ERYVIDPHTA
     VGICAANRQI AHDQNNEIHY ISLATAHPAK FADAVNEALS SYDDYNFDDV LPDRLRRLGD
     LEKRIKYVDN TDVDVIKSII EEELINMGIY NP
//