ID C5T7L6_ACIDE Unreviewed; 373 AA.
AC C5T7L6;
DT 01-SEP-2009, integrated into UniProtKB/TrEMBL.
DT 01-SEP-2009, sequence version 1.
DT 11-DEC-2019, entry version 43.
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=AcdelDRAFT_2896 {ECO:0000313|EMBL:EER59523.1};
OS Acidovorax delafieldii 2AN.
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Acidovorax.
OX NCBI_TaxID=573060 {ECO:0000313|EMBL:EER59523.1, ECO:0000313|Proteomes:UP000003856};
RN [1] {ECO:0000313|EMBL:EER59523.1, ECO:0000313|Proteomes:UP000003856}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=2AN {ECO:0000313|EMBL:EER59523.1,
RC ECO:0000313|Proteomes:UP000003856};
RG US DOE Joint Genome Institute (JGI-PGF);
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Tice H., Bruce D.,
RA Goodwin L., Pitluck S., Larimer F., Land M.L., Hauser L., Shelobolina E.S.,
RA Picardal F., Roden E., Emerson D.;
RT "The draft genome of Acidovorax delafieldii 2AN.";
RL Submitted (MAY-2009) 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:EER59523.1}.
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DR EMBL; ACQT01000118; EER59523.1; -; Genomic_DNA.
DR RefSeq; WP_005797860.1; NZ_ACQT01000118.1.
DR EnsemblBacteria; EER59523; EER59523; AcdelDRAFT_2896.
DR PATRIC; fig|573060.9.peg.2149; -.
DR BioCyc; ADEL573060:G10BO-2939-MONOMER; -.
DR UniPathway; UPA00053; UER00084.
DR Proteomes; UP000003856; 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:UP000003856};
KW Transferase {ECO:0000256|PIRNR:PIRNR001361, ECO:0000256|SAAS:SAAS00080156,
KW ECO:0000313|EMBL:EER59523.1}.
FT DOMAIN 60..356
FT /note="DAHP_synth_1"
FT /evidence="ECO:0000259|Pfam:PF00793"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 373 AA; 40528 MW; B0533A480FFCB576 CRC64;
MTAHATPASD AWYRSVEKTS QTDDERIKDI TVLPPPEHLI RFFPISGTPV EALITQTRKN
IHNIMAGKDD RLLVVIGPCS IHDPAAALEY ARRLAAVRAQ YADTLEIVMR VYFEKPRTTV
GWKGLINDPY LDESYRIDEG LRIARQLLIE INRLGIPAGS EFLDVISPQY IGDLISWGAI
GARTTESQVH RELASGISAP IGFKNGTDGN IRIATDAIQS ASRGHHFLSV HKNGQVAIVN
TKGNKDCHVI LRGGKTPNYD AASVAAACKD LEAAKLPPTL MVDCSHANSS KQHEKQLDVA
RDIAAQIAGG SRSVFGLMIE SHLHAGAQKF SPGKDQPSAL EYGKSITDAC LGWDDSLRSL
AELSAAVVAR RAR
//
