ID   AROG_YEAST              Reviewed;         370 AA.
AC   P32449; D6VQP5;
DT   01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1994, sequence version 2.
DT   04-NOV-2026, entry version 207.
DE   RecName: Full=Phospho-2-dehydro-3-deoxyheptonate aldolase, tyrosine-inhibited;
DE            EC=2.5.1.54;
DE   AltName: Full=3-deoxy-D-arabino-heptulosonate 7-phosphate synthase;
DE   AltName: Full=DAHP synthase;
DE   AltName: Full=Phospho-2-keto-3-deoxyheptonate aldolase;
GN   Name=ARO4; OrderedLocusNames=YBR249C; ORFNames=YBR1701;
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=1348717; DOI=10.1016/0378-1119(92)90670-k;
RA   Kuenzler M., Paravicini G., Egli C., Irniger S., Braus G.H.;
RT   "Cloning, primary structure and regulation of the ARO4 gene, encoding the
RT   tyrosine-inhibited 3-deoxy-D-arabino-heptulosonate-7-phosphate synthase
RT   from Saccharomyces cerevisiae.";
RL   Gene 113:67-74(1992).
RN   [2]
RP   SEQUENCE REVISION TO 205-207.
RA   Kuenzler M.;
RL   Submitted (NOV-1993) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=8256522; DOI=10.1002/yea.320091014;
RA   Doignon F., Biteau N., Aigle M., Crouzet M.;
RT   "The complete sequence of a 6794 bp segment located on the right arm of
RT   chromosome II of Saccharomyces cerevisiae. Finding of a putative dUTPase in
RT   a yeast.";
RL   Yeast 9:1131-1137(1993).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=7813418; DOI=10.1002/j.1460-2075.1994.tb06923.x;
RA   Feldmann H., Aigle M., Aljinovic G., Andre B., Baclet M.C., Barthe C.,
RA   Baur A., Becam A.-M., Biteau N., Boles E., Brandt T., Brendel M.,
RA   Brueckner M., Bussereau F., Christiansen C., Contreras R., Crouzet M.,
RA   Cziepluch C., Demolis N., Delaveau T., Doignon F., Domdey H.,
RA   Duesterhus S., Dubois E., Dujon B., El Bakkoury M., Entian K.-D.,
RA   Feuermann M., Fiers W., Fobo G.M., Fritz C., Gassenhuber J., Glansdorff N.,
RA   Goffeau A., Grivell L.A., de Haan M., Hein C., Herbert C.J.,
RA   Hollenberg C.P., Holmstroem K., Jacq C., Jacquet M., Jauniaux J.-C.,
RA   Jonniaux J.-L., Kallesoee T., Kiesau P., Kirchrath L., Koetter P.,
RA   Korol S., Liebl S., Logghe M., Lohan A.J.E., Louis E.J., Li Z.Y.,
RA   Maat M.J., Mallet L., Mannhaupt G., Messenguy F., Miosga T., Molemans F.,
RA   Mueller S., Nasr F., Obermaier B., Perea J., Pierard A., Piravandi E.,
RA   Pohl F.M., Pohl T.M., Potier S., Proft M., Purnelle B., Ramezani Rad M.,
RA   Rieger M., Rose M., Schaaff-Gerstenschlaeger I., Scherens B.,
RA   Schwarzlose C., Skala J., Slonimski P.P., Smits P.H.M., Souciet J.-L.,
RA   Steensma H.Y., Stucka R., Urrestarazu L.A., van der Aart Q.J.M.,
RA   Van Dyck L., Vassarotti A., Vetter I., Vierendeels F., Vissers S.,
RA   Wagner G., de Wergifosse P., Wolfe K.H., Zagulski M., Zimmermann F.K.,
RA   Mewes H.-W., Kleine K.;
RT   "Complete DNA sequence of yeast chromosome II.";
RL   EMBO J. 13:5795-5809(1994).
RN   [5]
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   [6]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 352-370.
RX   PubMed=8366040; DOI=10.1128/jb.175.17.5548-5558.1993;
RA   Kuenzler M., Balmelli T., Egli C.M., Paravicini G., Braus G.H.;
RT   "Cloning, primary structure, and regulation of the HIS7 gene encoding a
RT   bifunctional glutamine amidotransferase: cyclase from Saccharomyces
RT   cerevisiae.";
RL   J. Bacteriol. 175:5548-5558(1993).
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   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   [10]
RP   X-RAY CRYSTALLOGRAPHY.
RX   PubMed=12540830; DOI=10.1073/pnas.0337566100;
RA   Hartmann M., Schneider T.R., Pfeil A., Heinrich G., Lipscomb W.N.,
RA   Braus G.H.;
RT   "Evolution of feedback-inhibited beta/alpha barrel isoenzymes by gene
RT   duplication and a single mutation.";
RL   Proc. Natl. Acad. Sci. U.S.A. 100:862-867(2003).
CC   -!- FUNCTION: Stereospecific condensation of phosphoenolpyruvate (PEP) and
CC       D-erythrose-4-phosphate (E4P) giving rise to 3-deoxy-D-arabino-
CC       heptulosonate-7-phosphate (DAHP).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=D-erythrose 4-phosphate + phosphoenolpyruvate + H2O = 7-
CC         phospho-2-dehydro-3-deoxy-D-arabino-heptonate + phosphate;
CC         Xref=Rhea:RHEA:14717, ChEBI:CHEBI:15377, ChEBI:CHEBI:16897,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:58394, ChEBI:CHEBI:58702; EC=2.5.1.54;
CC   -!- ACTIVITY REGULATION: Inhibited by tyrosine.
CC   -!- PATHWAY: Metabolic intermediate biosynthesis; chorismate biosynthesis;
CC       chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step
CC       1/7.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|PROSITE-ProRule:PRU01406}.
CC   -!- INDUCTION: By amino acid starvation.
CC   -!- MISCELLANEOUS: Present with 26300 molecules/cell in log phase SD
CC       medium. {ECO:0000269|PubMed:14562106}.
CC   -!- SIMILARITY: Belongs to the class-I DAHP synthase family.
CC       {ECO:0000255|PROSITE-ProRule:PRU01406}.
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DR   EMBL; X61107; CAA43419.1; -; Genomic_DNA.
DR   EMBL; L20296; AAA65607.1; -; Genomic_DNA.
DR   EMBL; Z36118; CAA85212.1; -; Genomic_DNA.
DR   EMBL; BK006936; DAA07365.1; -; Genomic_DNA.
DR   PIR; S38185; S38185.
DR   RefSeq; NP_009808.1; NM_001178597.1.
DR   PDB; 1HFB; X-ray; 1.90 A; A/B/C/D/E/F/G/H=1-370.
DR   PDB; 1OAB; X-ray; 1.90 A; A/B=1-370.
DR   PDB; 1OF6; X-ray; 2.10 A; A/B/C/D/E/F/G/H=1-370.
DR   PDB; 1OF8; X-ray; 1.50 A; A/B=1-370.
DR   PDB; 1OFA; X-ray; 2.01 A; A/B=1-370.
DR   PDB; 1OFB; X-ray; 2.00 A; A/B=1-370.
DR   PDB; 1OFO; X-ray; 1.85 A; A/B=1-370.
DR   PDB; 1OFP; X-ray; 2.10 A; A/B/C/D=1-370.
DR   PDB; 1OFQ; X-ray; 2.70 A; A/B/C/D=1-370.
DR   PDB; 1OFR; X-ray; 2.70 A; A/B/C/D/E/F/G/H=1-370.
DR   PDB; 1OG0; X-ray; 2.70 A; A/B/C/D/E/F/G/H=1-370.
DR   AlphaFoldDB; P32449; -.
DR   SMR; P32449; -.
DR   BioGRID; 32944; 75.
DR   DIP; DIP-4175N; -.
DR   FunCoup; P32449; 302.
DR   IntAct; P32449; 15.
DR   STRING; 4932.YBR249C; -.
DR   iPTMnet; P32449; -.
DR   PaxDb; 4932-YBR249C; -.
DR   PeptideAtlas; P32449; -.
DR   EnsemblFungi; YBR249C_mRNA; YBR249C; YBR249C.
DR   GeneID; 852551; -.
DR   KEGG; sce:YBR249C; -.
DR   AGR; SGD:S000000453; -.
DR   SGD; S000000453; ARO4.
DR   VEuPathDB; FungiDB:YBR249C; -.
DR   eggNOG; ENOG502QPSU; Eukaryota.
DR   HOGENOM; CLU_030903_0_1_1; -.
DR   InParanoid; P32449; -.
DR   OMA; AAHPHTF; -.
DR   OrthoDB; 4699125at2759; -.
DR   BioCyc; YEAST:YBR249C-MONOMER; -.
DR   BRENDA; 2.5.1.54; 984.
DR   UniPathway; UPA00053; UER00084.
DR   BioGRID-ORCS; 852551; 2 hits in 10 CRISPR screens.
DR   EvolutionaryTrace; P32449; -.
DR   PRO; PR:P32449; -.
DR   Proteomes; UP000002311; Chromosome II.
DR   RNAct; P32449; protein.
DR   GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR   GO; GO:0005634; C:nucleus; HDA:SGD.
DR   GO; GO:0003849; F:3-deoxy-7-phosphoheptulonate synthase activity; IDA:SGD.
DR   GO; GO:0009073; P:aromatic amino acid biosynthetic process; IBA:GO_Central.
DR   GO; GO:0009423; P:chorismate biosynthetic process; TAS:SGD.
DR   GO; GO:0043085; P:positive regulation of catalytic activity; IMP:DisProt.
DR   DisProt; DP03815; -.
DR   FunFam; 3.20.20.70:FF:000005; Phospho-2-dehydro-3-deoxyheptonate aldolase; 1.
DR   Gene3D; 3.20.20.70; Aldolase class I; 1.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR006218; DAHP1/KDSA.
DR   InterPro; IPR006219; DAHP_synth_1.
DR   NCBIfam; TIGR00034; aroFGH; 1.
DR   NCBIfam; NF009395; PRK12755.1; 1.
DR   PANTHER; PTHR21225; PHOSPHO-2-DEHYDRO-3-DEOXYHEPTONATE ALDOLASE DAHP SYNTHETASE; 1.
DR   PANTHER; PTHR21225:SF12; PHOSPHO-2-DEHYDRO-3-DEOXYHEPTONATE ALDOLASE, TYROSINE-INHIBITED; 1.
DR   Pfam; PF00793; DAHP_synth_1; 1.
DR   PIRSF; PIRSF001361; DAHP_synthase; 1.
DR   SUPFAM; SSF51569; Aldolase; 1.
DR   PROSITE; PS52061; DAHPS_I; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Acetylation; Amino-acid biosynthesis;
KW   Aromatic amino acid biosynthesis; Cytoplasm; Reference proteome;
KW   Stress response; Transferase.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0007744|PubMed:22814378"
FT   CHAIN           2..370
FT                   /note="Phospho-2-dehydro-3-deoxyheptonate aldolase,
FT                   tyrosine-inhibited"
FT                   /id="PRO_0000140851"
FT   DOMAIN          66..368
FT                   /note="DAHPS class-I TIM-barrel"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01406"
FT   BINDING         107
FT                   /ligand="phosphoenolpyruvate"
FT                   /ligand_id="ChEBI:CHEBI:58702"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01406"
FT   BINDING         112
FT                   /ligand="phosphoenolpyruvate"
FT                   /ligand_id="ChEBI:CHEBI:58702"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01406"
FT   BINDING         179
FT                   /ligand="phosphoenolpyruvate"
FT                   /ligand_id="ChEBI:CHEBI:58702"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01406"
FT   BINDING         180
FT                   /ligand="phosphoenolpyruvate"
FT                   /ligand_id="ChEBI:CHEBI:58702"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01406"
FT   BINDING         201
FT                   /ligand="phosphoenolpyruvate"
FT                   /ligand_id="ChEBI:CHEBI:58702"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01406"
FT   BINDING         249
FT                   /ligand="phosphoenolpyruvate"
FT                   /ligand_id="ChEBI:CHEBI:58702"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01406"
FT   BINDING         282
FT                   /ligand="phosphoenolpyruvate"
FT                   /ligand_id="ChEBI:CHEBI:58702"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01406"
FT   MOD_RES         2
FT                   /note="N-acetylserine"
FT                   /evidence="ECO:0007744|PubMed:22814378"
FT   STRAND          25..29
FT                   /evidence="ECO:0007829|PDB:1OF8"
FT   HELIX           34..40
FT                   /evidence="ECO:0007829|PDB:1OF8"
FT   HELIX           45..62
FT                   /evidence="ECO:0007829|PDB:1OF8"
FT   STRAND          68..74
FT                   /evidence="ECO:0007829|PDB:1OF8"
FT   HELIX           81..98
FT                   /evidence="ECO:0007829|PDB:1OF8"
FT   TURN            99..101
FT                   /evidence="ECO:0007829|PDB:1OF8"
FT   STRAND          102..107
FT                   /evidence="ECO:0007829|PDB:1OF8"
FT   STRAND          115..118
FT                   /evidence="ECO:0007829|PDB:1OF8"
FT   TURN            122..124
FT                   /evidence="ECO:0007829|PDB:1OF8"
FT   STRAND          128..130
FT                   /evidence="ECO:0007829|PDB:1OF8"
FT   HELIX           134..149
FT                   /evidence="ECO:0007829|PDB:1OF8"
FT   TURN            150..152
FT                   /evidence="ECO:0007829|PDB:1OF8"
FT   STRAND          155..158
FT                   /evidence="ECO:0007829|PDB:1OF8"
FT   STRAND          161..163
FT                   /evidence="ECO:0007829|PDB:1OF8"
FT   HELIX           165..168
FT                   /evidence="ECO:0007829|PDB:1OF8"
FT   HELIX           169..171
FT                   /evidence="ECO:0007829|PDB:1OF8"
FT   STRAND          173..177
FT                   /evidence="ECO:0007829|PDB:1OF8"
FT   TURN            179..183
FT                   /evidence="ECO:0007829|PDB:1OF8"
FT   HELIX           185..192
FT                   /evidence="ECO:0007829|PDB:1OF8"
FT   STRAND          198..201
FT                   /evidence="ECO:0007829|PDB:1OF8"
FT   HELIX           209..218
FT                   /evidence="ECO:0007829|PDB:1OF8"
FT   STRAND          223..227
FT                   /evidence="ECO:0007829|PDB:1OF8"
FT   STRAND          231..238
FT                   /evidence="ECO:0007829|PDB:1OF8"
FT   STRAND          244..248
FT                   /evidence="ECO:0007829|PDB:1OF8"
FT   HELIX           259..268
FT                   /evidence="ECO:0007829|PDB:1OF8"
FT   STRAND          276..281
FT                   /evidence="ECO:0007829|PDB:1OF8"
FT   HELIX           282..285
FT                   /evidence="ECO:0007829|PDB:1OF8"
FT   HELIX           289..291
FT                   /evidence="ECO:0007829|PDB:1OF8"
FT   HELIX           292..304
FT                   /evidence="ECO:0007829|PDB:1OF8"
FT   STRAND          309..317
FT                   /evidence="ECO:0007829|PDB:1OF8"
FT   STRAND          319..323
FT                   /evidence="ECO:0007829|PDB:1OF8"
FT   HELIX           330..333
FT                   /evidence="ECO:0007829|PDB:1OF6"
FT   STRAND          339..342
FT                   /evidence="ECO:0007829|PDB:1OF8"
FT   HELIX           347..367
FT                   /evidence="ECO:0007829|PDB:1OF8"
SQ   SEQUENCE   370 AA;  39749 MW;  594ED48F24175979 CRC64;
     MSESPMFAAN GMPKVNQGAE EDVRILGYDP LASPALLQVQ IPATPTSLET AKRGRREAID
     IITGKDDRVL VIVGPCSIHD LEAAQEYALR LKKLSDELKG DLSIIMRAYL EKPRTTVGWK
     GLINDPDVNN TFNINKGLQS ARQLFVNLTN IGLPIGSEML DTISPQYLAD LVSFGAIGAR
     TTESQLHREL ASGLSFPVGF KNGTDGTLNV AVDACQAAAH SHHFMGVTKH GVAAITTTKG
     NEHCFVILRG GKKGTNYDAK SVAEAKAQLP AGSNGLMIDY SHGNSNKDFR NQPKVNDVVC
     EQIANGENAI TGVMIESNIN EGNQGIPAEG KAGLKYGVSI TDACIGWETT EDVLRKLAAA
     VRQRREVNKK
//