ID   AROG_AMYME              Reviewed;         203 AA.
AC   Q44093;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   25-MAY-2022, entry version 82.
DE   RecName: Full=Phospho-2-dehydro-3-deoxyheptonate aldolase;
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;
DE   Flags: Fragment;
GN   Name=aroA;
OS   Amycolatopsis methanolica.
OC   Bacteria; Actinobacteria; Pseudonocardiales; Pseudonocardiaceae;
OC   Amycolatopsis; Amycolatopsis methanolica group.
OX   NCBI_TaxID=1814;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=8550409; DOI=10.1128/jb.178.1.149-155.1996;
RA   Alves A.M., Meijer W.G., Vrijbloed J.W., Dijkhuizen L.;
RT   "Characterization and phylogeny of the pfp gene of Amycolatopsis
RT   methanolica encoding PPi-dependent phosphofructokinase.";
RL   J. Bacteriol. 178:149-155(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Rodrigues Alves A.M.;
RL   Submitted (JUL-1995) to the EMBL/GenBank/DDBJ databases.
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   -!- PATHWAY: Metabolic intermediate biosynthesis; chorismate biosynthesis;
CC       chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step
CC       1/7.
CC   -!- SIMILARITY: Belongs to the class-I DAHP synthase family. {ECO:0000305}.
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DR   EMBL; U31277; AAB01682.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q44093; -.
DR   SMR; Q44093; -.
DR   UniPathway; UPA00053; UER00084.
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; -; 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   TIGRFAMs; TIGR00034; aroFGH; 1.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis; Aromatic amino acid biosynthesis; Transferase.
FT   CHAIN           1..>203
FT                   /note="Phospho-2-dehydro-3-deoxyheptonate aldolase"
FT                   /id="PRO_0000140828"
FT   REGION          1..28
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   NON_TER         203
SQ   SEQUENCE   203 AA;  21886 MW;  F4F063F8BFEF7909 CRC64;
     MIDRLVRDSR GPVTERNPPH MSLSAGPAEI SEGLDNQRTL GVSPLISPAL LRQELPVDAA
     IAKTVAHGRS SAVDILHGDD DRLIVVVGPC SVHDPAAALD YAHRLAEHAA GVRDELHVIM
     RVYFEKPRTT LGWKGLINDP DLDGSYAVNK GLRMARKLLL DISALGLPVG CEFLDPITPQ
     FIADTVSWGS IGARTAASQV HRQ