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Database: UniProt
Entry: W1FRL3_ECOLX
LinkDB: W1FRL3_ECOLX
Original site: W1FRL3_ECOLX 
ID   W1FRL3_ECOLX            Unreviewed;       315 AA.
AC   W1FRL3;
DT   19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT   19-MAR-2014, sequence version 1.
DT   08-MAY-2019, entry version 21.
DE   RecName: Full=Phospho-2-dehydro-3-deoxyheptonate aldolase {ECO:0000256|PIRNR:PIRNR001361};
DE            EC=2.5.1.54 {ECO:0000256|PIRNR:PIRNR001361};
OS   Escherichia coli ISC11.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=1432557 {ECO:0000313|EMBL:CDL36443.1, ECO:0000313|Proteomes:UP000019194};
RN   [1] {ECO:0000313|EMBL:CDL36443.1, ECO:0000313|Proteomes:UP000019194}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ISC11 {ECO:0000313|EMBL:CDL36443.1,
RC   ECO:0000313|Proteomes:UP000019194};
RA   Barisic I., Mitteregger D., Hirschl A.M., Noehammer C.,
RA   Wiesinger-Mayr H.;
RT   "Antibiotic resistance diversity of beta-lactamase producers in the
RT   General Hospital Vienna.";
RL   Submitted (OCT-2013) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Stereospecific condensation of phosphoenolpyruvate (PEP)
CC       and D-erythrose-4-phosphate (E4P) giving rise to 3-deoxy-D-
CC       arabino-heptulosonate-7-phosphate (DAHP).
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;
CC         EC=2.5.1.54; Evidence={ECO:0000256|PIRNR:PIRNR001361};
CC   -!- PATHWAY: Metabolic intermediate biosynthesis; chorismate
CC       biosynthesis; chorismate from D-erythrose 4-phosphate and
CC       phosphoenolpyruvate: step 1/7. {ECO:0000256|PIRNR:PIRNR001361}.
CC   -!- SIMILARITY: Belongs to the class-I DAHP synthase family.
CC       {ECO:0000256|PIRNR:PIRNR001361}.
CC   -!- CAUTION: The sequence shown here is derived from an
CC       EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
CC       preliminary data. {ECO:0000313|EMBL:CDL36443.1}.
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DR   EMBL; CBWP010000012; CDL36443.1; -; Genomic_DNA.
DR   EnsemblBacteria; CDL36443; CDL36443; CDL36443.
DR   UniPathway; UPA00053; UER00084.
DR   Proteomes; UP000019194; Unassembled WGS sequence.
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: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 {ECO:0000256|PIRNR:PIRNR001361};
KW   Aromatic amino acid biosynthesis {ECO:0000256|PIRNR:PIRNR001361};
KW   Complete proteome {ECO:0000313|Proteomes:UP000019194};
KW   Reference proteome {ECO:0000313|Proteomes:UP000019194};
KW   Transferase {ECO:0000256|PIRNR:PIRNR001361,
KW   ECO:0000256|SAAS:SAAS00080156, ECO:0000313|EMBL:CDL36443.1}.
FT   DOMAIN        9    303       DAHP_synth_1. {ECO:0000259|Pfam:PF00793}.
SQ   SEQUENCE   315 AA;  33889 MW;  DE838AE5DBD23FD3 CRC64;
     MAHARKAIHK ILKGSDDRLL VVIGPCSIHD PAAAKEYAAR LLALREELKG ELEIVMRVYF
     EKPRTTVGWK GLINDPHMDN SFQINDGLRI ARKLLLDIND SGLPAAGEFL DMITPQYLAD
     LMSWGAIGAR TTESQVHREL ASGLSCPVGF KNGTDGTIKV AIDAINAAGA PHCFLSVTKW
     GHSAIVNTSG NGDCHIILRG GKEPNYSAQH VADVKEGLIK AGLSAQVMID FSHANSCKQF
     KKQMDVAKDV CGQVAGGEKA IIGVMIESHL VEGNQNPDSG EPLTYGKSIT DACIGWEDTD
     AVLRQLAEAV KARRG
//
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