TRP_YEAST
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 03-AUG-2022, entry version 205.
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; 39.
DR DIP; DIP-1398N; -.
DR IntAct; P00931; 13.
DR MINT; P00931; -.
DR STRING; 4932.YGL026C; -.
DR iPTMnet; P00931; -.
DR MaxQB; P00931; -.
DR PaxDb; P00931; -.
DR PRIDE; P00931; -.
DR EnsemblFungi; YGL026C_mRNA; YGL026C; YGL026C.
DR GeneID; 852858; -.
DR KEGG; sce:YGL026C; -.
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 BioCyc; YEAST:YGL026C-MON; -.
DR UniPathway; UPA00035; UER00044.
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; 3.20.20.70; -; 1.
DR Gene3D; 3.40.50.1100; -; 2.
DR HAMAP; MF_00131; Trp_synth_alpha; 1.
DR HAMAP; MF_00133; Trp_synth_beta; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR001926; PLP-dep.
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; IPR036052; Trypto_synt_PLP_dependent.
DR Pfam; PF00291; PALP; 1.
DR Pfam; PF00290; Trp_syntA; 1.
DR SUPFAM; SSF51366; SSF51366; 1.
DR SUPFAM; SSF53686; SSF53686; 1.
DR TIGRFAMs; TIGR00262; trpA; 1.
DR TIGRFAMs; TIGR00263; trpB; 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
