AROG_YEAST
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 03-AUG-2022, entry version 190.
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 (1.9 ANGSTROMS) OF 23-369.
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 + H2O + phosphoenolpyruvate = 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 -!- 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. {ECO:0000305}.
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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 PDBsum; 1HFB; -.
DR PDBsum; 1OAB; -.
DR PDBsum; 1OF6; -.
DR PDBsum; 1OF8; -.
DR PDBsum; 1OFA; -.
DR PDBsum; 1OFB; -.
DR PDBsum; 1OFO; -.
DR PDBsum; 1OFP; -.
DR PDBsum; 1OFQ; -.
DR PDBsum; 1OFR; -.
DR PDBsum; 1OG0; -.
DR AlphaFoldDB; P32449; -.
DR SMR; P32449; -.
DR BioGRID; 32944; 52.
DR DIP; DIP-4175N; -.
DR IntAct; P32449; 9.
DR MINT; P32449; -.
DR STRING; 4932.YBR249C; -.
DR iPTMnet; P32449; -.
DR MaxQB; P32449; -.
DR PaxDb; P32449; -.
DR PRIDE; P32449; -.
DR EnsemblFungi; YBR249C_mRNA; YBR249C; YBR249C.
DR GeneID; 852551; -.
DR KEGG; sce:YBR249C; -.
DR SGD; S000000453; ARO4.
DR VEuPathDB; FungiDB:YBR249C; -.
DR eggNOG; ENOG502QPSU; Eukaryota.
DR GeneTree; ENSGT00940000176767; -.
DR HOGENOM; CLU_030903_0_1_1; -.
DR InParanoid; P32449; -.
DR OMA; VMENVAN; -.
DR BioCyc; YEAST:YBR249C-MON; -.
DR BRENDA; 2.5.1.54; 984.
DR UniPathway; UPA00053; UER00084.
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 family biosynthetic process; IBA:GO_Central.
DR GO; GO:0008652; P:cellular amino acid biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0009423; P:chorismate biosynthetic process; TAS:SGD.
DR Gene3D; 3.20.20.70; -; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR006218; DAHP1/KDSA.
DR InterPro; IPR006219; DHAP_synth_1.
DR PANTHER; PTHR21225; PTHR21225; 1.
DR Pfam; PF00793; DAHP_synth_1; 1.
DR PIRSF; PIRSF001361; DAHP_synthase; 1.
DR TIGRFAMs; TIGR00034; aroFGH; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Amino-acid biosynthesis;
KW Aromatic amino acid biosynthesis; Reference proteome; Stress response;
KW 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 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
