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Database: UniProt
Entry: W1ISX9_9GAMM
LinkDB: W1ISX9_9GAMM
Original site: W1ISX9_9GAMM 
ID   W1ISX9_9GAMM            Unreviewed;       374 AA.
AC   W1ISX9;
DT   19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT   19-MAR-2014, sequence version 1.
DT   08-MAY-2019, entry version 21.
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=aroF {ECO:0000313|EMBL:CDL81539.1};
GN   ORFNames=XSR1_140015 {ECO:0000313|EMBL:CDL81539.1};
OS   Xenorhabdus szentirmaii DSM 16338.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Morganellaceae; Xenorhabdus.
OX   NCBI_TaxID=1427518 {ECO:0000313|EMBL:CDL81539.1, ECO:0000313|Proteomes:UP000019202};
RN   [1] {ECO:0000313|EMBL:CDL81539.1, ECO:0000313|Proteomes:UP000019202}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 16338 {ECO:0000313|EMBL:CDL81539.1,
RC   ECO:0000313|Proteomes:UP000019202};
RA   Gualtieri M., Ogier J.C., Pages S., Givaudan A., Gaudriault S.;
RT   "Draft genome sequence and annotation of the entomopathogenic
RT   bacteria, Xenorhabdus cabanillasi strain JM26 and Xenorhabdus
RT   szentirmai strain DSM 16338.";
RL   Submitted (NOV-2013) 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}.
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:CDL81539.1}.
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DR   EMBL; CBXF010000046; CDL81539.1; -; Genomic_DNA.
DR   EnsemblBacteria; CDL81539; CDL81539; XSR1_140015.
DR   UniPathway; UPA00053; UER00084.
DR   Proteomes; UP000019202; 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:UP000019202};
KW   Reference proteome {ECO:0000313|Proteomes:UP000019202};
KW   Transferase {ECO:0000256|PIRNR:PIRNR001361,
KW   ECO:0000256|SAAS:SAAS00080156, ECO:0000313|EMBL:CDL81539.1}.
FT   DOMAIN       53    352       DAHP_synth_1. {ECO:0000259|Pfam:PF00793}.
SQ   SEQUENCE   374 AA;  41136 MW;  51869E9BD216C235 CRC64;
     MKQAEKAGRG MIMQKDAINN VHILDEQVLI TPEELKEKYP LSNNDLHFIT NARNTIADII
     QHRDPRLLVV CGPCSIHDVD AALDYARRLK TLSGELSDCL YIVMRVYFEK PRTTVGWKGL
     ISDPYMDGSF DMGAGLHIAR GLLLNLVEMG LPLANEALDP NNPQYLGDLF SWSAIGARTT
     ESQTHREMAS GLSVSVGFKN GTDGNLNTAI NAMKAAAMPH RFMGINQSGQ VCLLQTQGNP
     NGHVILRGGA TPNYSAEHVE DCERQMIKAG LIPSLMIDCS HGNSNKDFRR QSVVVDSVAE
     QIMAGNQSII GIMLESHINE GNQSSEQSRS EMKYGVSVTD ACINWQTTEQ VLRKLHQQIA
     PHLANKNVVM EKAG
//
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