AROC_YEAST
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 03-AUG-2022, entry version 180.
DE RecName: Full=Chorismate synthase;
DE EC=4.2.3.5;
DE AltName: Full=5-enolpyruvylshikimate-3-phosphate phospholyase;
GN Name=ARO2; 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].
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 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 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 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).
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 -!- COFACTOR:
CC Name=FMNH2; Xref=ChEBI:CHEBI:57618;
CC -!- PATHWAY: Metabolic intermediate biosynthesis; chorismate biosynthesis;
CC chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step
CC 7/7.
CC -!- SUBUNIT: Homotetramer. {ECO:0000250}.
CC -!- INDUCTION: By amino acid starvation.
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; 290.
DR DIP; DIP-4219N; -.
DR IntAct; P28777; 6.
DR MINT; P28777; -.
DR STRING; 4932.YGL148W; -.
DR iPTMnet; P28777; -.
DR MaxQB; P28777; -.
DR PaxDb; P28777; -.
DR PRIDE; P28777; -.
DR EnsemblFungi; YGL148W_mRNA; YGL148W; YGL148W.
DR GeneID; 852729; -.
DR KEGG; sce:YGL148W; -.
DR SGD; S000003116; ARO2.
DR VEuPathDB; FungiDB:YGL148W; -.
DR eggNOG; KOG4492; Eukaryota.
DR HOGENOM; CLU_034547_0_1_1; -.
DR InParanoid; P28777; -.
DR OMA; MLSINAV; -.
DR BioCyc; YEAST:YGL148W-MON; -.
DR BRENDA; 4.2.3.5; 984.
DR UniPathway; UPA00053; UER00090.
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:0042602; F:riboflavin reductase (NADPH) activity; IDA:SGD.
DR GO; GO:0009073; P:aromatic amino acid family biosynthetic process; IMP:SGD.
DR GO; GO:0008652; P:cellular amino acid biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0009423; P:chorismate biosynthetic process; IBA:GO_Central.
DR CDD; cd07304; Chorismate_synthase; 1.
DR Gene3D; 3.60.150.10; -; 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 PANTHER; PTHR21085; PTHR21085; 1.
DR Pfam; PF01264; Chorismate_synt; 1.
DR PIRSF; PIRSF001456; Chorismate_synth; 1.
DR SUPFAM; SSF103263; SSF103263; 1.
DR TIGRFAMs; TIGR00033; 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; Lyase; Reference proteome;
KW Stress response.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:22814378"
FT CHAIN 2..376
FT /note="Chorismate synthase"
FT /id="PRO_0000140704"
FT REGION 39..61
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
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
