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Database: UniProt
Entry: A0A1F4H2M3_9BURK
LinkDB: A0A1F4H2M3_9BURK
Original site: A0A1F4H2M3_9BURK 
ID   A0A1F4H2M3_9BURK        Unreviewed;       368 AA.
AC   A0A1F4H2M3;
DT   15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT   15-FEB-2017, sequence version 1.
DT   08-MAY-2019, entry version 8.
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=A2X72_17490 {ECO:0000313|EMBL:OGA92212.1};
OS   Burkholderiales bacterium GWF1_66_17.
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales.
OX   NCBI_TaxID=1797551 {ECO:0000313|EMBL:OGA92212.1, ECO:0000313|Proteomes:UP000178834};
RN   [1] {ECO:0000313|EMBL:OGA92212.1, ECO:0000313|Proteomes:UP000178834}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=27774985; DOI=10.1038/ncomms13219;
RA   Anantharaman K., Brown C.T., Hug L.A., Sharon I., Castelle C.J.,
RA   Probst A.J., Thomas B.C., Singh A., Wilkins M.J., Karaoz U.,
RA   Brodie E.L., Williams K.H., Hubbard S.S., Banfield J.F.;
RT   "Thousands of microbial genomes shed light on interconnected
RT   biogeochemical processes in an aquifer system.";
RL   Nat. Commun. 7:13219-13219(2016).
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:OGA92212.1}.
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DR   EMBL; MERT01000009; OGA92212.1; -; Genomic_DNA.
DR   UniPathway; UPA00053; UER00084.
DR   Proteomes; UP000178834; 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:UP000178834};
KW   Transferase {ECO:0000256|PIRNR:PIRNR001361,
KW   ECO:0000256|SAAS:SAAS00080156}.
FT   DOMAIN       58    350       DAHP_synth_1. {ECO:0000259|Pfam:PF00793}.
SQ   SEQUENCE   368 AA;  39594 MW;  0E2562484081C8EB CRC64;
     MTHAHRTATP LSTQDTTRID DLRIGAVRPL ITPALLQEWL PTPPEALALV ESSRAALSRV
     LHGQDDRLIV VVGPCSIHDH GQAMEYARLL KEQVDALNDD LLIVMRVYFE KPRTTVGWKG
     YINDPHLDGS FAINEGLELA RQLLLDVLAL GLPVGTEFLD LLSPQFISDL VSWGAIGART
     TESQSHRQLA SGLSCPVGFK NGTDGGIKVA SDAIQAAQAS HAFMGMTKMG QAAIFETRGN
     ADCHVILRGG KATNYSAADV DAACALLKTA GLREQVMIDV SHANSSKQHR RQIDVSADVA
     QQIAAGDARI TGVMIESHLN EGRQDIVPGQ PLQHGVSVTD ACISFEQTVP VLQGLAEAVR
     ARRSKTSR
//
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