ID   AROF_CATRO              Reviewed;         493 AA.
AC   A0MH68;
DT   04-DEC-2007, integrated into UniProtKB/Swiss-Prot.
DT   04-DEC-2007, sequence version 2.
DT   02-SEP-2026, entry version 58.
DE   RecName: Full=Probable phospho-2-dehydro-3-deoxyheptonate aldolase, chloroplastic;
DE            EC=2.5.1.54;
DE   AltName: Full=3-deoxy-D-arabino-heptulosonate 7-phosphate synthase;
DE   AltName: Full=CrDHS1;
DE   AltName: Full=DAHP synthase;
DE   AltName: Full=Phospho-2-keto-3-deoxyheptonate aldolase;
DE   Flags: Precursor;
GN   Name=DHS1;
OS   Catharanthus roseus (Madagascar periwinkle) (Vinca rosea).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; lamiids; Gentianales; Apocynaceae; Rauvolfioideae; Vinceae;
OC   Catharanthinae; Catharanthus.
OX   NCBI_TaxID=4058;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Ramani S., Chelliah J.;
RL   Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
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   -!- PATHWAY: Metabolic intermediate biosynthesis; chorismate biosynthesis;
CC       chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step
CC       1/7.
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the class-II DAHP synthase family.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=ABK29527.1; Type=Frameshift; Evidence={ECO:0000305};
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; DQ859024; ABK29527.1; ALT_FRAME; mRNA.
DR   AlphaFoldDB; A0MH68; -.
DR   SMR; A0MH68; -.
DR   UniPathway; UPA00053; UER00084.
DR   GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
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:InterPro.
DR   GO; GO:0009423; P:chorismate biosynthetic process; IEA:UniProtKB-UniPathway.
DR   FunFam; 3.20.20.70:FF:000128; Phospho-2-dehydro-3-deoxyheptonate aldolase; 1.
DR   Gene3D; 3.20.20.70; Aldolase class I; 1.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR002480; DAHP_synth_2.
DR   PANTHER; PTHR21337; PHOSPHO-2-DEHYDRO-3-DEOXYHEPTONATE ALDOLASE 1, 2; 1.
DR   PANTHER; PTHR21337:SF24; PHOSPHO-2-DEHYDRO-3-DEOXYHEPTONATE ALDOLASE 1, CHLOROPLASTIC; 1.
DR   Pfam; PF01474; DAHP_synth_2; 1.
DR   SUPFAM; SSF51569; Aldolase; 1.
DR   PROSITE; PS52062; DAHPS_II; 1.
PE   2: Evidence at transcript level;
KW   Amino-acid biosynthesis; Aromatic amino acid biosynthesis; Chloroplast;
KW   Plastid; Transferase; Transit peptide.
FT   TRANSIT         1..58
FT                   /note="Chloroplast"
FT                   /evidence="ECO:0000255"
FT   CHAIN           59..493
FT                   /note="Probable phospho-2-dehydro-3-deoxyheptonate
FT                   aldolase, chloroplastic"
FT                   /id="PRO_0000312804"
FT   DOMAIN          126..493
FT                   /note="DAHPS class-II TIM-barrel"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01407"
FT   BINDING         174
FT                   /ligand="phosphoenolpyruvate"
FT                   /ligand_id="ChEBI:CHEBI:58702"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01407"
FT   BINDING         315..316
FT                   /ligand="phosphoenolpyruvate"
FT                   /ligand_id="ChEBI:CHEBI:58702"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01407"
FT   BINDING         338
FT                   /ligand="phosphoenolpyruvate"
FT                   /ligand_id="ChEBI:CHEBI:58702"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01407"
FT   BINDING         369
FT                   /ligand="phosphoenolpyruvate"
FT                   /ligand_id="ChEBI:CHEBI:58702"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01407"
SQ   SEQUENCE   493 AA;  54743 MW;  EF247BADC19098AB CRC64;
     MAMSNTSALA SKLLPSCKPH QPTLTFFSPS TTCQKKPRSS RPISAAVHVT QPPKTPISSA
     TATKRRLSLL NGVWESWKSK KALQLPEYPD EGKLDGVLKT IEAFPPLVFA GEARSLEEKL
     AQAAMGNAFL LQGGDCAESF KELMPLYSRY FQNTASDECR LTFGGQCPVI KVGRMAGQFA
     KPRLDPFEEK DGLWLSGANG WPVAWEAYCK LQQLSPSRAL LLVVCCYAES HPMDLDFVEH
     SEQGDRYQEL AHRVDEALGF MDACGLTVDH PIMATTEFWT SHECLLLPYE QALTREDSTS
     GLFYDCSAHM LWVGERTRQL DGAHVEFLRG VANPLGIKVS QKMDPNELVN LIEILNPTNK
     PGRITVIVRM GAENMRVKLP HLIRAVRGAG QIVTWVCDPM HGNTIKAPCG LKTRAFDAIL
     AEVRAFYDVH EQEGTLPGTE CVGGSRTITY DDRQTRYHTH CDPRLNASQS LELAFIIAER
     LRKEESVLNA HSP
//