ID   AROF_CANAX              Reviewed;         368 AA.
AC   P34725;
DT   01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1994, sequence version 1.
DT   25-MAY-2022, entry version 87.
DE   RecName: Full=Phospho-2-dehydro-3-deoxyheptonate aldolase, phenylalanine-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=ARO3;
OS   Candida albicans (Yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX   NCBI_TaxID=5476;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=ATCC 11651 / B792 / 171D;
RX   PubMed=7901125; DOI=10.1016/0378-1119(93)90191-5;
RA   Pereira S.A., Livi G.P.;
RT   "Cloning and expression of the ARO3 gene encoding DAHP synthase from
RT   Candida albicans.";
RL   Gene 132:159-165(1993).
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 phenyalanine.
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; L12217; AAA71966.1; -; Unassigned_DNA.
DR   PIR; JN0865; JN0865.
DR   AlphaFoldDB; P34725; -.
DR   SMR; P34725; -.
DR   VEuPathDB; FungiDB:C2_02030W_A; -.
DR   VEuPathDB; FungiDB:CAWG_03971; -.
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   PIRSF; PIRSF001361; DAHP_synthase; 1.
DR   TIGRFAMs; TIGR00034; aroFGH; 1.
PE   2: Evidence at transcript level;
KW   Amino-acid biosynthesis; Aromatic amino acid biosynthesis; Transferase.
FT   CHAIN           1..368
FT                   /note="Phospho-2-dehydro-3-deoxyheptonate aldolase,
FT                   phenylalanine-inhibited"
FT                   /id="PRO_0000140848"
SQ   SEQUENCE   368 AA;  40731 MW;  3F5F64E1A6A80F73 CRC64;
     MFITNEHVGD RSRMEDWRIR GYDPLTPPDL LQHEYPLTPE SQKIIVEGRN AACDILNGKD
     RRLIGPCSIH DPQAALDYCE RLYQASEKHK GELLIVMRAY LEKPRTTVGW KGLINDPDID
     GTFHINKGLR IARKLFVQLT SKLPIAGEML DTISPQFLSD LFSVGAIGAR TTESQLHREL
     ASGYHSQLDS KTVPMVLWVL PLTPLRAASH PHHFLSVTKP GVVAIVGTDG NQDCFVILRG
     GKKGTNYDAK SVQETQEELI KSKVVTEMKP GPRIMVDCSH GNSNKDHRNQ PKVAQVVAEQ
     VAGGDKSICG LMIESNINDG RQDVPPKEQG GKDALKYGVS ITDACIGWET TEEVLEVLAN
     AVKTRRSL