AROH_ECOLI
ID AROH_ECOLI Reviewed; 348 AA.
AC P00887; P78301;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 20-JUN-2003, sequence version 4.
DT 03-AUG-2022, entry version 162.
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=b1704, JW1694;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1677907; DOI=10.1016/0378-1119(91)90544-l;
RA Hudson G.S., Rellos P., Davidson B.E.;
RT "Two promoters control the aroH gene of Escherichia coli.";
RL Gene 102:87-91(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2903857; DOI=10.1128/jb.170.12.5500-5506.1988;
RA Ray J.M., Yanofsky C., Bauerle R.;
RT "Mutational analysis of the catalytic and feedback sites of the tryptophan-
RT sensitive 3-deoxy-D-arabino-heptulosonate-7-phosphate synthase of
RT Escherichia coli.";
RL J. Bacteriol. 170:5500-5506(1988).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=9097039; DOI=10.1093/dnares/3.6.363;
RA Aiba H., Baba T., Fujita K., Hayashi K., Inada T., Isono K., Itoh T.,
RA Kasai H., Kashimoto K., Kimura S., Kitakawa M., Kitagawa M., Makino K.,
RA Miki T., Mizobuchi K., Mori H., Mori T., Motomura K., Nakade S.,
RA Nakamura Y., Nashimoto H., Nishio Y., Oshima T., Saito N., Sampei G.,
RA Seki Y., Sivasundaram S., Tagami H., Takeda J., Takemoto K., Takeuchi Y.,
RA Wada C., Yamamoto Y., Horiuchi T.;
RT "A 570-kb DNA sequence of the Escherichia coli K-12 genome corresponding to
RT the 28.0-40.1 min region on the linkage map.";
RL DNA Res. 3:363-377(1996).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-36 AND 232-348.
RX PubMed=6167722; DOI=10.1016/0022-2836(81)90334-x;
RA Zurawski G., Gunsalus R.P., Brown K.D., Yanofsky C.;
RT "Structure and regulation of aroH, the structural gene for the tryptophan-
RT repressible 3-deoxy-D-arabino-heptulosonic acid-7-phosphate synthetase of
RT Escherichia coli.";
RL J. Mol. Biol. 145:47-73(1981).
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).
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 -!- INTERACTION:
CC P00887; P0A6F5: groEL; NbExp=3; IntAct=EBI-1125143, EBI-543750;
CC -!- MISCELLANEOUS: There are 3 DAHP synthases, AroH is feedback-inhibited
CC by Trp. The other 2 DAHP synthases are Tyr- and Phe-sensitive,
CC respectively.
CC -!- SIMILARITY: Belongs to the class-I DAHP synthase family. {ECO:0000305}.
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; M38266; AAA23497.1; -; Genomic_DNA.
DR EMBL; J04221; AAA23493.1; -; Genomic_DNA.
DR EMBL; U00096; AAC74774.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA15473.1; -; Genomic_DNA.
DR EMBL; V00261; CAA23510.1; -; Genomic_DNA.
DR EMBL; X04373; CAA27956.1; -; Genomic_DNA.
DR PIR; H64928; ADECH.
DR RefSeq; NP_416219.1; NC_000913.3.
DR RefSeq; WP_001082229.1; NZ_SSZK01000001.1.
DR AlphaFoldDB; P00887; -.
DR SMR; P00887; -.
DR BioGRID; 4260296; 11.
DR BioGRID; 850589; 1.
DR DIP; DIP-6846N; -.
DR IntAct; P00887; 5.
DR STRING; 511145.b1704; -.
DR jPOST; P00887; -.
DR PaxDb; P00887; -.
DR PRIDE; P00887; -.
DR EnsemblBacteria; AAC74774; AAC74774; b1704.
DR EnsemblBacteria; BAA15473; BAA15473; BAA15473.
DR GeneID; 66674402; -.
DR GeneID; 946229; -.
DR KEGG; ecj:JW1694; -.
DR KEGG; eco:b1704; -.
DR PATRIC; fig|1411691.4.peg.553; -.
DR EchoBASE; EB0078; -.
DR eggNOG; COG0722; Bacteria.
DR HOGENOM; CLU_030903_0_1_6; -.
DR InParanoid; P00887; -.
DR OMA; PCLSWED; -.
DR PhylomeDB; P00887; -.
DR BioCyc; EcoCyc:AROH-MON; -.
DR BioCyc; MetaCyc:AROH-MON; -.
DR UniPathway; UPA00053; UER00084.
DR PRO; PR:P00887; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IDA:EcoliWiki.
DR GO; GO:0003849; F:3-deoxy-7-phosphoheptulonate synthase activity; IDA:EcoliWiki.
DR GO; GO:0042802; F:identical protein binding; IDA:EcoCyc.
DR GO; GO:0009073; P:aromatic amino acid family biosynthetic process; IDA:EcoliWiki.
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 1: Evidence at protein level;
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_0000140840"
FT CONFLICT 203..205
FT /note="RAS -> AQ (in Ref. 2; AAA23493)"
FT /evidence="ECO:0000305"
FT CONFLICT 333..334
FT /note="TE -> RQ (in Ref. 2; AAA23493 and 6; CAA27956)"
FT /evidence="ECO:0000305"
FT CONFLICT 333
FT /note="T -> S (in Ref. 1; AAA23497)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 348 AA; 38735 MW; 52C3C482447226E0 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 GSTAIAGIMA
ESFLREGTQK IVGSQPLTYG QSITDPCLGW EDTERLVEKL ASAVDTRF
