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Database: UniProt
Entry: A0A1F4KF05_9BURK
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ID   A0A1F4KF05_9BURK        Unreviewed;       379 AA.
AC   A0A1F4KF05;
DT   15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT   15-FEB-2017, sequence version 1.
DT   31-JUL-2019, entry version 10.
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=A3F78_16370 {ECO:0000313|EMBL:OGB33270.1};
OS   Burkholderiales bacterium RIFCSPLOWO2_12_FULL_61_40.
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales.
OX   NCBI_TaxID=1797566 {ECO:0000313|EMBL:OGB33270.1, ECO:0000313|Proteomes:UP000178940};
RN   [1] {ECO:0000313|EMBL:OGB33270.1, ECO:0000313|Proteomes:UP000178940}
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:OGB33270.1}.
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DR   EMBL; MESI01000035; OGB33270.1; -; Genomic_DNA.
DR   UniPathway; UPA00053; UER00084.
DR   Proteomes; UP000178940; 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:UP000178940};
KW   Transferase {ECO:0000256|PIRNR:PIRNR001361,
KW   ECO:0000256|SAAS:SAAS00080156}.
FT   DOMAIN       66    363       DAHP_synth_1. {ECO:0000259|Pfam:PF00793}.
FT   REGION        1     31       Disordered. {ECO:0000256|SAM:MobiDB-
FT                                lite}.
SQ   SEQUENCE   379 AA;  41006 MW;  AF55736ABB142DF5 CRC64;
     MNAKATVAGS AAWAANPASH PSDRTSQTDD ERIKDITVLP PPEHLIRFFP IRGTAMESLI
     STTRRNIHQI MAGKDDRLLV VIGPCSIHDP AAALDYARQL LAQREKFADT LEIVMRVYFE
     KPRTTVGWKG LINDPYLDET FRIDEGLRIA RQLLIEINRL GLPAGSEFLD VISPQYLGDL
     ISWGAIGART TESQVHRELA SGLSAPIGFK NGTDGNIKIA TDAIQAAAGG HHFLSVHKNG
     QVAIVQTNGN PDCHVILRGG KAPNYDAASV ASACKDLEKA KLPATLMVDC SHANSSKQHE
     KQLEVARDIA QQMSSGSRSV FGVMVESHLN AGAQKFTPGK DDAAQLEYGK SITDACLGWD
     DSLQSLEVLS AAVKARRAR
//
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