AROF_ECOLI
ID AROF_ECOLI Reviewed; 356 AA.
AC P00888; Q47061;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 13-AUG-1987, sequence version 1.
DT 03-AUG-2022, entry version 174.
DE RecName: Full=Phospho-2-dehydro-3-deoxyheptonate aldolase, Tyr-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=aroF; OrderedLocusNames=b2601, JW2582;
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=6146618; DOI=10.1016/s0021-9258(17)42751-7;
RA Shultz J., Hermodson M.A., Garner C.C., Herrmann K.M.;
RT "The nucleotide sequence of the aroF gene of Escherichia coli and the amino
RT acid sequence of the encoded protein, the tyrosine-sensitive 3-deoxy-D-
RT arabino-heptulosonate 7-phosphate synthase.";
RL J. Biol. Chem. 259:9655-9661(1984).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=6396419; DOI=10.1016/0022-2836(84)90269-9;
RA Hudson G.S., Davidson B.E.;
RT "Nucleotide sequence and transcription of the phenylalanine and tyrosine
RT operons of Escherichia coli K12.";
RL J. Mol. Biol. 180:1023-1051(1984).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=9205837; DOI=10.1093/dnares/4.2.91;
RA Yamamoto Y., Aiba H., Baba T., Hayashi K., Inada T., Isono K., Itoh T.,
RA Kimura S., Kitagawa M., Makino K., Miki T., Mitsuhashi N., Mizobuchi K.,
RA Mori H., Nakade S., Nakamura Y., Nashimoto H., Oshima T., Oyama S.,
RA Saito N., Sampei G., Satoh Y., Sivasundaram S., Tagami H., Takahashi H.,
RA Takeda J., Takemoto K., Uehara K., Wada C., Yamagata S., Horiuchi T.;
RT "Construction of a contiguous 874-kb sequence of the Escherichia coli-K12
RT genome corresponding to 50.0-68.8 min on the linkage map and analysis of
RT its sequence features.";
RL DNA Res. 4:91-113(1997).
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 124-187.
RX PubMed=1977738; DOI=10.1128/jb.172.11.6581-6584.1990;
RA Weaver L.M., Herrmann K.M.;
RT "Cloning of an aroF allele encoding a tyrosine-insensitive 3-deoxy-D-
RT arabino-heptulosonate 7-phosphate synthase.";
RL J. Bacteriol. 172:6581-6584(1990).
RN [7]
RP PROTEIN SEQUENCE OF 1-30.
RX PubMed=6104668; DOI=10.1016/s0021-9258(20)79663-8;
RA Herrmann K.M., Shultz J., Hermodson M.A.;
RT "Sequence homology between the tyrosine-sensitive 3-deoxy-D-arabino-
RT heptulosonate 7-phosphate synthase from Escherichia coli and hemerythrin
RT from Sipunculida.";
RL J. Biol. Chem. 255:7079-7081(1980).
RN [8]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-6.
RX PubMed=2857723; DOI=10.1016/s0021-9258(19)83697-9;
RA Garner C.C., Herrmann K.M.;
RT "Operator mutations of the Escherichia coli aroF gene.";
RL J. Biol. Chem. 260:3820-3825(1985).
RN [9]
RP IDENTIFICATION BY 2D-GEL.
RX PubMed=9298644; DOI=10.1002/elps.1150180805;
RA VanBogelen R.A., Abshire K.Z., Moldover B., Olson E.R., Neidhardt F.C.;
RT "Escherichia coli proteome analysis using the gene-protein database.";
RL Electrophoresis 18:1243-1251(1997).
RN [10]
RP CHARACTERIZATION.
RX PubMed=9056491; DOI=10.1006/prep.1996.0690;
RA Ramilo C.A., Evans J.N.;
RT "Overexpression, purification, and characterization of tyrosine-sensitive
RT 3-deoxy-D-arabino-heptulosonic acid 7-phosphate synthase from Escherichia
RT coli.";
RL Protein Expr. Purif. 9:253-261(1997).
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 -!- COFACTOR:
CC Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240;
CC -!- ACTIVITY REGULATION: Specifically feedback inhibited by tyrosine with
CC 50% inhibition observed at 9 microM tyrosine, pH 7.0.
CC -!- PATHWAY: Metabolic intermediate biosynthesis; chorismate biosynthesis;
CC chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step
CC 1/7.
CC -!- MISCELLANEOUS: There are 3 DAHP synthases, AroF is feedback-inhibited
CC by Tyr. The other 2 DAHP synthases are Phe- and Trp-sensitive,
CC respectively.
CC -!- SIMILARITY: Belongs to the class-I DAHP synthase family. {ECO:0000305}.
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DR EMBL; K01989; AAA23489.1; -; Genomic_DNA.
DR EMBL; M10431; AAA24332.1; -; Genomic_DNA.
DR EMBL; U00096; AAC75650.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA16487.1; -; Genomic_DNA.
DR EMBL; M60890; AAA23491.1; -; Genomic_DNA.
DR EMBL; K03453; AAA23490.1; -; Genomic_DNA.
DR PIR; I41141; ADECHY.
DR RefSeq; NP_417092.1; NC_000913.3.
DR RefSeq; WP_001168037.1; NZ_LN832404.1.
DR PDB; 6AGL; X-ray; 2.50 A; A/B=1-356.
DR PDB; 6AGM; X-ray; 2.00 A; A/B/C/D=1-355.
DR PDBsum; 6AGL; -.
DR PDBsum; 6AGM; -.
DR AlphaFoldDB; P00888; -.
DR SMR; P00888; -.
DR BioGRID; 4263470; 22.
DR BioGRID; 851421; 2.
DR DIP; DIP-9154N; -.
DR IntAct; P00888; 3.
DR STRING; 511145.b2601; -.
DR SWISS-2DPAGE; P00888; -.
DR jPOST; P00888; -.
DR PaxDb; P00888; -.
DR PRIDE; P00888; -.
DR EnsemblBacteria; AAC75650; AAC75650; b2601.
DR EnsemblBacteria; BAA16487; BAA16487; BAA16487.
DR GeneID; 947084; -.
DR KEGG; ecj:JW2582; -.
DR KEGG; eco:b2601; -.
DR PATRIC; fig|1411691.4.peg.4138; -.
DR EchoBASE; EB0076; -.
DR eggNOG; COG0722; Bacteria.
DR HOGENOM; CLU_030903_0_1_6; -.
DR InParanoid; P00888; -.
DR OMA; VMENVAN; -.
DR PhylomeDB; P00888; -.
DR BioCyc; EcoCyc:AROF-MON; -.
DR BioCyc; MetaCyc:AROF-MON; -.
DR BRENDA; 2.5.1.54; 2026.
DR UniPathway; UPA00053; UER00084.
DR PRO; PR:P00888; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0003849; F:3-deoxy-7-phosphoheptulonate synthase activity; IDA:EcoCyc.
DR GO; GO:0042802; F:identical protein binding; IDA:EcoCyc.
DR GO; GO:0009073; P:aromatic amino acid family biosynthetic process; IMP:EcoCyc.
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 3D-structure; Amino-acid biosynthesis; Aromatic amino acid biosynthesis;
KW Direct protein sequencing; Reference proteome; Transferase.
FT CHAIN 1..356
FT /note="Phospho-2-dehydro-3-deoxyheptonate aldolase, Tyr-
FT sensitive"
FT /id="PRO_0000140831"
FT STRAND 6..8
FT /evidence="ECO:0007829|PDB:6AGM"
FT HELIX 20..26
FT /evidence="ECO:0007829|PDB:6AGM"
FT HELIX 31..48
FT /evidence="ECO:0007829|PDB:6AGM"
FT STRAND 54..60
FT /evidence="ECO:0007829|PDB:6AGM"
FT HELIX 67..84
FT /evidence="ECO:0007829|PDB:6AGM"
FT TURN 85..87
FT /evidence="ECO:0007829|PDB:6AGM"
FT STRAND 88..93
FT /evidence="ECO:0007829|PDB:6AGM"
FT STRAND 102..104
FT /evidence="ECO:0007829|PDB:6AGM"
FT HELIX 107..110
FT /evidence="ECO:0007829|PDB:6AGM"
FT STRAND 114..116
FT /evidence="ECO:0007829|PDB:6AGM"
FT HELIX 120..136
FT /evidence="ECO:0007829|PDB:6AGM"
FT STRAND 141..145
FT /evidence="ECO:0007829|PDB:6AGM"
FT STRAND 147..149
FT /evidence="ECO:0007829|PDB:6AGM"
FT HELIX 150..154
FT /evidence="ECO:0007829|PDB:6AGM"
FT HELIX 155..157
FT /evidence="ECO:0007829|PDB:6AGM"
FT STRAND 159..163
FT /evidence="ECO:0007829|PDB:6AGM"
FT HELIX 165..168
FT /evidence="ECO:0007829|PDB:6AGM"
FT STRAND 171..173
FT /evidence="ECO:0007829|PDB:6AGM"
FT HELIX 176..179
FT /evidence="ECO:0007829|PDB:6AGM"
FT STRAND 184..187
FT /evidence="ECO:0007829|PDB:6AGM"
FT HELIX 195..204
FT /evidence="ECO:0007829|PDB:6AGM"
FT STRAND 209..213
FT /evidence="ECO:0007829|PDB:6AGM"
FT STRAND 219..223
FT /evidence="ECO:0007829|PDB:6AGM"
FT STRAND 230..234
FT /evidence="ECO:0007829|PDB:6AGM"
FT STRAND 237..239
FT /evidence="ECO:0007829|PDB:6AGM"
FT HELIX 244..256
FT /evidence="ECO:0007829|PDB:6AGM"
FT STRAND 263..268
FT /evidence="ECO:0007829|PDB:6AGM"
FT HELIX 269..272
FT /evidence="ECO:0007829|PDB:6AGM"
FT HELIX 276..278
FT /evidence="ECO:0007829|PDB:6AGM"
FT HELIX 279..291
FT /evidence="ECO:0007829|PDB:6AGM"
FT STRAND 296..304
FT /evidence="ECO:0007829|PDB:6AGM"
FT HELIX 333..347
FT /evidence="ECO:0007829|PDB:6AGM"
FT TURN 348..354
FT /evidence="ECO:0007829|PDB:6AGM"
SQ SEQUENCE 356 AA; 38804 MW; A675537531FBC37D CRC64;
MQKDALNNVH ITDEQVLMTP EQLKAAFPLS LQQEAQIADS RKSISDIIAG RDPRLLVVCG
PCSIHDPETA LEYARRFKAL AAEVSDSLYL VMRVYFEKPR TTVGWKGLIN DPHMDGSFDV
EAGLQIARKL LLELVNMGLP LATEALDPNS PQYLGDLFSW SAIGARTTES QTHREMASGL
SMPVGFKNGT DGSLATAINA MRAAAQPHRF VGINQAGQVA LLQTQGNPDG HVILRGGKAP
NYSPADVAQC EKEMEQAGLR PSLMVDCSHG NSNKDYRRQP AVAESVVAQI KDGNRSIIGL
MIESNIHEGN QSSEQPRSEM KYGVSVTDAC ISWEMTDALL REIHQDLNGQ LTARVA
