ID   AROG_ARATH              Reviewed;         507 AA.
AC   Q00218; Q9SZC8;
DT   01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT   27-MAY-2002, sequence version 2.
DT   25-MAY-2022, entry version 158.
DE   RecName: Full=Phospho-2-dehydro-3-deoxyheptonate aldolase 2, chloroplastic;
DE            EC=2.5.1.54;
DE   AltName: Full=3-deoxy-D-arabino-heptulosonate 7-phosphate synthase 2;
DE   AltName: Full=DAHP synthase 2;
DE   AltName: Full=Phospho-2-keto-3-deoxyheptonate aldolase 2;
DE   Flags: Precursor;
GN   Name=DHS2; OrderedLocusNames=At4g33510; ORFNames=F17M5.270;
OS   Arabidopsis thaliana (Mouse-ear cress).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX   NCBI_TaxID=3702;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=1681544; DOI=10.1073/pnas.88.19.8821;
RA   Keith B., Dong X.N., Ausubel F.M., Fink G.R.;
RT   "Differential induction of 3-deoxy-D-arabino-heptulosonate 7-phosphate
RT   synthase genes in Arabidopsis thaliana by wounding and pathogenic attack.";
RL   Proc. Natl. Acad. Sci. U.S.A. 88:8821-8825(1991).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=10617198; DOI=10.1038/47134;
RA   Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA   Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA   Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA   de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA   Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA   Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA   Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA   Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA   Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA   Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA   Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA   Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA   Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA   Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA   Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA   Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA   Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA   Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA   Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA   Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA   Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA   Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA   Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA   Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA   Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA   Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA   Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA   de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA   Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA   Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA   Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA   Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA   Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA   Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA   Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA   Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA   Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA   O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA   Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA   Martienssen R., McCombie W.R.;
RT   "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL   Nature 402:769-777(1999).
RN   [3]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Columbia;
RX   PubMed=27862469; DOI=10.1111/tpj.13415;
RA   Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA   Town C.D.;
RT   "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT   genome.";
RL   Plant J. 89:789-804(2017).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=14593172; DOI=10.1126/science.1088305;
RA   Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA   Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA   Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA   Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA   Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA   Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA   Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA   Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA   Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA   Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA   Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA   Ecker J.R.;
RT   "Empirical analysis of transcriptional activity in the Arabidopsis
RT   genome.";
RL   Science 302:842-846(2003).
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   -!- PATHWAY: Metabolic intermediate biosynthesis; chorismate biosynthesis;
CC       chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step
CC       1/7.
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=1;
CC         Comment=A number of isoforms are produced. According to EST
CC         sequences.;
CC       Name=1;
CC         IsoId=Q00218-1; Sequence=Displayed;
CC   -!- SIMILARITY: Belongs to the class-II DAHP synthase family.
CC       {ECO:0000305}.
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DR   EMBL; M74820; AAA32785.1; -; mRNA.
DR   EMBL; AL035678; CAB38809.1; -; Genomic_DNA.
DR   EMBL; AL161583; CAB80068.1; -; Genomic_DNA.
DR   EMBL; CP002687; AEE86237.1; -; Genomic_DNA.
DR   EMBL; AF361798; AAK32811.1; -; mRNA.
DR   EMBL; AY124858; AAM70567.1; -; mRNA.
DR   PIR; T06002; T06002.
DR   RefSeq; NP_195077.1; NM_119505.3. [Q00218-1]
DR   AlphaFoldDB; Q00218; -.
DR   SMR; Q00218; -.
DR   BioGRID; 14773; 4.
DR   IntAct; Q00218; 3.
DR   STRING; 3702.AT4G33510.1; -.
DR   iPTMnet; Q00218; -.
DR   PaxDb; Q00218; -.
DR   PRIDE; Q00218; -.
DR   ProteomicsDB; 246967; -. [Q00218-1]
DR   EnsemblPlants; AT4G33510.1; AT4G33510.1; AT4G33510. [Q00218-1]
DR   GeneID; 829489; -.
DR   Gramene; AT4G33510.1; AT4G33510.1; AT4G33510. [Q00218-1]
DR   KEGG; ath:AT4G33510; -.
DR   Araport; AT4G33510; -.
DR   TAIR; locus:2005526; AT4G33510.
DR   eggNOG; ENOG502QPP7; Eukaryota.
DR   HOGENOM; CLU_026885_0_1_1; -.
DR   InParanoid; Q00218; -.
DR   OMA; MQRVNEW; -.
DR   PhylomeDB; Q00218; -.
DR   UniPathway; UPA00053; UER00084.
DR   PRO; PR:Q00218; -.
DR   Proteomes; UP000006548; Chromosome 4.
DR   ExpressionAtlas; Q00218; baseline and differential.
DR   Genevisible; Q00218; AT.
DR   GO; GO:0009507; C:chloroplast; HDA:TAIR.
DR   GO; GO:0009534; C:chloroplast thylakoid; HDA:TAIR.
DR   GO; GO:0005886; C:plasma membrane; HDA:TAIR.
DR   GO; GO:0003849; F:3-deoxy-7-phosphoheptulonate synthase activity; IEA:UniProtKB-EC.
DR   GO; GO:0009073; P:aromatic amino acid family biosynthetic process; IEA:UniProtKB-KW.
DR   GO; GO:0008652; P:cellular amino acid biosynthetic process; IEA:UniProtKB-KW.
DR   GO; GO:0009423; P:chorismate biosynthetic process; IEA:UniProtKB-UniPathway.
DR   Gene3D; 3.20.20.70; -; 2.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR002480; DAHP_synth_2.
DR   PANTHER; PTHR21337; PTHR21337; 1.
DR   Pfam; PF01474; DAHP_synth_2; 1.
DR   TIGRFAMs; TIGR01358; DAHP_synth_II; 1.
PE   2: Evidence at transcript level;
KW   Alternative splicing; Amino-acid biosynthesis;
KW   Aromatic amino acid biosynthesis; Chloroplast; Plastid; Reference proteome;
KW   Transferase; Transit peptide.
FT   TRANSIT         1..?
FT                   /note="Chloroplast"
FT                   /evidence="ECO:0000255"
FT   CHAIN           ?..507
FT                   /note="Phospho-2-dehydro-3-deoxyheptonate aldolase 2,
FT                   chloroplastic"
FT                   /id="PRO_0000002299"
FT   CONFLICT        165
FT                   /note="S -> L (in Ref. 1; AAA32785)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   507 AA;  56149 MW;  8B58271053399AA1 CRC64;
     MVTLNASSPL TTKSFLPYRH APRRPISFSP VFAVHSTDPK KSTQSASASV KWSLESWKSK
     KALQLPDYPD QKDVDSVLQT LSSFPPIVFA GEARKLEDKL GQAAMGQAFM LQGGDCAESF
     KEFNANNIRD TFRVLLQMGV VLMFGGQLPV IKVGRMAGQF AKPRSDPFEE KDGVKLPSYR
     GDNINGDAFD EKSRIPDPHR MVRAYTQSVA TLNLLRAFAT GGYAAMQRVS QWNLDFTQHS
     EQGDRYRELA NRVDEALGFM GAAGLTSAHP IMTTTEFWTS HECLLLPYEQ ALTREDSTSG
     LYYDCSAHML WVGERTRQLD GAHVEFLRGI ANPLGIKVSD KMVPSELVKL IEILNPQNKP
     GRITVIVRMG AENMRVKLPN LIRAVRGAGQ IVTWVSDPMH GNTIMAPGGL KTRSFDAIRA
     ELRAFFDVHD QEGSFPGGVH LEMTGQNVTE CVGGSRTITY NDLSSRYHTH CDPRLNASQS
     LELAFIIAER LRKRRLGSGN LPSSIGV