THRC_YEAST
ID THRC_YEAST Reviewed; 514 AA.
AC P16120; D6VR61; E9P943;
DT 01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-1990, sequence version 1.
DT 03-AUG-2022, entry version 189.
DE RecName: Full=Threonine synthase;
DE Short=TS;
DE EC=4.2.3.1;
GN Name=THR4; OrderedLocusNames=YCR053W; ORFNames=YCR53W;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 26786 / X2180-1A;
RX PubMed=2408022; DOI=10.1093/nar/18.3.665;
RA Aas S.F., Rognes S.E.;
RT "Nucleotide sequence of the yeast THR4 gene encoding threonine synthase.";
RL Nucleic Acids Res. 18:665-665(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2204248; DOI=10.1002/yea.320060408;
RA Mannhaupt G., van der Linden C.G., Vetter I., Maurer K., Pilz U.,
RA Planta R.J., Feldmann H.;
RT "Analysis of the THR4 region on chromosome III of the yeast Saccharomyces
RT cerevisiae.";
RL Yeast 6:353-361(1990).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=1574125; DOI=10.1038/357038a0;
RA Oliver S.G., van der Aart Q.J.M., Agostoni-Carbone M.L., Aigle M.,
RA Alberghina L., Alexandraki D., Antoine G., Anwar R., Ballesta J.P.G.,
RA Benit P., Berben G., Bergantino E., Biteau N., Bolle P.-A.,
RA Bolotin-Fukuhara M., Brown A., Brown A.J.P., Buhler J.-M., Carcano C.,
RA Carignani G., Cederberg H., Chanet R., Contreras R., Crouzet M.,
RA Daignan-Fornier B., Defoor E., Delgado M.D., Demolder J., Doira C.,
RA Dubois E., Dujon B., Duesterhoeft A., Erdmann D., Esteban M., Fabre F.,
RA Fairhead C., Faye G., Feldmann H., Fiers W., Francingues-Gaillard M.-C.,
RA Franco L., Frontali L., Fukuhara H., Fuller L.J., Galland P., Gent M.E.,
RA Gigot D., Gilliquet V., Glansdorff N., Goffeau A., Grenson M., Grisanti P.,
RA Grivell L.A., de Haan M., Haasemann M., Hatat D., Hoenicka J.,
RA Hegemann J.H., Herbert C.J., Hilger F., Hohmann S., Hollenberg C.P.,
RA Huse K., Iborra F., Indge K.J., Isono K., Jacq C., Jacquet M., James C.M.,
RA Jauniaux J.-C., Jia Y., Jimenez A., Kelly A., Kleinhans U., Kreisl P.,
RA Lanfranchi G., Lewis C., van der Linden C.G., Lucchini G.,
RA Lutzenkirchen K., Maat M.J., Mallet L., Mannhaupt G., Martegani E.,
RA Mathieu A., Maurer C.T.C., McConnell D., McKee R.A., Messenguy F.,
RA Mewes H.-W., Molemans F., Montague M.A., Muzi Falconi M., Navas L.,
RA Newlon C.S., Noone D., Pallier C., Panzeri L., Pearson B.M., Perea J.,
RA Philippsen P., Pierard A., Planta R.J., Plevani P., Poetsch B., Pohl F.M.,
RA Purnelle B., Ramezani Rad M., Rasmussen S.W., Raynal A., Remacha M.A.,
RA Richterich P., Roberts A.B., Rodriguez F., Sanz E.,
RA Schaaff-Gerstenschlaeger I., Scherens B., Schweitzer B., Shu Y., Skala J.,
RA Slonimski P.P., Sor F., Soustelle C., Spiegelberg R., Stateva L.I.,
RA Steensma H.Y., Steiner S., Thierry A., Thireos G., Tzermia M.,
RA Urrestarazu L.A., Valle G., Vetter I., van Vliet-Reedijk J.C., Voet M.,
RA Volckaert G., Vreken P., Wang H., Warmington J.R., von Wettstein D.,
RA Wicksteed B.L., Wilson C., Wurst H., Xu G., Yoshikawa A., Zimmermann F.K.,
RA Sgouros J.G.;
RT "The complete DNA sequence of yeast chromosome III.";
RL Nature 357:38-46(1992).
RN [4]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=17322287; DOI=10.1101/gr.6037607;
RA Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
RA Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J.,
RA Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J.,
RA Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D.,
RA LaBaer J.;
RT "Approaching a complete repository of sequence-verified protein-encoding
RT clones for Saccharomyces cerevisiae.";
RL Genome Res. 17:536-543(2007).
RN [6]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-467, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
RA Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT "A multidimensional chromatography technology for in-depth phosphoproteome
RT analysis.";
RL Mol. Cell. Proteomics 7:1389-1396(2008).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
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 -!- MISCELLANEOUS: Present with 26000 molecules/cell in log phase SD
CC medium. {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the threonine synthase family. {ECO:0000305}.
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DR EMBL; X17256; CAA35157.1; -; Genomic_DNA.
DR EMBL; X59720; CAA42284.1; -; Genomic_DNA.
DR EMBL; AY723762; AAU09679.1; -; Genomic_DNA.
DR EMBL; BK006937; DAA07530.1; -; Genomic_DNA.
DR PIR; S22836; SYBSR.
DR RefSeq; NP_009982.1; NM_001178767.1.
DR PDB; 1KL7; X-ray; 2.70 A; A/B=1-514.
DR PDBsum; 1KL7; -.
DR AlphaFoldDB; P16120; -.
DR SMR; P16120; -.
DR BioGRID; 31033; 775.
DR DIP; DIP-6522N; -.
DR IntAct; P16120; 5.
DR MINT; P16120; -.
DR STRING; 4932.YCR053W; -.
DR iPTMnet; P16120; -.
DR MaxQB; P16120; -.
DR PaxDb; P16120; -.
DR PRIDE; P16120; -.
DR TopDownProteomics; P16120; -.
DR DNASU; 850420; -.
DR EnsemblFungi; YCR053W_mRNA; YCR053W; YCR053W.
DR GeneID; 850420; -.
DR KEGG; sce:YCR053W; -.
DR SGD; S000000649; THR4.
DR VEuPathDB; FungiDB:YCR053W; -.
DR eggNOG; KOG2616; Eukaryota.
DR GeneTree; ENSGT00940000161144; -.
DR HOGENOM; CLU_015170_1_0_1; -.
DR InParanoid; P16120; -.
DR OMA; FGRIAFQ; -.
DR BioCyc; YEAST:YCR053W-MON; -.
DR BRENDA; 4.2.3.1; 984.
DR UniPathway; UPA00050; UER00065.
DR EvolutionaryTrace; P16120; -.
DR PRO; PR:P16120; -.
DR Proteomes; UP000002311; Chromosome III.
DR RNAct; P16120; protein.
DR GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR GO; GO:0005634; C:nucleus; HDA:SGD.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0004795; F:threonine synthase activity; IMP:SGD.
DR GO; GO:0009088; P:threonine biosynthetic process; IMP:SGD.
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 3D-structure; Amino-acid biosynthesis; Lyase; Phosphoprotein;
KW Pyridoxal phosphate; Reference proteome; Threonine biosynthesis.
FT CHAIN 1..514
FT /note="Threonine synthase"
FT /id="PRO_0000185645"
FT MOD_RES 124
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000250"
FT MOD_RES 467
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT CONFLICT 176
FT /note="K -> R (in Ref. 5; AAU09679)"
FT /evidence="ECO:0000305"
FT STRAND 8..10
FT /evidence="ECO:0007829|PDB:1KL7"
FT HELIX 21..27
FT /evidence="ECO:0007829|PDB:1KL7"
FT HELIX 46..51
FT /evidence="ECO:0007829|PDB:1KL7"
FT TURN 52..55
FT /evidence="ECO:0007829|PDB:1KL7"
FT HELIX 58..67
FT /evidence="ECO:0007829|PDB:1KL7"
FT TURN 72..74
FT /evidence="ECO:0007829|PDB:1KL7"
FT HELIX 77..87
FT /evidence="ECO:0007829|PDB:1KL7"
FT TURN 88..90
FT /evidence="ECO:0007829|PDB:1KL7"
FT STRAND 106..108
FT /evidence="ECO:0007829|PDB:1KL7"
FT STRAND 110..114
FT /evidence="ECO:0007829|PDB:1KL7"
FT HELIX 125..143
FT /evidence="ECO:0007829|PDB:1KL7"
FT STRAND 148..150
FT /evidence="ECO:0007829|PDB:1KL7"
FT STRAND 154..159
FT /evidence="ECO:0007829|PDB:1KL7"
FT STRAND 161..163
FT /evidence="ECO:0007829|PDB:1KL7"
FT HELIX 164..172
FT /evidence="ECO:0007829|PDB:1KL7"
FT STRAND 178..185
FT /evidence="ECO:0007829|PDB:1KL7"
FT HELIX 191..199
FT /evidence="ECO:0007829|PDB:1KL7"
FT STRAND 205..212
FT /evidence="ECO:0007829|PDB:1KL7"
FT HELIX 214..226
FT /evidence="ECO:0007829|PDB:1KL7"
FT HELIX 244..262
FT /evidence="ECO:0007829|PDB:1KL7"
FT STRAND 263..266
FT /evidence="ECO:0007829|PDB:1KL7"
FT STRAND 270..275
FT /evidence="ECO:0007829|PDB:1KL7"
FT STRAND 277..279
FT /evidence="ECO:0007829|PDB:1KL7"
FT HELIX 280..291
FT /evidence="ECO:0007829|PDB:1KL7"
FT STRAND 298..302
FT /evidence="ECO:0007829|PDB:1KL7"
FT HELIX 307..314
FT /evidence="ECO:0007829|PDB:1KL7"
FT STRAND 315..318
FT /evidence="ECO:0007829|PDB:1KL7"
FT HELIX 329..331
FT /evidence="ECO:0007829|PDB:1KL7"
FT HELIX 339..350
FT /evidence="ECO:0007829|PDB:1KL7"
FT HELIX 356..373
FT /evidence="ECO:0007829|PDB:1KL7"
FT STRAND 374..377
FT /evidence="ECO:0007829|PDB:1KL7"
FT HELIX 380..386
FT /evidence="ECO:0007829|PDB:1KL7"
FT TURN 387..389
FT /evidence="ECO:0007829|PDB:1KL7"
FT STRAND 390..394
FT /evidence="ECO:0007829|PDB:1KL7"
FT HELIX 397..410
FT /evidence="ECO:0007829|PDB:1KL7"
FT HELIX 421..437
FT /evidence="ECO:0007829|PDB:1KL7"
FT STRAND 442..448
FT /evidence="ECO:0007829|PDB:1KL7"
FT HELIX 452..455
FT /evidence="ECO:0007829|PDB:1KL7"
FT HELIX 456..463
FT /evidence="ECO:0007829|PDB:1KL7"
FT HELIX 471..474
FT /evidence="ECO:0007829|PDB:1KL7"
FT HELIX 478..481
FT /evidence="ECO:0007829|PDB:1KL7"
FT HELIX 483..485
FT /evidence="ECO:0007829|PDB:1KL7"
FT HELIX 498..506
FT /evidence="ECO:0007829|PDB:1KL7"
SQ SEQUENCE 514 AA; 57474 MW; EF6BA9DF56D94B6F CRC64;
MPNASQVYRS TRSSSPKTIS FEEAIIQGLA TDGGLFIPPT IPQVDQATLF NDWSKLSFQD
LAFAIMRLYI AQEEIPDADL KDLIKRSYST FRSDEVTPLV QNVTGDKENL HILELFHGPT
YAFKDVALQF VGNLFEYFLQ RTNANLPEGE KKQITVVGAT SGDTGSAAIY GLRGKKDVSV
FILYPTGRIS PIQEEQMTTV PDENVQTLSV TGTFDNCQDI VKAIFGDKEF NSKHNVGAVN
SINWARILAQ MTYYFYSFFQ ATNGKDSKKV KFVVPSGNFG DILAGYFAKK MGLPIEKLAI
ATNENDILDR FLKSGLYERS DKVAATLSPA MDILISSNFE RLLWYLAREY LANGDDLKAG
EIVNNWFQEL KTNGKFQVDK SIIEGASKDF TSERVSNEET SETIKKIYES SVNPKHYILD
PHTAVGVCAT ERLIAKDNDK SIQYISLSTA HPAKFADAVN NALSGFSNYS FEKDVLPEEL
KKLSTLKKKL KFIERADVEL VKNAIEEELA KMKL
