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Database: UniProt
Entry: H5WT96_9BURK
LinkDB: H5WT96_9BURK
Original site: H5WT96_9BURK 
ID   H5WT96_9BURK            Unreviewed;       377 AA.
AC   H5WT96;
DT   18-APR-2012, integrated into UniProtKB/TrEMBL.
DT   18-APR-2012, sequence version 1.
DT   31-JUL-2019, entry version 33.
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=BurJ1DRAFT_0070 {ECO:0000313|EMBL:EHR68969.1};
OS   Burkholderiales bacterium JOSHI_001.
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales.
OX   NCBI_TaxID=864051 {ECO:0000313|EMBL:EHR68969.1, ECO:0000313|Proteomes:UP000004674};
RN   [1] {ECO:0000313|EMBL:EHR68969.1, ECO:0000313|Proteomes:UP000004674}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JOSHI_001 {ECO:0000313|EMBL:EHR68969.1,
RC   ECO:0000313|Proteomes:UP000004674};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA   Peters L., Mikhailova N., Zeytun A., Lu M., Detter J.C., Han C.,
RA   Tapia R., Land M., Hauser L., Kyrpides N., Ivanova N., Pagani I.,
RA   Smith J., Lewis G., Woyke T.;
RT   "Noncontiguous Finished sequence of Burkholderiales bacterium
RT   JOSHI_001.";
RL   Submitted (NOV-2011) 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}.
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DR   EMBL; CM001438; EHR68969.1; -; Genomic_DNA.
DR   RefSeq; WP_009548115.1; NZ_CM001438.1.
DR   STRING; 864051.BurJ1DRAFT_0070; -.
DR   EnsemblBacteria; EHR68969; EHR68969; BurJ1DRAFT_0070.
DR   OrthoDB; 853329at2; -.
DR   BioCyc; BBAC864051:G1H30-69-MONOMER; -.
DR   UniPathway; UPA00053; UER00084.
DR   Proteomes; UP000004674; Chromosome.
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:UP000004674};
KW   Reference proteome {ECO:0000313|Proteomes:UP000004674};
KW   Transferase {ECO:0000256|PIRNR:PIRNR001361,
KW   ECO:0000256|SAAS:SAAS00080156}.
FT   DOMAIN       66    362       DAHP_synth_1. {ECO:0000259|Pfam:PF00793}.
FT   REGION        1     31       Disordered. {ECO:0000256|SAM:MobiDB-
FT                                lite}.
FT   COMPBIAS      1     24       Polar. {ECO:0000256|SAM:MobiDB-lite}.
SQ   SEQUENCE   377 AA;  40784 MW;  AFAA7D599F58A24F CRC64;
     MAPKSTGPSS TEGGYGYALS EKTSQTDDQR IKDVTPLPPP EHLIRFFPIA GTKTEALIGH
     TRDAVRQIMA RQDDRLLVVV GPCSIHDPAA AVDYAKRLMT QREKYAGTLE IVMRVYFEKP
     RTTVGWKGLI NDPYLDESYR IHEGLRIARQ LLVEINRLGM PAGSEFLDVI SPQYIGDLIS
     WGAIGARTTE SQVHRELASG LSAPIGFKNG TDGNLKIAID AIQAASRPHH FMSVHKNGQV
     AIVETKGNPD CHVILRGGKA PNYDGASVAA ACKEIEAAKL ACNLMVDASH ANSSKQHERQ
     LEVLKDVGAQ MAAGNRCIFG VMIESHLEAG AQKFSAGKDD PAKLVYGQSI TDACIGWDHT
     LQALAGLDAA VKARRQA
//
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