TRPG_YEAST
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 03-AUG-2022, entry version 205.
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 + H(+) + L-glutamate +
CC pyruvate; Xref=Rhea:RHEA:21732, ChEBI:CHEBI:15361, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:16567, ChEBI:CHEBI:29748, ChEBI:CHEBI:29985,
CC 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=3; 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; 101.
DR ComplexPortal; CPX-1850; Anthranilate synthase complex.
DR DIP; DIP-543N; -.
DR IntAct; P00937; 36.
DR MINT; P00937; -.
DR STRING; 4932.YKL211C; -.
DR MEROPS; C26.959; -.
DR iPTMnet; P00937; -.
DR MaxQB; P00937; -.
DR PaxDb; P00937; -.
DR PRIDE; P00937; -.
DR EnsemblFungi; YKL211C_mRNA; YKL211C; YKL211C.
DR GeneID; 853669; -.
DR KEGG; sce:YKL211C; -.
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; CLEVSSW; -.
DR BioCyc; YEAST:YKL211C-MON; -.
DR SABIO-RK; P00937; -.
DR UniPathway; UPA00035; UER00040.
DR UniPathway; UPA00035; UER00043.
DR PRO; PR:P00937; -.
DR Proteomes; UP000002311; Chromosome XI.
DR RNAct; P00937; protein.
DR GO; GO:0005950; C:anthranilate synthase complex; IPI:SGD.
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:glutamine metabolic process; IDA:ComplexPortal.
DR GO; GO:0000162; P:tryptophan biosynthetic process; IDA:ComplexPortal.
DR CDD; cd01743; GATase1_Anthranilate_Synthase; 1.
DR CDD; cd00331; IGPS; 1.
DR Gene3D; 3.20.20.70; -; 1.
DR Gene3D; 3.40.50.880; -; 1.
DR InterPro; IPR013785; Aldolase_TIM.
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 Pfam; PF00117; GATase; 1.
DR Pfam; PF00218; IGPS; 1.
DR SUPFAM; SSF51366; SSF51366; 1.
DR SUPFAM; SSF52317; SSF52317; 1.
DR TIGRFAMs; TIGR00566; trpG_papA; 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
