ID   AROF_ENTAG              Reviewed;         213 AA.
AC   Q02285;
DT   01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-APR-1993, sequence version 1.
DT   25-MAY-2022, entry version 89.
DE   RecName: Full=Phospho-2-dehydro-3-deoxyheptonate aldolase, Tyr-sensitive;
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=aroF;
OS   Enterobacter agglomerans (Erwinia herbicola) (Pantoea agglomerans).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Erwiniaceae; Pantoea; Pantoea agglomerans group.
OX   NCBI_TaxID=549;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=1512561; DOI=10.1099/00221287-138-7-1309;
RA   Xia T., Zhao G., Fischer R.S., Jensen R.A.;
RT   "A monofunctional prephenate dehydrogenase created by cleavage of the 5'
RT   109 bp of the tyrA gene from Erwinia herbicola.";
RL   J. Gen. Microbiol. 138:1309-1316(1992).
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   -!- MISCELLANEOUS: There are 3 DAHP synthases, AroF is feedback-inhibited
CC       by Tyr. The other 2 DAHP synthases are Phe- and Trp-sensitive,
CC       respectively.
CC   -!- SIMILARITY: Belongs to the class-I DAHP synthase family. {ECO:0000305}.
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DR   EMBL; X60420; CAA42951.1; -; Genomic_DNA.
DR   PIR; S26055; S26055.
DR   AlphaFoldDB; Q02285; -.
DR   SMR; Q02285; -.
DR   STRING; 549.BW31_02111; -.
DR   eggNOG; COG0722; Bacteria.
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..213
FT                   /note="Phospho-2-dehydro-3-deoxyheptonate aldolase, Tyr-
FT                   sensitive"
FT                   /id="PRO_0000140832"
FT   NON_TER         1
SQ   SEQUENCE   213 AA;  22967 MW;  3C6A35809FD4DBDF CRC64;
     DPNSPQYLGD LFSWSAIGAR TTESQTHREM ASGLSMPVGF KNGTDGSLGT AINAMRAAAM
     PHRFVGINQA GQVCLLQTQG NPDGHVILRG GKAPNYGPED VAQCEKEMLK AGLRPALMID
     CSHGNSNKDY SRQPGVAESA IAQIKDGNRS IIGLMLESHI NEGNQSSEQP RSEMKYGVSV
     TDACINWEVT ETLLREMHQD LQGVLSARLS QEV