ID   TRPG_YEAST              Reviewed;         484 AA.
AC   P00937; D6VWZ2;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1994, sequence version 2.
DT   02-SEP-2026, entry version 221.
DE   RecName: Full=Multifunctional tryptophan biosynthesis protein;
DE   Includes:
DE     RecName: Full=Anthranilate synthase component 2;
DE              Short=AS;
DE              EC=4.1.3.27;
DE     AltName: Full=Anthranilate synthase, glutamine amidotransferase component;
DE   Includes:
DE     RecName: Full=Indole-3-glycerol phosphate synthase;
DE              EC=4.1.1.48;
DE     AltName: Full=PRAI;
GN   Name=TRP3; OrderedLocusNames=YKL211C;
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=6323449; DOI=10.1016/s0021-9258(17)43193-0;
RA   Zalkin H., Paluh J.L., van Cleemput M., Moye W.S., Yanofsky C.;
RT   "Nucleotide sequence of Saccharomyces cerevisiae genes TRP2 and TRP3
RT   encoding bifunctional anthranilate synthase: indole-3-glycerol phosphate
RT   synthase.";
RL   J. Biol. Chem. 259:3985-3992(1984).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 96604 / S288c / FY1679;
RX   PubMed=7941750; DOI=10.1002/yea.320100511;
RA   Tzermia M., Horaitis O., Alexandraki D.;
RT   "The complete sequencing of a 24.6 kb segment of yeast chromosome XI
RT   identified the known loci URA1, SAC1 and TRP3, and revealed 6 new open
RT   reading frames including homologues to the threonine dehydratases, membrane
RT   transporters, hydantoinases and the phospholipase A2-activating protein.";
RL   Yeast 10:663-679(1994).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=8196765; DOI=10.1038/369371a0;
RA   Dujon B., Alexandraki D., Andre B., Ansorge W., Baladron V.,
RA   Ballesta J.P.G., Banrevi A., Bolle P.-A., Bolotin-Fukuhara M., Bossier P.,
RA   Bou G., Boyer J., Buitrago M.J., Cheret G., Colleaux L.,
RA   Daignan-Fornier B., del Rey F., Dion C., Domdey H., Duesterhoeft A.,
RA   Duesterhus S., Entian K.-D., Erfle H., Esteban P.F., Feldmann H.,
RA   Fernandes L., Fobo G.M., Fritz C., Fukuhara H., Gabel C., Gaillon L.,
RA   Garcia-Cantalejo J.M., Garcia-Ramirez J.J., Gent M.E., Ghazvini M.,
RA   Goffeau A., Gonzalez A., Grothues D., Guerreiro P., Hegemann J.H.,
RA   Hewitt N., Hilger F., Hollenberg C.P., Horaitis O., Indge K.J.,
RA   Jacquier A., James C.M., Jauniaux J.-C., Jimenez A., Keuchel H.,
RA   Kirchrath L., Kleine K., Koetter P., Legrain P., Liebl S., Louis E.J.,
RA   Maia e Silva A., Marck C., Monnier A.-L., Moestl D., Mueller S.,
RA   Obermaier B., Oliver S.G., Pallier C., Pascolo S., Pfeiffer F.,
RA   Philippsen P., Planta R.J., Pohl F.M., Pohl T.M., Poehlmann R.,
RA   Portetelle D., Purnelle B., Puzos V., Ramezani Rad M., Rasmussen S.W.,
RA   Remacha M.A., Revuelta J.L., Richard G.-F., Rieger M.,
RA   Rodrigues-Pousada C., Rose M., Rupp T., Santos M.A., Schwager C.,
RA   Sensen C., Skala J., Soares H., Sor F., Stegemann J., Tettelin H.,
RA   Thierry A., Tzermia M., Urrestarazu L.A., van Dyck L.,
RA   van Vliet-Reedijk J.C., Valens M., Vandenbol M., Vilela C., Vissers S.,
RA   von Wettstein D., Voss H., Wiemann S., Xu G., Zimmermann J., Haasemann M.,
RA   Becker I., Mewes H.-W.;
RT   "Complete DNA sequence of yeast chromosome XI.";
RL   Nature 369:371-378(1994).
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] OF 1-280.
RA   Aebi M., Furter R., Prantl F., Niederberger P., Huetter R.;
RT   "Structure and function of the TRP3 gene of Saccharomyces cerevisiae:
RT   analysis of transcription, promoter sequence, and sequence coding for a
RT   glutamine amidotransferase.";
RL   Curr. Genet. 8:165-172(1984).
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-2, AND IDENTIFICATION BY MASS
RP   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).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=chorismate + L-glutamine = anthranilate + pyruvate + L-
CC         glutamate + H(+); Xref=Rhea:RHEA:21732, ChEBI:CHEBI:15361,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:16567, ChEBI:CHEBI:29748,
CC         ChEBI:CHEBI:29985, ChEBI:CHEBI:58359; EC=4.1.3.27;
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate + H(+)
CC         = (1S,2R)-1-C-(indol-3-yl)glycerol 3-phosphate + CO2 + H2O;
CC         Xref=Rhea:RHEA:23476, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:16526, ChEBI:CHEBI:58613, ChEBI:CHEBI:58866; EC=4.1.1.48;
CC   -!- PATHWAY: Amino-acid biosynthesis; L-tryptophan biosynthesis; L-
CC       tryptophan from chorismate: step 1/5.
CC   -!- PATHWAY: Amino-acid biosynthesis; L-tryptophan biosynthesis; L-
CC       tryptophan from chorismate: step 4/5.
CC   -!- SUBUNIT: Tetramer of two components I and two components II.
CC   -!- INTERACTION:
CC       P00937; P00899: TRP2; NbExp=4; IntAct=EBI-19585, EBI-19575;
CC   -!- INDUCTION: By tryptophan starvation.
CC   -!- MISCELLANEOUS: Component I catalyzes the formation of anthranilate
CC       using ammonia rather than glutamine, whereas component II provides
CC       glutamine amidotransferase activity.
CC   -!- MISCELLANEOUS: Yeast component II C-terminal half also has indole-3-
CC       glycerol phosphate synthase activity.
CC   -!- MISCELLANEOUS: Present with 13400 molecules/cell in log phase SD
CC       medium. {ECO:0000269|PubMed:14562106}.
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DR   EMBL; K01386; AAA35176.1; -; Genomic_DNA.
DR   EMBL; X75951; CAA53562.1; -; Genomic_DNA.
DR   EMBL; Z28211; CAA82056.1; -; Genomic_DNA.
DR   EMBL; M36300; AAA34450.1; -; Genomic_DNA.
DR   EMBL; BK006944; DAA08958.1; -; Genomic_DNA.
DR   PIR; S38049; NNBY2.
DR   RefSeq; NP_012711.1; NM_001179776.1.
DR   AlphaFoldDB; P00937; -.
DR   SMR; P00937; -.
DR   BioGRID; 33954; 113.
DR   ComplexPortal; CPX-1850; Anthranilate synthase complex.
DR   DIP; DIP-543N; -.
DR   FunCoup; P00937; 500.
DR   IntAct; P00937; 38.
DR   MINT; P00937; -.
DR   STRING; 4932.YKL211C; -.
DR   MEROPS; C26.959; -.
DR   iPTMnet; P00937; -.
DR   PaxDb; 4932-YKL211C; -.
DR   PeptideAtlas; P00937; -.
DR   EnsemblFungi; YKL211C_mRNA; YKL211C; YKL211C.
DR   GeneID; 853669; -.
DR   KEGG; sce:YKL211C; -.
DR   AGR; SGD:S000001694; -.
DR   SGD; S000001694; TRP3.
DR   VEuPathDB; FungiDB:YKL211C; -.
DR   eggNOG; KOG0026; Eukaryota.
DR   eggNOG; KOG4201; Eukaryota.
DR   HOGENOM; CLU_039523_0_0_1; -.
DR   InParanoid; P00937; -.
DR   OMA; EPIEWAN; -.
DR   OrthoDB; 524799at2759; -.
DR   BioCyc; YEAST:YKL211C-MONOMER; -.
DR   SABIO-RK; P00937; -.
DR   UniPathway; UPA00035; UER00040.
DR   UniPathway; UPA00035; UER00043.
DR   BioGRID-ORCS; 853669; 0 hits in 10 CRISPR screens.
DR   PRO; PR:P00937; -.
DR   Proteomes; UP000002311; Chromosome XI.
DR   RNAct; P00937; protein.
DR   GO; GO:0005950; C:anthranilate synthase complex; IPI:ComplexPortal.
DR   GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR   GO; GO:0004049; F:anthranilate synthase activity; IEA:UniProtKB-EC.
DR   GO; GO:0004425; F:indole-3-glycerol-phosphate synthase activity; IMP:SGD.
DR   GO; GO:0006541; P:L-glutamine metabolic process; IDA:ComplexPortal.
DR   GO; GO:0000162; P:L-tryptophan biosynthetic process; IDA:ComplexPortal.
DR   CDD; cd01743; GATase1_Anthranilate_Synthase; 1.
DR   CDD; cd00331; IGPS; 1.
DR   FunFam; 3.20.20.70:FF:000136; Multifunctional tryptophan biosynthesis protein; 1.
DR   FunFam; 3.40.50.880:FF:000031; Multifunctional tryptophan biosynthesis protein; 1.
DR   Gene3D; 3.40.50.880; -; 1.
DR   Gene3D; 3.20.20.70; Aldolase class I; 1.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR050472; Anth_synth/Amidotransfase.
DR   InterPro; IPR029062; Class_I_gatase-like.
DR   InterPro; IPR017926; GATASE.
DR   InterPro; IPR013798; Indole-3-glycerol_P_synth_dom.
DR   InterPro; IPR001468; Indole-3-GlycerolPSynthase_CS.
DR   InterPro; IPR011060; RibuloseP-bd_barrel.
DR   InterPro; IPR006221; TrpG/PapA_dom.
DR   NCBIfam; TIGR00566; trpG_papA; 1.
DR   PANTHER; PTHR43418:SF4; MULTIFUNCTIONAL TRYPTOPHAN BIOSYNTHESIS PROTEIN; 1.
DR   PANTHER; PTHR43418; MULTIFUNCTIONAL TRYPTOPHAN BIOSYNTHESIS PROTEIN-RELATED; 1.
DR   Pfam; PF00117; GATase; 1.
DR   Pfam; PF00218; IGPS; 1.
DR   PRINTS; PR00097; ANTSNTHASEII.
DR   PRINTS; PR00099; CPSGATASE.
DR   PRINTS; PR00096; GATASE.
DR   SUPFAM; SSF52317; Class I glutamine amidotransferase-like; 1.
DR   SUPFAM; SSF51366; Ribulose-phoshate binding barrel; 1.
DR   PROSITE; PS51273; GATASE_TYPE_1; 1.
DR   PROSITE; PS00614; IGPS; 1.
PE   1: Evidence at protein level;
KW   Amino-acid biosynthesis; Aromatic amino acid biosynthesis;
KW   Glutamine amidotransferase; Lyase; Multifunctional enzyme; Phosphoprotein;
KW   Reference proteome; Tryptophan biosynthesis.
FT   CHAIN           1..484
FT                   /note="Multifunctional tryptophan biosynthesis protein"
FT                   /id="PRO_0000056866"
FT   DOMAIN          13..207
FT                   /note="Glutamine amidotransferase type-1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00605"
FT   REGION          215..484
FT                   /note="Indole-3-glycerol phosphate synthase"
FT   ACT_SITE        92
FT                   /note="Nucleophile; for GATase activity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00605"
FT   ACT_SITE        181
FT                   /note="For GATase activity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00605"
FT   ACT_SITE        183
FT                   /note="For GATase activity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00605"
FT   BINDING         64..66
FT                   /ligand="L-glutamine"
FT                   /ligand_id="ChEBI:CHEBI:58359"
FT                   /evidence="ECO:0000250|UniProtKB:P00900"
FT   BINDING         96
FT                   /ligand="L-glutamine"
FT                   /ligand_id="ChEBI:CHEBI:58359"
FT                   /evidence="ECO:0000250|UniProtKB:P00900"
FT   BINDING         142..143
FT                   /ligand="L-glutamine"
FT                   /ligand_id="ChEBI:CHEBI:58359"
FT                   /evidence="ECO:0000250|UniProtKB:P00900"
FT   MOD_RES         2
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18407956"
FT   CONFLICT        32
FT                   /note="C -> S (in Ref. 5; AAA34450)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        63..65
FT                   /note="PGP -> LGL (in Ref. 5; AAA34450)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        129
FT                   /note="K -> R (in Ref. 1; AAA35176)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        170
FT                   /note="H -> Y (in Ref. 5; AAA34450)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        236
FT                   /note="G -> S (in Ref. 5; AAA34450)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   484 AA;  53489 MW;  34EF65E829279C1F CRC64;
     MSVHAATNPI NKHVVLIDNY DSFTWNVYEY LCQEGAKVSV YRNDAITVPE IAALNPDTLL
     ISPGPGHPKT DSGISRDCIR YFTGKIPVFG ICMGQQCMFD VFGGEVAYAG EIVHGKTSPI
     SHDNCGIFKN VPQGIAVTRY HSLAGTESSL PSCLKVTAST ENGIIMGVRH KKYTVEGVQF
     HPESILTEEG HLMIRNILNV SGGTWEENKS SPSNSILDRI YARRKIDVNE QSKIPGFTFQ
     DLQSNYDLGL APPLQDFYTV LSSSHKRAVV LAEVKRASPS KGPICLKAVA AEQALKYAEA
     GASAISVLTE PHWFHGSLQD LVNVRKILDL KFPPKERPCV LRKEFIFSKY QILEARLAGA
     DTVLLIVKML SQPLLKELYS YSKDLNMEPL VEVNSKEELQ RALEIGAKVV GVNNRDLHSF
     NVDLNTTSNL VESIPKDVLL IALSGITTRD DAEKYKKEGV HGFLVGEALM KSTDVKKFIH
     ELCE
//