ID AROC_YEAST Reviewed; 376 AA.
AC P28777; D6VU01;
DT 01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-1992, sequence version 1.
DT 27-MAR-2024, entry version 186.
DE RecName: Full=Chorismate synthase ARO2 {ECO:0000303|PubMed:1837329};
DE EC=1.5.1.38 {ECO:0000269|PubMed:8971708};
DE EC=4.2.3.5 {ECO:0000269|PubMed:8971708};
DE AltName: Full=5-enolpyruvylshikimate-3-phosphate phospholyase {ECO:0000303|PubMed:1837329};
DE AltName: Full=Aromatic amino acid requiring protein 2 {ECO:0000303|PubMed:361708};
GN Name=ARO2 {ECO:0000303|PubMed:361708}; OrderedLocusNames=YGL148W;
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], AND INDUCTION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=1837329; DOI=10.1111/j.1365-2958.1991.tb02144.x;
RA Jones D.G.L., Reusser U., Braus G.H.;
RT "Molecular cloning, characterization and analysis of the regulation of the
RT ARO2 gene, encoding chorismate synthase, of Saccharomyces cerevisiae.";
RL Mol. Microbiol. 5:2143-2152(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 96604 / S288c / FY1679;
RX PubMed=9046099;
RX DOI=10.1002/(sici)1097-0061(199702)13:2<177::aid-yea62>3.0.co;2-2;
RA Voet M., Defoor E., Verhasselt P., Riles L., Robben J., Volckaert G.;
RT "The sequence of a nearly unclonable 22.8 kb segment on the left arm
RT chromosome VII from Saccharomyces cerevisiae reveals ARO2, RPL9A, TIP1,
RT MRF1 genes and six new open reading frames.";
RL Yeast 13:177-182(1997).
RN [3]
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 [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 FUNCTION, DISRUPTION PHENOTYPE, AND PATHWAY.
RX PubMed=361708; DOI=10.1128/jb.136.1.55-62.1978;
RA Lucchini G., Biraghi A., Carbone M.L., de Scrilli A., Magni G.E.;
RT "Effect of mutation in the aromatic amino acid pathway on sporulation of
RT Saccharomyces cerevisiae.";
RL J. Bacteriol. 136:55-62(1978).
RN [6]
RP FUNCTION, CATALYTIC ACTIVITY, AND PATHWAY.
RX PubMed=8971708; DOI=10.1046/j.1365-2958.1996.01534.x;
RA Henstrand J.M., Schaller A., Braun M., Amrhein N., Schmid J.;
RT "Saccharomyces cerevisiae chorismate synthase has a flavin reductase
RT activity.";
RL Mol. Microbiol. 22:859-866(1996).
RN [7]
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 [8]
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 [9]
RP INDUCTION.
RX PubMed=22842922; DOI=10.1038/ncb2549;
RA Tkach J.M., Yimit A., Lee A.Y., Riffle M., Costanzo M., Jaschob D.,
RA Hendry J.A., Ou J., Moffat J., Boone C., Davis T.N., Nislow C., Brown G.W.;
RT "Dissecting DNA damage response pathways by analysing protein localization
RT and abundance changes during DNA replication stress.";
RL Nat. Cell Biol. 14:966-976(2012).
RN [10]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [11] {ECO:0007744|PDB:1R52, ECO:0007744|PDB:1R53}
RP X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS), AND SUBUNIT.
RX PubMed=14573601; DOI=10.1074/jbc.m310380200;
RA Quevillon-Cheruel S., Leulliot N., Meyer P., Graille M., Bremang M.,
RA Blondeau K., Sorel I., Poupon A., Janin J., van Tilbeurgh H.;
RT "Crystal structure of the bifunctional chorismate synthase from
RT Saccharomyces cerevisiae.";
RL J. Biol. Chem. 279:619-625(2004).
CC -!- FUNCTION: Bifunctional chorismate synthase and flavin reductase that
CC catalyzes the conversion of 5-enolpyruvylshikimate 3-phosphate (EPSP)
CC to form chorismate, which is the last common intermediate in the
CC synthesis of the three aromatic amino acids phenylalanine, tyrosine and
CC tryptophan (PubMed:8971708). Acts also as a flavin reductase (FR) able
CC to generate reduced flavin mononucleotide in the presence of NADPH
CC (PubMed:8971708). {ECO:0000269|PubMed:8971708}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=5-O-(1-carboxyvinyl)-3-phosphoshikimate = chorismate +
CC phosphate; Xref=Rhea:RHEA:21020, ChEBI:CHEBI:29748,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:57701; EC=4.2.3.5;
CC Evidence={ECO:0000269|PubMed:8971708};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:21021;
CC Evidence={ECO:0000269|PubMed:8971708};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=FMNH2 + NADP(+) = FMN + 2 H(+) + NADPH; Xref=Rhea:RHEA:21624,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57618, ChEBI:CHEBI:57783,
CC ChEBI:CHEBI:58210, ChEBI:CHEBI:58349; EC=1.5.1.38;
CC Evidence={ECO:0000269|PubMed:8971708};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:21626;
CC Evidence={ECO:0000269|PubMed:8971708};
CC -!- PATHWAY: Metabolic intermediate biosynthesis; chorismate biosynthesis;
CC chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step
CC 7/7. {ECO:0000269|PubMed:361708, ECO:0000269|PubMed:8971708}.
CC -!- SUBUNIT: Homotetramer. {ECO:0000269|PubMed:14573601}.
CC -!- INDUCTION: By amino acid starvation (PubMed:1837329). Expression is
CC increased in response to DNA replication stress (PubMed:22842922).
CC {ECO:0000269|PubMed:1837329, ECO:0000269|PubMed:22842922}.
CC -!- DISRUPTION PHENOTYPE: Impairs sporulation, probably by blocking the
CC biosynthesis of aromatic amino acids. {ECO:0000269|PubMed:361708}.
CC -!- MISCELLANEOUS: Present with 2310 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the chorismate synthase family. {ECO:0000305}.
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DR EMBL; X60190; CAA42745.1; -; Genomic_DNA.
DR EMBL; X99960; CAA68214.1; -; Genomic_DNA.
DR EMBL; Z72670; CAA96860.1; -; Genomic_DNA.
DR EMBL; BK006941; DAA07962.1; -; Genomic_DNA.
DR PIR; S17246; S17246.
DR RefSeq; NP_011367.1; NM_001181013.1.
DR PDB; 1R52; X-ray; 2.89 A; A/B/C/D=1-376.
DR PDB; 1R53; X-ray; 2.20 A; A=1-376.
DR PDBsum; 1R52; -.
DR PDBsum; 1R53; -.
DR AlphaFoldDB; P28777; -.
DR SMR; P28777; -.
DR BioGRID; 33104; 300.
DR DIP; DIP-4219N; -.
DR IntAct; P28777; 6.
DR MINT; P28777; -.
DR STRING; 4932.YGL148W; -.
DR iPTMnet; P28777; -.
DR MaxQB; P28777; -.
DR PaxDb; 4932-YGL148W; -.
DR PeptideAtlas; P28777; -.
DR EnsemblFungi; YGL148W_mRNA; YGL148W; YGL148W.
DR GeneID; 852729; -.
DR KEGG; sce:YGL148W; -.
DR AGR; SGD:S000003116; -.
DR SGD; S000003116; ARO2.
DR VEuPathDB; FungiDB:YGL148W; -.
DR eggNOG; KOG4492; Eukaryota.
DR HOGENOM; CLU_034547_0_1_1; -.
DR InParanoid; P28777; -.
DR OMA; NAVKGFE; -.
DR OrthoDB; 275401at2759; -.
DR BioCyc; YEAST:YGL148W-MONOMER; -.
DR BRENDA; 4.2.3.5; 984.
DR UniPathway; UPA00053; UER00090.
DR BioGRID-ORCS; 852729; 9 hits in 10 CRISPR screens.
DR EvolutionaryTrace; P28777; -.
DR PRO; PR:P28777; -.
DR Proteomes; UP000002311; Chromosome VII.
DR RNAct; P28777; Protein.
DR GO; GO:0005737; C:cytoplasm; IDA:SGD.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0004107; F:chorismate synthase activity; IDA:SGD.
DR GO; GO:0010181; F:FMN binding; IBA:GO_Central.
DR GO; GO:0008752; F:FMN reductase (NAD(P)H) activity; IEA:RHEA.
DR GO; GO:0052873; F:FMN reductase (NADPH) activity; IEA:RHEA.
DR GO; GO:0042602; F:riboflavin reductase (NADPH) activity; IDA:SGD.
DR GO; GO:0008652; P:amino acid biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0009073; P:aromatic amino acid family biosynthetic process; IMP:SGD.
DR GO; GO:0009423; P:chorismate biosynthetic process; IBA:GO_Central.
DR CDD; cd07304; Chorismate_synthase; 1.
DR Gene3D; 3.60.150.10; Chorismate synthase AroC; 2.
DR HAMAP; MF_00300; Chorismate_synth; 1.
DR InterPro; IPR000453; Chorismate_synth.
DR InterPro; IPR035904; Chorismate_synth_AroC_sf.
DR InterPro; IPR020541; Chorismate_synthase_CS.
DR NCBIfam; TIGR00033; aroC; 1.
DR PANTHER; PTHR21085; CHORISMATE SYNTHASE; 1.
DR PANTHER; PTHR21085:SF0; CHORISMATE SYNTHASE; 1.
DR Pfam; PF01264; Chorismate_synt; 1.
DR PIRSF; PIRSF001456; Chorismate_synth; 1.
DR SUPFAM; SSF103263; Chorismate synthase, AroC; 1.
DR PROSITE; PS00787; CHORISMATE_SYNTHASE_1; 1.
DR PROSITE; PS00788; CHORISMATE_SYNTHASE_2; 1.
DR PROSITE; PS00789; CHORISMATE_SYNTHASE_3; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Amino-acid biosynthesis;
KW Aromatic amino acid biosynthesis; Flavoprotein; FMN; Lyase; Oxidoreductase;
KW Reference proteome; Stress response.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:22814378"
FT CHAIN 2..376
FT /note="Chorismate synthase ARO2"
FT /id="PRO_0000140704"
FT REGION 39..61
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 17
FT /evidence="ECO:0000250|UniProtKB:Q12640"
FT ACT_SITE 104
FT /evidence="ECO:0000250|UniProtKB:Q12640"
FT ACT_SITE 339
FT /evidence="ECO:0000250|UniProtKB:Q12640"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0007744|PubMed:22814378"
FT STRAND 6..13
FT /evidence="ECO:0007829|PDB:1R53"
FT STRAND 18..26
FT /evidence="ECO:0007829|PDB:1R53"
FT STRAND 30..33
FT /evidence="ECO:0007829|PDB:1R52"
FT HELIX 36..38
FT /evidence="ECO:0007829|PDB:1R53"
FT HELIX 40..44
FT /evidence="ECO:0007829|PDB:1R53"
FT STRAND 63..65
FT /evidence="ECO:0007829|PDB:1R52"
FT STRAND 67..70
FT /evidence="ECO:0007829|PDB:1R53"
FT STRAND 79..84
FT /evidence="ECO:0007829|PDB:1R53"
FT HELIX 130..145
FT /evidence="ECO:0007829|PDB:1R53"
FT STRAND 150..158
FT /evidence="ECO:0007829|PDB:1R53"
FT HELIX 170..178
FT /evidence="ECO:0007829|PDB:1R53"
FT HELIX 181..186
FT /evidence="ECO:0007829|PDB:1R53"
FT HELIX 195..210
FT /evidence="ECO:0007829|PDB:1R53"
FT STRAND 217..225
FT /evidence="ECO:0007829|PDB:1R53"
FT TURN 233..235
FT /evidence="ECO:0007829|PDB:1R53"
FT HELIX 238..247
FT /evidence="ECO:0007829|PDB:1R53"
FT STRAND 254..257
FT /evidence="ECO:0007829|PDB:1R52"
FT TURN 258..261
FT /evidence="ECO:0007829|PDB:1R53"
FT HELIX 262..265
FT /evidence="ECO:0007829|PDB:1R53"
FT HELIX 268..272
FT /evidence="ECO:0007829|PDB:1R53"
FT STRAND 293..295
FT /evidence="ECO:0007829|PDB:1R53"
FT STRAND 304..310
FT /evidence="ECO:0007829|PDB:1R53"
FT HELIX 342..345
FT /evidence="ECO:0007829|PDB:1R53"
FT HELIX 347..370
FT /evidence="ECO:0007829|PDB:1R53"
SQ SEQUENCE 376 AA; 40838 MW; AF3AF65605B91E8E CRC64;
MSTFGKLFRV TTYGESHCKS VGCIVDGVPP GMSLTEADIQ PQLTRRRPGQ SKLSTPRDEK
DRVEIQSGTE FGKTLGTPIA MMIKNEDQRP HDYSDMDKFP RPSHADFTYS EKYGIKASSG
GGRASARETI GRVASGAIAE KFLAQNSNVE IVAFVTQIGE IKMNRDSFDP EFQHLLNTIT
REKVDSMGPI RCPDASVAGL MVKEIEKYRG NKDSIGGVVT CVVRNLPTGL GEPCFDKLEA
MLAHAMLSIP ASKGFEIGSG FQGVSVPGSK HNDPFYFEKE TNRLRTKTNN SGGVQGGISN
GENIYFSVPF KSVATISQEQ KTATYDGEEG ILAAKGRHDP AVTPRAIPIV EAMTALVLAD
ALLIQKARDF SRSVVH
//
