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Database: UniProt
Entry: A0A085JDS9_9GAMM
LinkDB: A0A085JDS9_9GAMM
Original site: A0A085JDS9_9GAMM 
ID   A0A085JDS9_9GAMM        Unreviewed;       361 AA.
AC   A0A085JDS9;
DT   29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   29-OCT-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};
GN   ORFNames=GTPT_2386 {ECO:0000313|EMBL:KFD18625.1};
OS   Tatumella ptyseos ATCC 33301.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Erwiniaceae; Tatumella.
OX   NCBI_TaxID=1005995 {ECO:0000313|EMBL:KFD18625.1, ECO:0000313|Proteomes:UP000028602};
RN   [1] {ECO:0000313|EMBL:KFD18625.1, ECO:0000313|Proteomes:UP000028602}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 33301 {ECO:0000313|EMBL:KFD18625.1,
RC   ECO:0000313|Proteomes:UP000028602};
RA   Plunkett G.III., Neeno-Eckwall E.C., Glasner J.D., Perna N.T.;
RT   "ATOL: Assembling a taxonomically balanced genome-scale reconstruction
RT   of the evolutionary history of the Enterobacteriaceae.";
RL   Submitted (MAY-2014) 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:KFD18625.1}.
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DR   EMBL; JMPR01000037; KFD18625.1; -; Genomic_DNA.
DR   STRING; 1005995.GTPT_2386; -.
DR   EnsemblBacteria; KFD18625; KFD18625; GTPT_2386.
DR   UniPathway; UPA00053; UER00084.
DR   Proteomes; UP000028602; 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   Coiled coil {ECO:0000256|SAM:Coils};
KW   Complete proteome {ECO:0000313|Proteomes:UP000028602};
KW   Reference proteome {ECO:0000313|Proteomes:UP000028602};
KW   Transferase {ECO:0000256|PIRNR:PIRNR001361,
KW   ECO:0000256|SAAS:SAAS00080156, ECO:0000313|EMBL:KFD18625.1}.
FT   DOMAIN       58    351       DAHP_synth_1. {ECO:0000259|Pfam:PF00793}.
FT   COILED      285    305       {ECO:0000256|SAM:Coils}.
SQ   SEQUENCE   361 AA;  40140 MW;  6B8DD8571276B6FA CRC64;
     MPAFSGKQHD FETIMNKTDE LRTSPVARLV TPEQLARQYP VSEDISANIL ATRQRISQIL
     QHPTPRLLVV IGPCSLHDPQ SAFDYAQRLN LLRERYQGPL EIVMRTYFEK PRTVTGWKGL
     INDPWLDGSY HINEGLAIAR KLLLDINALG MPTATEFLDR VTGQFIADLI SWGAIGARTT
     ESQVHREMAS ALSCPVGFKN GTDGNIRIAI DAIRAARASH RFLSPDKQGQ MTIYQTRGNP
     DGHIILRGGR TPNYSAEHVA ESRNLLEASR LPARLVIDFS HGNCLKQHQR QLQVAQDVAR
     QLRNGETAIA GVMIESFLEE GRQDMTPGQP LVYGQSITDP CLSWGDTEKV LENLAEAVSA
     L
//
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