ID B7JCE0_ECOLX Unreviewed; 278 AA.
AC B7JCE0;
DT 10-FEB-2009, integrated into UniProtKB/TrEMBL.
DT 10-FEB-2009, sequence version 1.
DT 27-MAR-2024, entry version 45.
DE RecName: Full=3-deoxy-7-phosphoheptulonate synthase {ECO:0000256|ARBA:ARBA00012694};
DE EC=2.5.1.54 {ECO:0000256|ARBA:ARBA00012694};
DE AltName: Full=3-deoxy-D-arabino-heptulosonate 7-phosphate synthase {ECO:0000256|ARBA:ARBA00032193};
DE AltName: Full=DAHP synthase {ECO:0000256|ARBA:ARBA00031349};
DE AltName: Full=Phospho-2-keto-3-deoxyheptonate aldolase {ECO:0000256|ARBA:ARBA00031111};
GN ORFNames=pO103_47 {ECO:0000313|EMBL:ACJ63532.1};
OS Escherichia coli.
OG Plasmid pAPEC-O103-ColBM {ECO:0000313|EMBL:ACJ63532.1}.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=562 {ECO:0000313|EMBL:ACJ63532.1};
RN [1] {ECO:0000313|EMBL:ACJ63532.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=APEC O103 {ECO:0000313|EMBL:ACJ63532.1};
RC PLASMID=pAPEC-O103-ColBM {ECO:0000313|EMBL:ACJ63532.1};
RX PubMed=20160015; DOI=10.1128/IAI.01174-09;
RA Johnson T.J., Jordan D., Kariyawasam S., Stell A.L., Bell N.P.,
RA Wannemuehler Y.M., Alarcon C.F., Li G., Tivendale K.A., Logue C.M.,
RA Nolan L.K.;
RT "Sequence analysis and characterization of a transferable hybrid plasmid
RT encoding multidrug resistance and enabling zoonotic potential for
RT extraintestinal Escherichia coli.";
RL Infect. Immun. 78:1931-1942(2010).
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 -!- 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 -!- PATHWAY: Metabolic intermediate biosynthesis; chorismate biosynthesis;
CC chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step
CC 1/7. {ECO:0000256|ARBA:ARBA00004688}.
CC -!- SIMILARITY: Belongs to the class-I DAHP synthase family.
CC {ECO:0000256|ARBA:ARBA00007985}.
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DR EMBL; CP001232; ACJ63532.1; -; Genomic_DNA.
DR RefSeq; WP_000140241.1; NZ_PHSR02000055.1.
DR RefSeq; YP_002527503.1; NC_011964.1.
DR AlphaFoldDB; B7JCE0; -.
DR UniPathway; UPA00053; UER00084.
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:InterPro.
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:SF12; PHOSPHO-2-DEHYDRO-3-DEOXYHEPTONATE ALDOLASE, PHE-SENSITIVE; 1.
DR Pfam; PF00793; DAHP_synth_1; 1.
DR SUPFAM; SSF51569; Aldolase; 1.
PE 3: Inferred from homology;
KW Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022605};
KW Plasmid {ECO:0000313|EMBL:ACJ63532.1};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 19..271
FT /note="DAHP synthetase I/KDSA"
FT /evidence="ECO:0000259|Pfam:PF00793"
SQ SEQUENCE 278 AA; 30992 MW; 7696F64CC288176E CRC64;
MTESAEKNFP AYSHLPKYLS KMYIVMRTYF EKPRTRKGWK GIMHDPDLNG SYDVEKGIRY
ARQCLSSITT MRVATATEFL DPFLTPYIAD LICWGAIGAR TTESQTHRQL ASGLHCPVGF
KNSTDGNINL AIDAIIAARE QHIVYMTSLT NSISTLLTDG NPHGHLILRG GREPNYGLSD
ITKAVKLMHD EGINHRLIID CSHGNSGKVA KRQISVARQV IDNRKKIPGY VAGIMVESFL
QDGKQSDSFP LEYGQSVTDE CISWQQTEQL LSTLAAQL
//
