AROG_ECOLI
ID AROG_ECOLI Reviewed; 350 AA.
AC P0AB91; P00886;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 21-JUL-1986, sequence version 1.
DT 03-AUG-2022, entry version 129.
DE RecName: Full=Phospho-2-dehydro-3-deoxyheptonate aldolase, Phe-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=aroG; OrderedLocusNames=b0754, JW0737;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12;
RX PubMed=6125934; DOI=10.1093/nar/10.13.4045;
RA Davies W.D., Davidson B.E.;
RT "The nucleotide sequence of aroG, the gene for 3-deoxy-D-
RT arabinoheptulosonate-7-phosphate synthetase (phe) in Escherichia coli
RT K12.";
RL Nucleic Acids Res. 10:4045-4058(1982).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=8905232; DOI=10.1093/dnares/3.3.137;
RA Oshima T., Aiba H., Baba T., Fujita K., Hayashi K., Honjo A., Ikemoto K.,
RA Inada T., Itoh T., Kajihara M., Kanai K., Kashimoto K., Kimura S.,
RA Kitagawa M., Makino K., Masuda S., Miki T., Mizobuchi K., Mori H.,
RA Motomura K., Nakamura Y., Nashimoto H., Nishio Y., Saito N., Sampei G.,
RA Seki Y., Tagami H., Takemoto K., Wada C., Yamamoto Y., Yano M.,
RA Horiuchi T.;
RT "A 718-kb DNA sequence of the Escherichia coli K-12 genome corresponding to
RT the 12.7-28.0 min region on the linkage map.";
RL DNA Res. 3:137-155(1996).
RN [3]
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 [4]
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 [5]
RP PROTEIN SEQUENCE OF 1-12.
RC STRAIN=K12 / EMG2;
RX PubMed=9298646; DOI=10.1002/elps.1150180807;
RA Link A.J., Robison K., Church G.M.;
RT "Comparing the predicted and observed properties of proteins encoded in the
RT genome of Escherichia coli K-12.";
RL Electrophoresis 18:1259-1313(1997).
RN [6]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-244, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC STRAIN=K12 / JW1106, and K12 / MG1655 / ATCC 47076;
RX PubMed=18723842; DOI=10.1074/mcp.m800187-mcp200;
RA Zhang J., Sprung R., Pei J., Tan X., Kim S., Zhu H., Liu C.F.,
RA Grishin N.V., Zhao Y.;
RT "Lysine acetylation is a highly abundant and evolutionarily conserved
RT modification in Escherichia coli.";
RL Mol. Cell. Proteomics 8:215-225(2009).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS).
RX PubMed=10425687; DOI=10.1016/s0969-2126(99)80109-9;
RA Shumilin I.A., Kretsinger R.H., Bauerle R.H.;
RT "Crystal structure of phenylalanine-regulated 3-deoxy-D-arabino-
RT heptulosonate-7-phosphate synthase from Escherichia coli.";
RL Structure 7:865-875(1999).
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 -!- SUBUNIT: Homotetramer.
CC -!- INTERACTION:
CC P0AB91; P0AB91: aroG; NbExp=5; IntAct=EBI-1120055, EBI-1120055;
CC -!- MISCELLANEOUS: There are 3 DAHP synthases, AroG is feedback-inhibited
CC by Phe. The other 2 DAHP synthases are Tyr- and Trp-sensitive,
CC respectively.
CC -!- SIMILARITY: Belongs to the class-I DAHP synthase family. {ECO:0000305}.
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DR EMBL; J01591; AAA23492.1; -; Genomic_DNA.
DR EMBL; U00096; AAC73841.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA35416.1; -; Genomic_DNA.
DR PIR; A01106; ADECHF.
DR RefSeq; NP_415275.1; NC_000913.3.
DR RefSeq; WP_001109196.1; NZ_SSZK01000002.1.
DR PDB; 1GG1; X-ray; 2.00 A; A/B/C/D=1-350.
DR PDB; 1KFL; X-ray; 2.80 A; A/B/C/D/E/F/G/H=2-350.
DR PDB; 1N8F; X-ray; 1.75 A; A/B/C/D=1-350.
DR PDB; 1QR7; X-ray; 2.60 A; A/B/C/D=1-350.
DR PDB; 5CKS; X-ray; 2.12 A; A/B/C/D=1-350.
DR PDB; 7RUD; X-ray; 2.80 A; A/B/C/D=1-350.
DR PDB; 7RUE; X-ray; 2.50 A; A/B/C/D=1-350.
DR PDBsum; 1GG1; -.
DR PDBsum; 1KFL; -.
DR PDBsum; 1N8F; -.
DR PDBsum; 1QR7; -.
DR PDBsum; 5CKS; -.
DR PDBsum; 7RUD; -.
DR PDBsum; 7RUE; -.
DR AlphaFoldDB; P0AB91; -.
DR SMR; P0AB91; -.
DR BioGRID; 4261709; 17.
DR DIP; DIP-35898N; -.
DR IntAct; P0AB91; 3.
DR STRING; 511145.b0754; -.
DR BindingDB; P0AB91; -.
DR DrugBank; DB02726; 2-Phosphoglycolic Acid.
DR DrugBank; DB01819; Phosphoenolpyruvate.
DR iPTMnet; P0AB91; -.
DR SWISS-2DPAGE; P0AB91; -.
DR jPOST; P0AB91; -.
DR PaxDb; P0AB91; -.
DR PRIDE; P0AB91; -.
DR EnsemblBacteria; AAC73841; AAC73841; b0754.
DR EnsemblBacteria; BAA35416; BAA35416; BAA35416.
DR GeneID; 66670975; -.
DR GeneID; 945605; -.
DR KEGG; ecj:JW0737; -.
DR KEGG; eco:b0754; -.
DR PATRIC; fig|1411691.4.peg.1525; -.
DR EchoBASE; EB0077; -.
DR eggNOG; COG0722; Bacteria.
DR HOGENOM; CLU_030903_0_1_6; -.
DR InParanoid; P0AB91; -.
DR OMA; DINTGLR; -.
DR PhylomeDB; P0AB91; -.
DR BioCyc; EcoCyc:AROG-MON; -.
DR BioCyc; MetaCyc:AROG-MON; -.
DR BRENDA; 2.5.1.54; 2026.
DR SABIO-RK; P0AB91; -.
DR UniPathway; UPA00053; UER00084.
DR EvolutionaryTrace; P0AB91; -.
DR PRO; PR:P0AB91; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IDA:EcoCyc.
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; 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 1: Evidence at protein level;
KW 3D-structure; Acetylation; Amino-acid biosynthesis;
KW Aromatic amino acid biosynthesis; Direct protein sequencing;
KW Reference proteome; Transferase.
FT CHAIN 1..350
FT /note="Phospho-2-dehydro-3-deoxyheptonate aldolase, Phe-
FT sensitive"
FT /id="PRO_0000140835"
FT MOD_RES 244
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000269|PubMed:18723842"
FT STRAND 10..14
FT /evidence="ECO:0007829|PDB:1N8F"
FT HELIX 19..25
FT /evidence="ECO:0007829|PDB:1N8F"
FT HELIX 30..47
FT /evidence="ECO:0007829|PDB:1N8F"
FT STRAND 54..59
FT /evidence="ECO:0007829|PDB:1N8F"
FT HELIX 66..82
FT /evidence="ECO:0007829|PDB:1N8F"
FT TURN 83..86
FT /evidence="ECO:0007829|PDB:1N8F"
FT STRAND 87..92
FT /evidence="ECO:0007829|PDB:1N8F"
FT STRAND 100..103
FT /evidence="ECO:0007829|PDB:1N8F"
FT TURN 107..109
FT /evidence="ECO:0007829|PDB:1N8F"
FT STRAND 113..115
FT /evidence="ECO:0007829|PDB:1N8F"
FT HELIX 119..135
FT /evidence="ECO:0007829|PDB:1N8F"
FT STRAND 140..143
FT /evidence="ECO:0007829|PDB:1N8F"
FT STRAND 146..148
FT /evidence="ECO:0007829|PDB:5CKS"
FT HELIX 150..153
FT /evidence="ECO:0007829|PDB:1N8F"
FT HELIX 154..156
FT /evidence="ECO:0007829|PDB:1N8F"
FT STRAND 158..162
FT /evidence="ECO:0007829|PDB:1N8F"
FT TURN 164..168
FT /evidence="ECO:0007829|PDB:1N8F"
FT HELIX 170..177
FT /evidence="ECO:0007829|PDB:1N8F"
FT STRAND 183..186
FT /evidence="ECO:0007829|PDB:1N8F"
FT HELIX 194..203
FT /evidence="ECO:0007829|PDB:1N8F"
FT STRAND 208..212
FT /evidence="ECO:0007829|PDB:1N8F"
FT STRAND 216..223
FT /evidence="ECO:0007829|PDB:1N8F"
FT STRAND 229..233
FT /evidence="ECO:0007829|PDB:1N8F"
FT STRAND 236..238
FT /evidence="ECO:0007829|PDB:1N8F"
FT HELIX 243..255
FT /evidence="ECO:0007829|PDB:1N8F"
FT STRAND 262..265
FT /evidence="ECO:0007829|PDB:1N8F"
FT HELIX 268..270
FT /evidence="ECO:0007829|PDB:1N8F"
FT TURN 271..273
FT /evidence="ECO:0007829|PDB:1N8F"
FT HELIX 275..277
FT /evidence="ECO:0007829|PDB:1N8F"
FT HELIX 278..290
FT /evidence="ECO:0007829|PDB:1N8F"
FT STRAND 295..303
FT /evidence="ECO:0007829|PDB:1N8F"
FT STRAND 305..309
FT /evidence="ECO:0007829|PDB:1N8F"
FT STRAND 312..314
FT /evidence="ECO:0007829|PDB:1N8F"
FT STRAND 323..326
FT /evidence="ECO:0007829|PDB:1N8F"
FT HELIX 331..349
FT /evidence="ECO:0007829|PDB:1N8F"
SQ SEQUENCE 350 AA; 38010 MW; 7477D361962E8710 CRC64;
MNYQNDDLRI KEIKELLPPV ALLEKFPATE NAANTVAHAR KAIHKILKGN DDRLLVVIGP
CSIHDPVAAK EYATRLLALR EELKDELEIV MRVYFEKPRT TVGWKGLIND PHMDNSFQIN
DGLRIARKLL LDINDSGLPA AGEFLDMITP QYLADLMSWG AIGARTTESQ VHRELASGLS
CPVGFKNGTD GTIKVAIDAI NAAGAPHCFL SVTKWGHSAI VNTSGNGDCH IILRGGKEPN
YSAKHVAEVK EGLNKAGLPA QVMIDFSHAN SSKQFKKQMD VCADVCQQIA GGEKAIIGVM
VESHLVEGNQ SLESGEPLAY GKSITDACIG WEDTDALLRQ LANAVKARRG
