ID   AROH_BUCAP              Reviewed;         348 AA.
AC   P46245;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   30-AUG-2002, sequence version 2.
DT   03-AUG-2022, entry version 126.
DE   RecName: Full=Phospho-2-dehydro-3-deoxyheptonate aldolase, Trp-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;
GN   Name=aroH; OrderedLocusNames=BUsg_116;
OS   Buchnera aphidicola subsp. Schizaphis graminum (strain Sg).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Erwiniaceae; Buchnera.
OX   NCBI_TaxID=198804;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=7766160; DOI=10.1007/bf00295507;
RA   Kolibachuk D., Rouhbakhsh D., Baumann P.;
RT   "Aromatic amino acid biosynthesis in Buchnera aphidicola (endosymbiont of
RT   aphids): cloning and sequencing of a DNA fragment containing aroH-thrS-
RT   infC-rpmI-rplT.";
RL   Curr. Microbiol. 30:313-316(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Sg;
RX   PubMed=12089438; DOI=10.1126/science.1071278;
RA   Tamas I., Klasson L., Canbaeck B., Naeslund A.K., Eriksson A.-S.,
RA   Wernegreen J.J., Sandstroem J.P., Moran N.A., Andersson S.G.E.;
RT   "50 million years of genomic stasis in endosymbiotic bacteria.";
RL   Science 296:2376-2379(2002).
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; U11066; AAC43604.1; -; Genomic_DNA.
DR   EMBL; AE013218; AAM67685.1; -; Genomic_DNA.
DR   PIR; I40070; I40070.
DR   RefSeq; WP_011053651.1; NC_004061.1.
DR   AlphaFoldDB; P46245; -.
DR   SMR; P46245; -.
DR   STRING; 198804.BUsg_116; -.
DR   EnsemblBacteria; AAM67685; AAM67685; BUsg_116.
DR   KEGG; bas:BUsg_116; -.
DR   eggNOG; COG0722; Bacteria.
DR   HOGENOM; CLU_030903_0_1_6; -.
DR   OMA; PCLSWED; -.
DR   OrthoDB; 853329at2; -.
DR   UniPathway; UPA00053; UER00084.
DR   Proteomes; UP000000416; Chromosome.
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   3: Inferred from homology;
KW   Amino-acid biosynthesis; Aromatic amino acid biosynthesis; Transferase.
FT   CHAIN           1..348
FT                   /note="Phospho-2-dehydro-3-deoxyheptonate aldolase, Trp-
FT                   sensitive"
FT                   /id="PRO_0000140838"
FT   CONFLICT        137..142
FT                   /note="MPAATE -> CLQQQS (in Ref. 1; AAC43604)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   348 AA;  39148 MW;  BD601FB68AFFD500 CRC64;
     MKKTDELRTI RIDPLITPSE LAKKYAITSE IMDNVIITRQ NIARIMTGED LRLLVVIGPC
     SVHDPIAAVE YAHRLYELRK KYQDRLEIIM RTYFEKPRTV VGWKGLISDP DLNGSFRVNH
     GLAVARKLLL DINELGMPAA TEFLDMVIGQ FIADLISWGA IGARTTESQI HREMASALSC
     PVGFKNGTDG NIRIAIDAIR AAQARHLFFA PNKDGQMTIN HTSGNPYGHI IMRGGRTPNY
     HAHDINSAIE HLREFNLLEH LMIDFSHGNC LKEHIRQKDV AKSVSKQISQ GSKTIFGVMI
     ESFLEEGFQT VKENQPLIYG KSITDACLNW KDSVLIIKQL ADAVDTRF