TRPE_YEAST
ID TRPE_YEAST Reviewed; 507 AA.
AC P00899; D3DLZ7;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 4.
DT 03-AUG-2022, entry version 196.
DE RecName: Full=Anthranilate synthase component 1;
DE EC=4.1.3.27;
DE AltName: Full=Anthranilate synthase component I;
GN Name=TRP2; OrderedLocusNames=YER090W;
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=S288C / X2180-1A;
RX PubMed=8432699; DOI=10.1128/jb.175.4.1061-1068.1993;
RA Graf R., Mehmann B., Braus G.H.;
RT "Analysis of feedback-resistant anthranilate synthases from Saccharomyces
RT cerevisiae.";
RL J. Bacteriol. 175:1061-1068(1993).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169868;
RA Dietrich F.S., Mulligan J.T., Hennessy K.M., Yelton M.A., Allen E.,
RA Araujo R., Aviles E., Berno A., Brennan T., Carpenter J., Chen E.,
RA Cherry J.M., Chung E., Duncan M., Guzman E., Hartzell G., Hunicke-Smith S.,
RA Hyman R.W., Kayser A., Komp C., Lashkari D., Lew H., Lin D., Mosedale D.,
RA Nakahara K., Namath A., Norgren R., Oefner P., Oh C., Petel F.X.,
RA Roberts D., Sehl P., Schramm S., Shogren T., Smith V., Taylor P., Wei Y.,
RA Botstein D., Davis R.W.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome V.";
RL Nature 387:78-81(1997).
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 PROTEIN SEQUENCE OF 2-16.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=7483834; DOI=10.1002/yea.320110702;
RA Boucherie H., Dujardin G., Kermorgant M., Monribot C., Slonimski P.P.,
RA Perrot M.;
RT "Two-dimensional protein map of Saccharomyces cerevisiae: construction of a
RT gene-protein index.";
RL Yeast 11:601-613(1995).
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-81 AND THR-223, 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).
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 -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:P00897};
CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000250|UniProtKB:P00897};
CC -!- PATHWAY: Amino-acid biosynthesis; L-tryptophan biosynthesis; L-
CC tryptophan from chorismate: step 1/5.
CC -!- SUBUNIT: Tetramer of two components I and two components II.
CC -!- INTERACTION:
CC P00899; P00937: TRP3; NbExp=3; IntAct=EBI-19575, EBI-19585;
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: Present with 6510 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the anthranilate synthase component I family.
CC {ECO:0000305}.
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DR EMBL; K01388; AAA35175.1; -; Genomic_DNA.
DR EMBL; X68327; CAA48402.1; -; Genomic_DNA.
DR EMBL; U18839; AAB64645.1; -; Genomic_DNA.
DR EMBL; BK006939; DAA07751.1; -; Genomic_DNA.
DR PIR; A49701; NNBY1.
DR RefSeq; NP_011014.1; NM_001178981.1.
DR AlphaFoldDB; P00899; -.
DR SMR; P00899; -.
DR BioGRID; 36835; 163.
DR ComplexPortal; CPX-1850; Anthranilate synthase complex.
DR DIP; DIP-542N; -.
DR IntAct; P00899; 15.
DR MINT; P00899; -.
DR STRING; 4932.YER090W; -.
DR iPTMnet; P00899; -.
DR MaxQB; P00899; -.
DR PaxDb; P00899; -.
DR PRIDE; P00899; -.
DR EnsemblFungi; YER090W_mRNA; YER090W; YER090W.
DR GeneID; 856824; -.
DR KEGG; sce:YER090W; -.
DR SGD; S000000892; TRP2.
DR VEuPathDB; FungiDB:YER090W; -.
DR eggNOG; KOG1223; Eukaryota.
DR HOGENOM; CLU_006493_9_3_1; -.
DR InParanoid; P00899; -.
DR OMA; GCVGYLD; -.
DR BioCyc; YEAST:MON3O-30; -.
DR SABIO-RK; P00899; -.
DR UniPathway; UPA00035; UER00040.
DR PRO; PR:P00899; -.
DR Proteomes; UP000002311; Chromosome V.
DR RNAct; P00899; 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; IDA:SGD.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006541; P:glutamine metabolic process; IDA:ComplexPortal.
DR GO; GO:0000162; P:tryptophan biosynthetic process; IDA:ComplexPortal.
DR Gene3D; 3.60.120.10; -; 1.
DR InterPro; IPR005801; ADC_synthase.
DR InterPro; IPR019999; Anth_synth_I-like.
DR InterPro; IPR006805; Anth_synth_I_N.
DR InterPro; IPR005256; Anth_synth_I_PabB.
DR InterPro; IPR015890; Chorismate_C.
DR PANTHER; PTHR11236; PTHR11236; 1.
DR Pfam; PF04715; Anth_synt_I_N; 1.
DR Pfam; PF00425; Chorismate_bind; 1.
DR PRINTS; PR00095; ANTSNTHASEI.
DR SUPFAM; SSF56322; SSF56322; 1.
DR TIGRFAMs; TIGR00564; trpE_most; 1.
PE 1: Evidence at protein level;
KW Amino-acid biosynthesis; Aromatic amino acid biosynthesis;
KW Direct protein sequencing; Lyase; Magnesium; Metal-binding; Phosphoprotein;
KW Reference proteome; Tryptophan biosynthesis.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:7483834"
FT CHAIN 2..507
FT /note="Anthranilate synthase component 1"
FT /id="PRO_0000154134"
FT BINDING 65
FT /ligand="L-tryptophan"
FT /ligand_id="ChEBI:CHEBI:57912"
FT /evidence="ECO:0000250|UniProtKB:P00897"
FT BINDING 280..282
FT /ligand="L-tryptophan"
FT /ligand_id="ChEBI:CHEBI:57912"
FT /evidence="ECO:0000250|UniProtKB:P00897"
FT BINDING 316..317
FT /ligand="chorismate"
FT /ligand_id="ChEBI:CHEBI:29748"
FT /evidence="ECO:0000250|UniProtKB:P00897"
FT BINDING 343
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P00897"
FT BINDING 431
FT /ligand="chorismate"
FT /ligand_id="ChEBI:CHEBI:29748"
FT /evidence="ECO:0000250|UniProtKB:P00897"
FT BINDING 452
FT /ligand="chorismate"
FT /ligand_id="ChEBI:CHEBI:29748"
FT /evidence="ECO:0000250|UniProtKB:P00897"
FT BINDING 466..468
FT /ligand="chorismate"
FT /ligand_id="ChEBI:CHEBI:29748"
FT /evidence="ECO:0000250|UniProtKB:P00897"
FT BINDING 468
FT /ligand="chorismate"
FT /ligand_id="ChEBI:CHEBI:29748"
FT /evidence="ECO:0000250|UniProtKB:P00897"
FT BINDING 481
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P00897"
FT MOD_RES 81
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT MOD_RES 223
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT CONFLICT 204..212
FT /note="TDDSSPIPY -> DRRFLANTI (in Ref. 1; AAA35175)"
FT /evidence="ECO:0000305"
FT CONFLICT 220
FT /note="L -> P (in Ref. 1)"
FT /evidence="ECO:0000305"
FT CONFLICT 223..238
FT /note="TFESNVGKEGYENHVS -> LLNRMWARKVTKITSP (in Ref. 1)"
FT /evidence="ECO:0000305"
FT CONFLICT 262..268
FT /note="TSLHPFN -> SRYILSIFTD (in Ref. 1; AAA35175)"
FT /evidence="ECO:0000305"
FT CONFLICT 276
FT /note="V -> I (in Ref. 1; AAA35175)"
FT /evidence="ECO:0000305"
FT CONFLICT 323
FT /note="T -> A (in Ref. 1; AAA35175)"
FT /evidence="ECO:0000305"
FT CONFLICT 330
FT /note="L -> G (in Ref. 1; AAA35175)"
FT /evidence="ECO:0000305"
FT CONFLICT 401..402
FT /note="SI -> TN (in Ref. 1; AAA35175)"
FT /evidence="ECO:0000305"
FT CONFLICT 461..507
FT /note="AYLQAGGGIVYDSDEYDEYVETMNKMMANHSTIVQAEELWADIVGSA -> L
FT TCKLAVVLFTIQLSTMNMLETMNNDGQSQYYCASRRIVGRYRRISLKRAFSVFFPLDDI
FT FIVFE (in Ref. 1)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 507 AA; 56768 MW; FCC179C481DB3107 CRC64;
MTASIKIQPD IDSLKQLQQQ NDDSSINMYP VYAYLPSLDL TPHVAYLKLA QLNNPDRKES
FLLESAKTNN ELDRYSFIGI SPRKTIKTGP TEGIETDPLE ILEKEMSTFK VAENVPGLPK
LSGGAIGYIS YDCVRYFEPK TRRPLKDVLR LPEAYLMLCD TIIAFDNVFQ RFQIIHNINT
NETSLEEGYQ AAAQIITDIV SKLTDDSSPI PYPEQPPIKL NQTFESNVGK EGYENHVSTL
KKHIKKGDII QGVPSQRVAR PTSLHPFNIY RHLRTVNPSP YLFYIDCLDF QIIGASPELL
CKSDSKNRVI THPIAGTVKR GATTEEDDAL ADQLRGSLKD RAEHVMLVDL ARNDINRICD
PLTTSVDKLL TIQKFSHVQH LVSQVSGVLR PEKTRFDAFR SIFPAGTVSG APKVRAMELI
AELEGERRGV YAGAVGHWSY DGKTMDNCIA LRTMVYKDGI AYLQAGGGIV YDSDEYDEYV
ETMNKMMANH STIVQAEELW ADIVGSA
