ID   TRP_YEAST               Reviewed;         707 AA.
AC   P00931; D6VUB2;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   21-JUL-1986, sequence version 1.
DT   27-MAR-2024, entry version 210.
DE   RecName: Full=Tryptophan synthase;
DE            EC=4.2.1.20;
GN   Name=TRP5; OrderedLocusNames=YGL026C;
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].
RX   PubMed=6276387; DOI=10.1016/s0021-9258(19)68220-7;
RA   Zalkin H., Yanofsky C.;
RT   "Yeast gene TRP5: structure, function, regulation.";
RL   J. Biol. Chem. 257:1491-1500(1982).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=9169869;
RA   Tettelin H., Agostoni-Carbone M.L., Albermann K., Albers M., Arroyo J.,
RA   Backes U., Barreiros T., Bertani I., Bjourson A.J., Brueckner M.,
RA   Bruschi C.V., Carignani G., Castagnoli L., Cerdan E., Clemente M.L.,
RA   Coblenz A., Coglievina M., Coissac E., Defoor E., Del Bino S., Delius H.,
RA   Delneri D., de Wergifosse P., Dujon B., Durand P., Entian K.-D., Eraso P.,
RA   Escribano V., Fabiani L., Fartmann B., Feroli F., Feuermann M.,
RA   Frontali L., Garcia-Gonzalez M., Garcia-Saez M.I., Goffeau A.,
RA   Guerreiro P., Hani J., Hansen M., Hebling U., Hernandez K., Heumann K.,
RA   Hilger F., Hofmann B., Indge K.J., James C.M., Klima R., Koetter P.,
RA   Kramer B., Kramer W., Lauquin G., Leuther H., Louis E.J., Maillier E.,
RA   Marconi A., Martegani E., Mazon M.J., Mazzoni C., McReynolds A.D.K.,
RA   Melchioretto P., Mewes H.-W., Minenkova O., Mueller-Auer S., Nawrocki A.,
RA   Netter P., Neu R., Nombela C., Oliver S.G., Panzeri L., Paoluzi S.,
RA   Plevani P., Portetelle D., Portillo F., Potier S., Purnelle B., Rieger M.,
RA   Riles L., Rinaldi T., Robben J., Rodrigues-Pousada C.,
RA   Rodriguez-Belmonte E., Rodriguez-Torres A.M., Rose M., Ruzzi M.,
RA   Saliola M., Sanchez-Perez M., Schaefer B., Schaefer M., Scharfe M.,
RA   Schmidheini T., Schreer A., Skala J., Souciet J.-L., Steensma H.Y.,
RA   Talla E., Thierry A., Vandenbol M., van der Aart Q.J.M., Van Dyck L.,
RA   Vanoni M., Verhasselt P., Voet M., Volckaert G., Wambutt R., Watson M.D.,
RA   Weber N., Wedler E., Wedler H., Wipfli P., Wolf K., Wright L.F.,
RA   Zaccaria P., Zimmermann M., Zollner A., Kleine K.;
RT   "The nucleotide sequence of Saccharomyces cerevisiae chromosome VII.";
RL   Nature 387:81-84(1997).
RN   [3]
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   [4]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-172.
RX   PubMed=6282714; DOI=10.1016/0378-1119(82)90076-2;
RA   Brosius J., Walz A.;
RT   "DNA sequences flanking an E. coli insertion element IS2 in a cloned yeast
RT   TRP5 gene.";
RL   Gene 17:223-228(1982).
RN   [5]
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   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-540 AND SER-683, AND
RP   IDENTIFICATION BY 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   [7]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=19779198; DOI=10.1126/science.1172867;
RA   Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
RT   "Global analysis of Cdk1 substrate phosphorylation sites provides insights
RT   into evolution.";
RL   Science 325:1682-1686(2009).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(1S,2R)-1-C-(indol-3-yl)glycerol 3-phosphate + L-serine = D-
CC         glyceraldehyde 3-phosphate + H2O + L-tryptophan;
CC         Xref=Rhea:RHEA:10532, ChEBI:CHEBI:15377, ChEBI:CHEBI:33384,
CC         ChEBI:CHEBI:57912, ChEBI:CHEBI:58866, ChEBI:CHEBI:59776; EC=4.2.1.20;
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC   -!- PATHWAY: Amino-acid biosynthesis; L-tryptophan biosynthesis; L-
CC       tryptophan from chorismate: step 5/5.
CC   -!- MISCELLANEOUS: Present with 15500 molecules/cell in log phase SD
CC       medium. {ECO:0000269|PubMed:14562106}.
CC   -!- SIMILARITY: In the N-terminal section; belongs to the TrpA family.
CC       {ECO:0000305}.
CC   -!- SIMILARITY: In the C-terminal section; belongs to the TrpB family.
CC       {ECO:0000305}.
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DR   EMBL; V01342; CAA24635.1; -; Genomic_DNA.
DR   EMBL; V01343; CAA24636.1; -; Genomic_DNA.
DR   EMBL; Z72548; CAA96727.1; -; Genomic_DNA.
DR   EMBL; BK006941; DAA08073.1; -; Genomic_DNA.
DR   PIR; A01154; TSBYAB.
DR   RefSeq; NP_011489.1; NM_001180891.1.
DR   AlphaFoldDB; P00931; -.
DR   SMR; P00931; -.
DR   BioGRID; 33221; 47.
DR   DIP; DIP-1398N; -.
DR   IntAct; P00931; 13.
DR   MINT; P00931; -.
DR   STRING; 4932.YGL026C; -.
DR   GlyGen; P00931; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; P00931; -.
DR   MaxQB; P00931; -.
DR   PaxDb; 4932-YGL026C; -.
DR   PeptideAtlas; P00931; -.
DR   EnsemblFungi; YGL026C_mRNA; YGL026C; YGL026C.
DR   GeneID; 852858; -.
DR   KEGG; sce:YGL026C; -.
DR   AGR; SGD:S000002994; -.
DR   SGD; S000002994; TRP5.
DR   VEuPathDB; FungiDB:YGL026C; -.
DR   eggNOG; KOG1395; Eukaryota.
DR   eggNOG; KOG4175; Eukaryota.
DR   HOGENOM; CLU_016734_1_1_1; -.
DR   InParanoid; P00931; -.
DR   OMA; VDTARHS; -.
DR   OrthoDB; 9569at2759; -.
DR   BioCyc; YEAST:YGL026C-MONOMER; -.
DR   UniPathway; UPA00035; UER00044.
DR   BioGRID-ORCS; 852858; 2 hits in 10 CRISPR screens.
DR   PRO; PR:P00931; -.
DR   Proteomes; UP000002311; Chromosome VII.
DR   RNAct; P00931; Protein.
DR   GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR   GO; GO:0005634; C:nucleus; HDA:SGD.
DR   GO; GO:0004834; F:tryptophan synthase activity; IDA:SGD.
DR   GO; GO:0000162; P:tryptophan biosynthetic process; IMP:SGD.
DR   CDD; cd06446; Trp-synth_B; 1.
DR   CDD; cd04724; Tryptophan_synthase_alpha; 1.
DR   Gene3D; 3.40.50.1100; -; 2.
DR   Gene3D; 3.20.20.70; Aldolase class I; 1.
DR   HAMAP; MF_00131; Trp_synth_alpha; 1.
DR   HAMAP; MF_00133; Trp_synth_beta; 1.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR011060; RibuloseP-bd_barrel.
DR   InterPro; IPR006653; Trp_synth_b_CS.
DR   InterPro; IPR006654; Trp_synth_beta.
DR   InterPro; IPR023026; Trp_synth_beta/beta-like.
DR   InterPro; IPR018204; Trp_synthase_alpha_AS.
DR   InterPro; IPR002028; Trp_synthase_suA.
DR   InterPro; IPR001926; TrpB-like_PALP.
DR   InterPro; IPR036052; TrpB-like_PALP_sf.
DR   NCBIfam; TIGR00262; trpA; 1.
DR   NCBIfam; TIGR00263; trpB; 1.
DR   PANTHER; PTHR48077:SF3; TRYPTOPHAN SYNTHASE; 1.
DR   PANTHER; PTHR48077; TRYPTOPHAN SYNTHASE-RELATED; 1.
DR   Pfam; PF00291; PALP; 1.
DR   Pfam; PF00290; Trp_syntA; 1.
DR   SUPFAM; SSF51366; Ribulose-phoshate binding barrel; 1.
DR   SUPFAM; SSF53686; Tryptophan synthase beta subunit-like PLP-dependent enzymes; 1.
DR   PROSITE; PS00167; TRP_SYNTHASE_ALPHA; 1.
DR   PROSITE; PS00168; TRP_SYNTHASE_BETA; 1.
PE   1: Evidence at protein level;
KW   Amino-acid biosynthesis; Aromatic amino acid biosynthesis; Lyase;
KW   Phosphoprotein; Pyridoxal phosphate; Reference proteome;
KW   Tryptophan biosynthesis.
FT   CHAIN           1..707
FT                   /note="Tryptophan synthase"
FT                   /id="PRO_0000098726"
FT   REGION          1..297
FT                   /note="Tryptophan synthase alpha chain"
FT   REGION          298..707
FT                   /note="Tryptophan synthase beta chain"
FT   ACT_SITE        50
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        61
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         384
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         540
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18407956"
FT   MOD_RES         683
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18407956"
SQ   SEQUENCE   707 AA;  76626 MW;  F5241A0127A2D166 CRC64;
     MSEQLRQTFA NAKKENRNAL VTFMTAGYPT VKDTVPILKG FQDGGVDIIE LGMPFSDPIA
     DGPTIQLSNT VALQNGVTLP QTLEMVSQAR NEGVTVPIIL MGYYNPILNY GEERFIQDAA
     KAGANGFIIV DLPPEEALKV RNYINDNGLS LIPLVAPSTT DERLELLSHI ADSFVYVVSR
     MGTTGVQSSV ASDLDELISR VRKYTKDTPL AVGFGVSTRE HFQSVGSVAD GVVIGSKIVT
     LCGDAPEGKR YDVAKEYVQG ILNGAKHKVL SKDEFFAFQK ESLKSANVKK EILDEFDENH
     KHPIRFGDFG GQYVPEALHA CLRELEKGFD EAVADPTFWE DFKSLYSYIG RPSSLHKAER
     LTEHCQGAQI WLKREDLNHT GSHKINNALA QVLLAKRLGK KNVIAETGAG QHGVATATAC
     AKFGLTCTVF MGAEDVRRQA LNVFRMRILG AKVIAVTNGT KTLRDATSEA FRFWVTNLKT
     TYYVVGSAIG PHPYPTLVRT FQSVIGKETK EQFAAMNNGK LPDAVVACVG GGSNSTGMFS
     PFEHDTSVKL LGVEAGGDGV DTKFHSATLT AGRPGVFHGV KTYVLQDSDG QVHDTHSVSA
     GLDYPGVGPE LAYWKSTGRA QFIAATDAQA LLGFKLLSQL EGIIPALESS HAVYGACELA
     KTMKPDQHLV INISGRGDKD VQSVAEVLPK LGPKIGWDLR FEEDPSA
//