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Database: UniProt
Entry: A0A011R1U0_9PROT
LinkDB: A0A011R1U0_9PROT
Original site: A0A011R1U0_9PROT 
ID   A0A011R1U0_9PROT        Unreviewed;       359 AA.
AC   A0A011R1U0;
DT   11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT   11-JUN-2014, sequence version 1.
DT   11-DEC-2019, entry version 24.
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=aroG {ECO:0000313|EMBL:EXI85144.1};
GN   ORFNames=AW11_03703 {ECO:0000313|EMBL:EXI85144.1};
OS   Candidatus Accumulibacter sp. BA-93.
OC   Bacteria; Proteobacteria; Betaproteobacteria; Candidatus Accumulibacter;
OC   unclassified Candidatus Accumulibacter.
OX   NCBI_TaxID=1454004 {ECO:0000313|EMBL:EXI85144.1, ECO:0000313|Proteomes:UP000022141};
RN   [1] {ECO:0000313|EMBL:EXI85144.1, ECO:0000313|Proteomes:UP000022141}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BA-93 {ECO:0000313|Proteomes:UP000022141};
RA   Skennerton C.T., Barr J.J., Slater F.R., Bond P.L., Tyson G.W.;
RT   "Expanding our view of genomic diversity in Candidatus Accumulibacter
RT   clades.";
RL   Submitted (FEB-2014) 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|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|PIRNR:PIRNR001361};
CC   -!- PATHWAY: Metabolic intermediate biosynthesis; chorismate biosynthesis;
CC       chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step
CC       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 EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EXI85144.1}.
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DR   EMBL; JEMY01000059; EXI85144.1; -; Genomic_DNA.
DR   STRING; 1454004.AW11_03703; -.
DR   PATRIC; fig|1454004.3.peg.3810; -.
DR   UniPathway; UPA00053; UER00084.
DR   Proteomes; UP000022141; 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   Reference proteome {ECO:0000313|Proteomes:UP000022141};
KW   Transferase {ECO:0000256|PIRNR:PIRNR001361, ECO:0000256|SAAS:SAAS00080156,
KW   ECO:0000313|EMBL:EXI85144.1}.
FT   DOMAIN          44..341
FT                   /note="DAHP_synth_1"
FT                   /evidence="ECO:0000259|Pfam:PF00793"
SQ   SEQUENCE   359 AA;  39351 MW;  D7BCCF8896CFC124 CRC64;
     MTLQSKPNTD DVRIREIKEL VPPAHVFREF PVGVRAAMTT FEARQNIHRI LHGADNRLLV
     VIGPCSIHDV DSAIEYATRL QKEVPRFADD LLIAMRVYFE KPRTTVGWKG LINDPRLDNS
     FRINEGLRLA RGLLLQINDM GLPCATEFLD TITPQYTADL IAWGAIGART TESQVHRELA
     SGLSCPVGFK NGTDGNIRIA IDAIRAAQSP HHFLSVTKAG HSAIVSTAGN EDCHVILRGG
     QEPNHDAAHV DAACKQIAAA GLAARLMIDA SHANSNKRFK QQIEVARDTA SQVTAGDERI
     IGVMIESHLV EGRQDLVPGQ QLEYGKSVTD ACLGWEDSLL VLEVLAKSVR DRRLVEAAE
//
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