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Database: UniProt
Entry: Q93K85_ECOLX
LinkDB: Q93K85_ECOLX
Original site: Q93K85_ECOLX 
ID   Q93K85_ECOLX            Unreviewed;       344 AA.
AC   Q93K85;
DT   01-DEC-2001, integrated into UniProtKB/TrEMBL.
DT   01-DEC-2001, sequence version 1.
DT   24-JAN-2024, entry version 96.
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.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=562 {ECO:0000313|EMBL:CAC43413.1};
RN   [1] {ECO:0000313|EMBL:CAC43413.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=536 {ECO:0000313|EMBL:CAC43413.1};
RX   PubMed=11401961; DOI=10.1128/IAI.69.7.4248-4256.2001;
RA   Dobrindt U., Blum-Oehler G., Hartsch T., Gottschalk G., Ron E.Z.,
RA   Funfstuck R., Hacker J.;
RT   "S-fimbria-encoding determinant sfa(I) is located on pathogenicity island
RT   III(536) of uropathogenic Escherichia coli strain 536.";
RL   Infect. Immun. 69:4248-4256(2001).
RN   [2] {ECO:0000313|EMBL:CAC43413.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=536 {ECO:0000313|EMBL:CAC43413.1};
RX   PubMed=12379716; DOI=10.1128/IAI.70.11.6365-6372.2002;
RA   Dobrindt U., Blum-Oehler G., Nagy G., Schneider G., Johann A.,
RA   Gottschalk G., Hacker J.;
RT   "Genetic structure and distribution of four pathogenicity islands (PAI
RT   I(536) to PAI IV(536)) of uropathogenic Escherichia coli strain 536.";
RL   Infect. Immun. 70:6365-6372(2002).
RN   [3] {ECO:0000313|EMBL:CAC43413.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=536 {ECO:0000313|EMBL:CAC43413.1};
RA   Dobrindt U.;
RL   Submitted (FEB-2003) to the EMBL/GenBank/DDBJ databases.
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; X16664; CAC43413.1; -; Genomic_DNA.
DR   RefSeq; WP_001335133.1; NZ_VOTL01000027.1.
DR   AlphaFoldDB; Q93K85; -.
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: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:SF12; PHOSPHO-2-DEHYDRO-3-DEOXYHEPTONATE ALDOLASE, PHE-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|ARBA:ARBA00022605,
KW   ECO:0000256|PIRNR:PIRNR001361};
KW   Aromatic amino acid biosynthesis {ECO:0000256|PIRNR:PIRNR001361};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR001361}.
FT   DOMAIN          41..337
FT                   /note="DAHP synthetase I/KDSA"
FT                   /evidence="ECO:0000259|Pfam:PF00793"
SQ   SEQUENCE   344 AA;  38165 MW;  9D12A25E6DCA64AA CRC64;
     MQSVSKSIYR GKLLGSLPAV GEIHKEIAVS EETVTWISLQ REIIANILLG KDPRLLVIVG
     PCSIHDVQAA VEYAKRLSVL QNKYLSQMYI VMRTYFEKPR TRKGWKGIMH EPDLNGSYNV
     EKGIRYARQC LSSITTMRVA TATEFLDPFL TPYIADLICW GAVGARTTES QTHRQLASGL
     HCPVGFKNST DGNINLAIDA ILAAREQHVV YMTSLTKCIS TLLTDGNPHG HLILRGGREP
     NYGLSDITKA VKLMHDEGIN HRLIIDCSHG NSGKVAERQI SVAREVIDNR KKMPGYVAGI
     MLESFLQGGK QSDSLPREYG QSVTDECLSW QQTEQLLSTL AAQL
//
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