ID B7LDJ0_ECO55 Unreviewed; 356 AA.
AC B7LDJ0;
DT 10-FEB-2009, integrated into UniProtKB/TrEMBL.
DT 10-FEB-2009, sequence version 1.
DT 27-MAR-2024, entry version 73.
DE RecName: Full=Phospho-2-dehydro-3-deoxyheptonate aldolase {ECO:0000256|PIRNR:PIRNR001361};
DE EC=2.5.1.54 {ECO:0000256|PIRNR:PIRNR001361};
GN Name=aroF {ECO:0000313|EMBL:CAU98756.1};
GN OrderedLocusNames=EC55989_2890 {ECO:0000313|EMBL:CAU98756.1};
OS Escherichia coli (strain 55989 / EAEC).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=585055 {ECO:0000313|EMBL:CAU98756.1, ECO:0000313|Proteomes:UP000000746};
RN [1] {ECO:0000313|Proteomes:UP000000746}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=55989 / EAEC {ECO:0000313|Proteomes:UP000000746};
RX PubMed=19165319; DOI=10.1371/journal.pgen.1000344;
RA Touchon M., Hoede C., Tenaillon O., Barbe V., Baeriswyl S., Bidet P.,
RA Bingen E., Bonacorsi S., Bouchier C., Bouvet O., Calteau A., Chiapello H.,
RA Clermont O., Cruveiller S., Danchin A., Diard M., Dossat C., Karoui M.E.,
RA Frapy E., Garry L., Ghigo J.M., Gilles A.M., Johnson J., Le Bouguenec C.,
RA Lescat M., Mangenot S., Martinez-Jehanne V., Matic I., Nassif X., Oztas S.,
RA Petit M.A., Pichon C., Rouy Z., Ruf C.S., Schneider D., Tourret J.,
RA Vacherie B., Vallenet D., Medigue C., Rocha E.P.C., Denamur E.;
RT "Organised genome dynamics in the Escherichia coli species results in
RT highly diverse adaptive paths.";
RL PLoS Genet. 5:E1000344-E1000344(2009).
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:0000256|ARBA:ARBA00003726,
CC ECO:0000256|PIRNR:PIRNR001361}.
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 Evidence={ECO:0000256|ARBA:ARBA00001370,
CC ECO:0000256|PIRNR:PIRNR001361};
CC -!- PATHWAY: Metabolic intermediate biosynthesis; chorismate biosynthesis;
CC chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step
CC 1/7. {ECO:0000256|ARBA:ARBA00004688, ECO:0000256|PIRNR:PIRNR001361}.
CC -!- SIMILARITY: Belongs to the class-I DAHP synthase family.
CC {ECO:0000256|ARBA:ARBA00007985, ECO:0000256|PIRNR:PIRNR001361}.
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DR EMBL; CU928145; CAU98756.1; -; Genomic_DNA.
DR RefSeq; WP_001168054.1; NC_011748.1.
DR AlphaFoldDB; B7LDJ0; -.
DR GeneID; 75205862; -.
DR KEGG; eck:EC55989_2890; -.
DR HOGENOM; CLU_030903_0_1_6; -.
DR UniPathway; UPA00053; UER00084.
DR Proteomes; UP000000746; Chromosome.
DR GO; GO:0003849; F:3-deoxy-7-phosphoheptulonate synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0008652; P:amino acid biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0009073; P:aromatic amino acid family biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0009423; P:chorismate biosynthetic process; IEA:UniProtKB-UniPathway.
DR Gene3D; 3.20.20.70; Aldolase class I; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR006218; DAHP1/KDSA.
DR InterPro; IPR006219; DAHP_synth_1.
DR NCBIfam; TIGR00034; aroFGH; 1.
DR PANTHER; PTHR21225; PHOSPHO-2-DEHYDRO-3-DEOXYHEPTONATE ALDOLASE DAHP SYNTHETASE; 1.
DR PANTHER; PTHR21225:SF10; PHOSPHO-2-DEHYDRO-3-DEOXYHEPTONATE ALDOLASE, TYR-SENSITIVE; 1.
DR Pfam; PF00793; DAHP_synth_1; 1.
DR PIRSF; PIRSF001361; DAHP_synthase; 1.
DR SUPFAM; SSF51569; Aldolase; 1.
PE 3: Inferred from homology;
KW Amino-acid biosynthesis {ECO:0000256|PIRNR:PIRNR001361};
KW Aromatic amino acid biosynthesis {ECO:0000256|PIRNR:PIRNR001361};
KW Reference proteome {ECO:0000313|Proteomes:UP000000746};
KW Transferase {ECO:0000256|PIRNR:PIRNR001361, ECO:0000313|EMBL:CAU98756.1}.
FT DOMAIN 40..340
FT /note="DAHP synthetase I/KDSA"
FT /evidence="ECO:0000259|Pfam:PF00793"
SQ SEQUENCE 356 AA; 38846 MW; 89B541980D243E6E CRC64;
MQKDALNNVH ITDEQVLMTP EQLKAAFPLS LQQEAQIADS RRTISDIIAG RDPRLLVVCG
PCSIHDPETA LEYARRFKAL AAEVSDSLYL VMRVYFEKPR TTVGWKGLIN DPHMDGSFDV
EAGLQIARKL LLELVNMGLP LATEALDPNS PQYLGDLFSW SAIGARTTES QTHREMASGL
SMPVGFKNGT DGSLATAINA MRAAAQPHRF VGINQAGQVA LLQTQGNPDG HVILRGGKAP
NYSPADVAQC EKEMEQAGLR PSLMVDCSHG NSNKDYRRQP AVAESVVAQI KDGNRSIIGL
MIESNIHEGN QSSEQPRSEM KYGVSVTDAC ISWEMTDALL REIHQDLNGQ LTARVA
//
