AROH_SALTY
ID AROH_SALTY Reviewed; 348 AA.
AC Q8ZPS4;
DT 20-JUN-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 97.
DE RecName: Full=Phospho-2-dehydro-3-deoxyheptonate aldolase, Trp-sensitive;
DE EC=2.5.1.54;
DE AltName: Full=3-deoxy-D-arabino-heptulosonate 7-phosphate synthase;
DE AltName: Full=DAHP synthase;
DE AltName: Full=Phospho-2-keto-3-deoxyheptonate aldolase;
GN Name=aroH; OrderedLocusNames=STM1347;
OS Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=99287;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX PubMed=11677609; DOI=10.1038/35101614;
RA McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P.,
RA Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D.,
RA Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E.,
RA Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R.,
RA Wilson R.K.;
RT "Complete genome sequence of Salmonella enterica serovar Typhimurium LT2.";
RL Nature 413:852-856(2001).
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:0000250}.
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 -!- PATHWAY: Metabolic intermediate biosynthesis; chorismate biosynthesis;
CC chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step
CC 1/7.
CC -!- SIMILARITY: Belongs to the class-I DAHP synthase family. {ECO:0000305}.
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DR EMBL; AE006468; AAL20272.1; -; Genomic_DNA.
DR RefSeq; NP_460313.1; NC_003197.2.
DR RefSeq; WP_001082196.1; NC_003197.2.
DR AlphaFoldDB; Q8ZPS4; -.
DR SMR; Q8ZPS4; -.
DR STRING; 99287.STM1347; -.
DR PaxDb; Q8ZPS4; -.
DR EnsemblBacteria; AAL20272; AAL20272; STM1347.
DR GeneID; 1252865; -.
DR KEGG; stm:STM1347; -.
DR PATRIC; fig|99287.12.peg.1430; -.
DR HOGENOM; CLU_030903_0_1_6; -.
DR OMA; PCLSWED; -.
DR PhylomeDB; Q8ZPS4; -.
DR BioCyc; SENT99287:STM1347-MON; -.
DR UniPathway; UPA00053; UER00084.
DR Proteomes; UP000001014; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0003849; F:3-deoxy-7-phosphoheptulonate synthase activity; IBA:GO_Central.
DR GO; GO:0009073; P:aromatic amino acid family biosynthetic process; IBA:GO_Central.
DR GO; GO:0008652; P:cellular amino acid 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; Aromatic amino acid biosynthesis;
KW Reference proteome; Transferase.
FT CHAIN 1..348
FT /note="Phospho-2-dehydro-3-deoxyheptonate aldolase, Trp-
FT sensitive"
FT /id="PRO_0000140845"
SQ SEQUENCE 348 AA; 38750 MW; 7A9830B929B4C576 CRC64;
MNRTDELRTA RIDSLVTPTE LAQRYPVSSS VASHVTDSRR RIEKILNGED PRLLVVIGPC
SIHDLNAAME YATQLQAQRQ KHQARLEIVM RTYFEKPRTV VGWKGLISDP DLNGSYRVNY
GLELARRLLL QVNELGVPTA TEFLDMVTGQ FIADLISWGA IGARTTESQI HREMASALSC
PVGFKNGTDG NTRIAVDAIR ASRASHMFLS PDKDGQMTIY QTSGNPYGHI IMRGGKKPNY
HAEDIAAACD TLHEFDLPEH LVVDFSHGNC QKQHRRQLEV CDDICQQIRN GSTAIAGIMA
ESFLREGTQK IISGQPLIYG QSITDPCLNW EDTEVLLEKL AAAVDSRF