GenomeNet

Database: UniProt
Entry: G5Q6D3_SALMO
LinkDB: G5Q6D3_SALMO
Original site: G5Q6D3_SALMO 
ID   G5Q6D3_SALMO            Unreviewed;       356 AA.
AC   G5Q6D3;
DT   25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT   25-JAN-2012, sequence version 1.
DT   24-JAN-2024, entry version 45.
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=LTSEMON_3809 {ECO:0000313|EMBL:EHC76229.1};
OS   Salmonella enterica subsp. enterica serovar Montevideo str. S5-403.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=913242 {ECO:0000313|EMBL:EHC76229.1, ECO:0000313|Proteomes:UP000003221};
RN   [1] {ECO:0000313|EMBL:EHC76229.1, ECO:0000313|Proteomes:UP000003221}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=S5-403 {ECO:0000313|EMBL:EHC76229.1,
RC   ECO:0000313|Proteomes:UP000003221};
RX   PubMed=21859443; DOI=10.1186/1471-2164-12-425;
RA   den Bakker H.C., Moreno Switt A.I., Govoni G., Cummings C.A., Ranieri M.L.,
RA   Degoricija L., Hoelzer K., Rodriguez-Rivera L.D., Brown S., Bolchacova E.,
RA   Furtado M.R., Wiedmann M.;
RT   "Genome sequencing reveals diversification of virulence factor content and
RT   possible host adaptation in distinct subpopulations of Salmonella
RT   enterica.";
RL   BMC Genomics 12:425-425(2011).
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|ARBA:ARBA00003726,
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; EC=2.5.1.54;
CC         Evidence={ECO:0000256|ARBA:ARBA00001370,
CC         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|ARBA:ARBA00004688, ECO:0000256|PIRNR:PIRNR001361}.
CC   -!- SIMILARITY: Belongs to the class-I DAHP synthase family.
CC       {ECO:0000256|ARBA:ARBA00007985, 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:EHC76229.1}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AFCS01000891; EHC76229.1; -; Genomic_DNA.
DR   AlphaFoldDB; G5Q6D3; -.
DR   SMR; G5Q6D3; -.
DR   PATRIC; fig|913242.3.peg.3279; -.
DR   UniPathway; UPA00053; UER00084.
DR   Proteomes; UP000003221; Unassembled WGS sequence.
DR   GO; GO:0003849; F:3-deoxy-7-phosphoheptulonate synthase activity; IEA:UniProtKB-EC.
DR   GO; GO:0008652; P:amino acid biosynthetic process; IEA:UniProtKB-KW.
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; Aldolase class I; 1.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR006218; DAHP1/KDSA.
DR   InterPro; IPR006219; DAHP_synth_1.
DR   NCBIfam; TIGR00034; aroFGH; 1.
DR   PANTHER; PTHR21225; PHOSPHO-2-DEHYDRO-3-DEOXYHEPTONATE ALDOLASE DAHP SYNTHETASE; 1.
DR   PANTHER; PTHR21225:SF10; PHOSPHO-2-DEHYDRO-3-DEOXYHEPTONATE ALDOLASE, TYR-SENSITIVE; 1.
DR   Pfam; PF00793; DAHP_synth_1; 1.
DR   PIRSF; PIRSF001361; DAHP_synthase; 1.
DR   SUPFAM; SSF51569; Aldolase; 1.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis {ECO:0000256|PIRNR:PIRNR001361};
KW   Aromatic amino acid biosynthesis {ECO:0000256|PIRNR:PIRNR001361};
KW   Transferase {ECO:0000256|PIRNR:PIRNR001361}.
FT   DOMAIN          41..340
FT                   /note="DAHP synthetase I/KDSA"
FT                   /evidence="ECO:0000259|Pfam:PF00793"
SQ   SEQUENCE   356 AA;  38713 MW;  51EC218FC47B30A4 CRC64;
     MQKDALNNVR ITDEQVLMTP EQLKAAFPLS LAQEAQIAQS RGIISDIIAG RDPRLLVVCG
     PCSIHDPETA LEYARRFKAL AAEVSDSLYL VMRVYFEKPR TTVGWKGLIN DPHMDGSFDV
     EAGLKIARQL LVELVNMGLP LATEALDPNS PQYLGDLFSW SAIGARTTES QTHREMASGL
     SMPVGFKNGT DGSLATAINA MRAAAQPHRF VGINQAGQVA LLQTQGNPHG HVILRGGKAP
     NYSPADVAQC EKEMEQAGLR PSLMVDCSHG NSNKDYRRQP AVAESVVAQI KDGNRSIIGL
     MIESNIHEGN QSSEQPRSEM KYGVSVTDAC ISWEMTDALL REIHKDLSGQ LAVRVA
//
DBGET integrated database retrieval system