AROH_ECOL6
ID AROH_ECOL6 Reviewed; 348 AA.
AC Q8FH32;
DT 20-JUN-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 96.
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=c2100;
OS Escherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=199310;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CFT073 / ATCC 700928 / UPEC;
RX PubMed=12471157; DOI=10.1073/pnas.252529799;
RA Welch R.A., Burland V., Plunkett G. III, Redford P., Roesch P., Rasko D.,
RA Buckles E.L., Liou S.-R., Boutin A., Hackett J., Stroud D., Mayhew G.F.,
RA Rose D.J., Zhou S., Schwartz D.C., Perna N.T., Mobley H.L.T.,
RA Donnenberg M.S., Blattner F.R.;
RT "Extensive mosaic structure revealed by the complete genome sequence of
RT uropathogenic Escherichia coli.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:17020-17024(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). {ECO:0000250}.
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; AE014075; AAN80560.1; -; Genomic_DNA.
DR RefSeq; WP_001082226.1; NC_004431.1.
DR AlphaFoldDB; Q8FH32; -.
DR SMR; Q8FH32; -.
DR STRING; 199310.c2100; -.
DR EnsemblBacteria; AAN80560; AAN80560; c2100.
DR GeneID; 58463920; -.
DR KEGG; ecc:c2100; -.
DR eggNOG; COG0722; Bacteria.
DR HOGENOM; CLU_030903_0_1_6; -.
DR OMA; PCLSWED; -.
DR BioCyc; ECOL199310:C2100-MON; -.
DR UniPathway; UPA00053; UER00084.
DR Proteomes; UP000001410; 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_0000140841"
SQ SEQUENCE 348 AA; 38705 MW; 52C3D89F85B226E0 CRC64;
MNRTDELRTA RIESLVTPAE LALRYPVTPG VATHVTDSRR RIEKILNGED KRLLVIIGPC
SIHDLTAAME YATRLQSLRN QYQSRLEIVM RTYFEKPRTV VGWKGLISDP DLNGSYRVNH
GLELARKLLL QVNELGVPTA TEFLDMVTGQ FIADLISWGA IGARTTESQI HREMASALSC
PVGFKNGTDG NTRIAVDAIR AARASHMFLS PDKNGQMTIY QTSGNPYGHI IMRGGKKPNY
HADDIAAACD TLHEFDLPEH LVVDFSHGNC QKQHRRQLEV CEDICQQIRN GSTAIAGIMA
ESFLREGTQK IVGGQPLTYG QSITDPCLGW EDTERLVEKL ASAVDTRF
