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Database: UniProt
Entry: AROH_SHIFL
LinkDB: AROH_SHIFL
Original site: AROH_SHIFL 
ID   AROH_SHIFL              Reviewed;         348 AA.
AC   P59736;
DT   20-JUN-2003, integrated into UniProtKB/Swiss-Prot.
DT   20-JUN-2003, sequence version 1.
DT   18-SEP-2019, entry version 106.
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=SF1526, S1644;
OS   Shigella flexneri.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Shigella.
OX   NCBI_TaxID=623;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=301 / Serotype 2a;
RX   PubMed=12384590; DOI=10.1093/nar/gkf566;
RA   Jin Q., Yuan Z., Xu J., Wang Y., Shen Y., Lu W., Wang J., Liu H.,
RA   Yang J., Yang F., Zhang X., Zhang J., Yang G., Wu H., Qu D., Dong J.,
RA   Sun L., Xue Y., Zhao A., Gao Y., Zhu J., Kan B., Ding K., Chen S.,
RA   Cheng H., Yao Z., He B., Chen R., Ma D., Qiang B., Wen Y., Hou Y.,
RA   Yu J.;
RT   "Genome sequence of Shigella flexneri 2a: insights into pathogenicity
RT   through comparison with genomes of Escherichia coli K12 and O157.";
RL   Nucleic Acids Res. 30:4432-4441(2002).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700930 / 2457T / Serotype 2a;
RX   PubMed=12704152; DOI=10.1128/iai.71.5.2775-2786.2003;
RA   Wei J., Goldberg M.B., Burland V., Venkatesan M.M., Deng W.,
RA   Fournier G., Mayhew G.F., Plunkett G. III, Rose D.J., Darling A.,
RA   Mau B., Perna N.T., Payne S.M., Runyen-Janecky L.J., Zhou S.,
RA   Schwartz D.C., Blattner F.R.;
RT   "Complete genome sequence and comparative genomics of Shigella
RT   flexneri serotype 2a strain 2457T.";
RL   Infect. Immun. 71:2775-2786(2003).
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). {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;
CC         EC=2.5.1.54;
CC   -!- PATHWAY: Metabolic intermediate biosynthesis; chorismate
CC       biosynthesis; chorismate from D-erythrose 4-phosphate and
CC       phosphoenolpyruvate: step 1/7.
CC   -!- SIMILARITY: Belongs to the class-I DAHP synthase family.
CC       {ECO:0000305}.
DR   EMBL; AE005674; AAN43116.1; -; Genomic_DNA.
DR   EMBL; AE014073; AAP17007.1; -; Genomic_DNA.
DR   RefSeq; NP_707409.1; NC_004337.2.
DR   RefSeq; WP_001082230.1; NZ_UIQL01000059.1.
DR   SMR; P59736; -.
DR   EnsemblBacteria; AAN43116; AAN43116; SF1526.
DR   EnsemblBacteria; AAP17007; AAP17007; S1644.
DR   GeneID; 1024719; -.
DR   KEGG; sfl:SF1526; -.
DR   KEGG; sfx:S1644; -.
DR   PATRIC; fig|198214.7.peg.1802; -.
DR   eggNOG; ENOG4105E99; Bacteria.
DR   eggNOG; COG0722; LUCA.
DR   HOGENOM; HOG000220501; -.
DR   KO; K01626; -.
DR   OMA; PCLSWED; -.
DR   OrthoDB; 853329at2; -.
DR   UniPathway; UPA00053; UER00084.
DR   Proteomes; UP000001006; Chromosome.
DR   Proteomes; UP000002673; 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; Aromatic amino acid biosynthesis;
KW   Complete proteome; Reference proteome; Transferase.
FT   CHAIN         1    348       Phospho-2-dehydro-3-deoxyheptonate
FT                                aldolase, Trp-sensitive.
FT                                /FTId=PRO_0000140846.
SQ   SEQUENCE   348 AA;  38823 MW;  02C7DC9F85B23D8B CRC64;
     MNRTDELRTA RIESLVTPAE LALRYPVTPG VATHVTDSRR RIEKILNGED KRLLVIIGPC
     SIHDLTAAME YATRLQSLRN QYQSRLEIVM RTYFEKPRTV VGWKGLISDP DLNGSYRVNH
     GLELARKLLL QVNELGVPTA TEFLDMVTGQ FIADLISWGA IGARTTESQI HREMASALSC
     PVGFKNGTDG NTRIAVDAIR AARASHMFLS PDKNGQMTIY QTSGNPYGHI IMRGGKKPNY
     HADDIAAACD TLHEFDLPEH LVVDFSHGNC QKQHRRQLEV CEDICQQIRN GSTEIAGIMA
     ESFLREGTQK IVGGQPLTYG QSITDPCLGW EDTERLVEKL AFAVDTRF
//
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