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Protein

Phospho-2-dehydro-3-deoxyheptonate aldolase, Phe-sensitive

Gene

aroG

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Stereospecific condensation of phosphoenolpyruvate (PEP) and D-erythrose-4-phosphate (E4P) giving rise to 3-deoxy-D-arabino-heptulosonate-7-phosphate (DAHP).

Catalytic activityi

Phosphoenolpyruvate + D-erythrose 4-phosphate + H2O = 3-deoxy-D-arabino-hept-2-ulosonate 7-phosphate + phosphate.

Pathwayi: chorismate biosynthesis

This protein is involved in step 1 of the subpathway that synthesizes chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate.
Proteins known to be involved in the 7 steps of the subpathway in this organism are:
  1. Phospho-2-dehydro-3-deoxyheptonate aldolase, Tyr-sensitive (aroF), Phospho-2-dehydro-3-deoxyheptonate aldolase, Trp-sensitive (aroH), Phospho-2-dehydro-3-deoxyheptonate aldolase, Phe-sensitive (aroG)
  2. 3-dehydroquinate synthase (aroB)
  3. 3-dehydroquinate dehydratase (aroD)
  4. Quinate/shikimate dehydrogenase (ydiB), Shikimate dehydrogenase (NADP(+)) (aroE)
  5. Shikimate kinase 2 (aroL), Shikimate kinase 1 (aroK)
  6. 3-phosphoshikimate 1-carboxyvinyltransferase (aroA)
  7. Chorismate synthase (aroC)
This subpathway is part of the pathway chorismate biosynthesis, which is itself part of Metabolic intermediate biosynthesis.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate, the pathway chorismate biosynthesis and in Metabolic intermediate biosynthesis.

GO - Molecular functioni

  • 3-deoxy-7-phosphoheptulonate synthase activity Source: EcoCyc
  • identical protein binding Source: EcoCyc

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Transferase

Keywords - Biological processi

Amino-acid biosynthesis, Aromatic amino acid biosynthesis

Enzyme and pathway databases

BioCyciEcoCyc:AROG-MONOMER.
ECOL316407:JW0737-MONOMER.
MetaCyc:AROG-MONOMER.
RETL1328306-WGS:GSTH-2382-MONOMER.
BRENDAi2.5.1.54. 2026.
SABIO-RKP0AB91.
UniPathwayiUPA00053; UER00084.

Names & Taxonomyi

Protein namesi
Recommended name:
Phospho-2-dehydro-3-deoxyheptonate aldolase, Phe-sensitive (EC:2.5.1.54)
Alternative name(s):
3-deoxy-D-arabino-heptulosonate 7-phosphate synthase
DAHP synthase
Phospho-2-keto-3-deoxyheptonate aldolase
Gene namesi
Name:aroG
Ordered Locus Names:b0754, JW0737
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG10079. aroG.

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: EcoCyc
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 350350Phospho-2-dehydro-3-deoxyheptonate aldolase, Phe-sensitivePRO_0000140835Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei244 – 2441N6-acetyllysine1 Publication

Keywords - PTMi

Acetylation

Proteomic databases

EPDiP0AB91.
PaxDbiP0AB91.
PRIDEiP0AB91.

2D gel databases

SWISS-2DPAGEP0AB91.

Interactioni

Subunit structurei

Homotetramer.

GO - Molecular functioni

  • identical protein binding Source: EcoCyc

Protein-protein interaction databases

BioGridi4261709. 10 interactions.
DIPiDIP-35898N.
IntActiP0AB91. 3 interactions.
STRINGi511145.b0754.

Chemistry

BindingDBiP0AB91.

Structurei

Secondary structure

1
350
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi10 – 145Combined sources
Helixi19 – 257Combined sources
Helixi30 – 4718Combined sources
Beta strandi54 – 596Combined sources
Helixi66 – 8217Combined sources
Turni83 – 864Combined sources
Beta strandi87 – 926Combined sources
Beta strandi100 – 1034Combined sources
Turni107 – 1093Combined sources
Beta strandi113 – 1153Combined sources
Helixi119 – 13517Combined sources
Beta strandi140 – 1434Combined sources
Beta strandi146 – 1483Combined sources
Helixi150 – 1534Combined sources
Helixi154 – 1563Combined sources
Beta strandi158 – 1625Combined sources
Turni164 – 1685Combined sources
Helixi170 – 1778Combined sources
Beta strandi183 – 1864Combined sources
Helixi194 – 20310Combined sources
Beta strandi208 – 2125Combined sources
Beta strandi216 – 2238Combined sources
Beta strandi229 – 2335Combined sources
Beta strandi236 – 2383Combined sources
Helixi243 – 25513Combined sources
Beta strandi262 – 2654Combined sources
Helixi268 – 2703Combined sources
Turni271 – 2733Combined sources
Helixi275 – 2773Combined sources
Helixi278 – 29013Combined sources
Beta strandi295 – 3039Combined sources
Beta strandi305 – 3095Combined sources
Beta strandi312 – 3143Combined sources
Beta strandi323 – 3264Combined sources
Helixi331 – 34919Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1GG1X-ray2.00A/B/C/D1-350[»]
1KFLX-ray2.80A/B/C/D/E/F/G/H2-350[»]
1N8FX-ray1.75A/B/C/D1-350[»]
1QR7X-ray2.60A/B/C/D1-350[»]
ProteinModelPortaliP0AB91.
SMRiP0AB91. Positions 8-350.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP0AB91.

Family & Domainsi

Sequence similaritiesi

Belongs to the class-I DAHP synthase family.Curated

Phylogenomic databases

eggNOGiENOG4105E99. Bacteria.
COG0722. LUCA.
HOGENOMiHOG000220501.
InParanoidiP0AB91.
KOiK01626.
OMAiGNIKIAT.
OrthoDBiEOG63JR9W.
PhylomeDBiP0AB91.

Family and domain databases

Gene3Di3.20.20.70. 1 hit.
InterProiIPR013785. Aldolase_TIM.
IPR006218. DAHP1/KDSA.
IPR006219. DHAP_synth_1.
[Graphical view]
PANTHERiPTHR21225. PTHR21225. 1 hit.
PfamiPF00793. DAHP_synth_1. 1 hit.
[Graphical view]
PIRSFiPIRSF001361. DAHP_synthase. 1 hit.
TIGRFAMsiTIGR00034. aroFGH. 1 hit.

Sequencei

Sequence statusi: Complete.

P0AB91-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MNYQNDDLRI KEIKELLPPV ALLEKFPATE NAANTVAHAR KAIHKILKGN
60 70 80 90 100
DDRLLVVIGP CSIHDPVAAK EYATRLLALR EELKDELEIV MRVYFEKPRT
110 120 130 140 150
TVGWKGLIND PHMDNSFQIN DGLRIARKLL LDINDSGLPA AGEFLDMITP
160 170 180 190 200
QYLADLMSWG AIGARTTESQ VHRELASGLS CPVGFKNGTD GTIKVAIDAI
210 220 230 240 250
NAAGAPHCFL SVTKWGHSAI VNTSGNGDCH IILRGGKEPN YSAKHVAEVK
260 270 280 290 300
EGLNKAGLPA QVMIDFSHAN SSKQFKKQMD VCADVCQQIA GGEKAIIGVM
310 320 330 340 350
VESHLVEGNQ SLESGEPLAY GKSITDACIG WEDTDALLRQ LANAVKARRG
Length:350
Mass (Da):38,010
Last modified:July 21, 1986 - v1
Checksum:i7477D361962E8710
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J01591 Genomic DNA. Translation: AAA23492.1.
U00096 Genomic DNA. Translation: AAC73841.1.
AP009048 Genomic DNA. Translation: BAA35416.1.
PIRiA01106. ADECHF.
RefSeqiNP_415275.1. NC_000913.3.
WP_001109196.1. NZ_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAC73841; AAC73841; b0754.
BAA35416; BAA35416; BAA35416.
GeneIDi945605.
KEGGiecj:JW0737.
eco:b0754.
PATRICi32116707. VBIEscCol129921_0779.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J01591 Genomic DNA. Translation: AAA23492.1.
U00096 Genomic DNA. Translation: AAC73841.1.
AP009048 Genomic DNA. Translation: BAA35416.1.
PIRiA01106. ADECHF.
RefSeqiNP_415275.1. NC_000913.3.
WP_001109196.1. NZ_LN832404.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1GG1X-ray2.00A/B/C/D1-350[»]
1KFLX-ray2.80A/B/C/D/E/F/G/H2-350[»]
1N8FX-ray1.75A/B/C/D1-350[»]
1QR7X-ray2.60A/B/C/D1-350[»]
ProteinModelPortaliP0AB91.
SMRiP0AB91. Positions 8-350.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4261709. 10 interactions.
DIPiDIP-35898N.
IntActiP0AB91. 3 interactions.
STRINGi511145.b0754.

Chemistry

BindingDBiP0AB91.

2D gel databases

SWISS-2DPAGEP0AB91.

Proteomic databases

EPDiP0AB91.
PaxDbiP0AB91.
PRIDEiP0AB91.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC73841; AAC73841; b0754.
BAA35416; BAA35416; BAA35416.
GeneIDi945605.
KEGGiecj:JW0737.
eco:b0754.
PATRICi32116707. VBIEscCol129921_0779.

Organism-specific databases

EchoBASEiEB0077.
EcoGeneiEG10079. aroG.

Phylogenomic databases

eggNOGiENOG4105E99. Bacteria.
COG0722. LUCA.
HOGENOMiHOG000220501.
InParanoidiP0AB91.
KOiK01626.
OMAiGNIKIAT.
OrthoDBiEOG63JR9W.
PhylomeDBiP0AB91.

Enzyme and pathway databases

UniPathwayiUPA00053; UER00084.
BioCyciEcoCyc:AROG-MONOMER.
ECOL316407:JW0737-MONOMER.
MetaCyc:AROG-MONOMER.
RETL1328306-WGS:GSTH-2382-MONOMER.
BRENDAi2.5.1.54. 2026.
SABIO-RKP0AB91.

Miscellaneous databases

EvolutionaryTraceiP0AB91.
PROiP0AB91.

Family and domain databases

Gene3Di3.20.20.70. 1 hit.
InterProiIPR013785. Aldolase_TIM.
IPR006218. DAHP1/KDSA.
IPR006219. DHAP_synth_1.
[Graphical view]
PANTHERiPTHR21225. PTHR21225. 1 hit.
PfamiPF00793. DAHP_synth_1. 1 hit.
[Graphical view]
PIRSFiPIRSF001361. DAHP_synthase. 1 hit.
TIGRFAMsiTIGR00034. aroFGH. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The nucleotide sequence of aroG, the gene for 3-deoxy-D-arabinoheptulosonate-7-phosphate synthetase (phe) in Escherichia coli K12."
    Davies W.D., Davidson B.E.
    Nucleic Acids Res. 10:4045-4058(1982) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: K12.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  4. "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
    Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
    Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  5. "Comparing the predicted and observed properties of proteins encoded in the genome of Escherichia coli K-12."
    Link A.J., Robison K., Church G.M.
    Electrophoresis 18:1259-1313(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 1-12.
    Strain: K12 / EMG2.
  6. "Lysine acetylation is a highly abundant and evolutionarily conserved modification in Escherichia coli."
    Zhang J., Sprung R., Pei J., Tan X., Kim S., Zhu H., Liu C.F., Grishin N.V., Zhao Y.
    Mol. Cell. Proteomics 8:215-225(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-244, IDENTIFICATION BY MASS SPECTROMETRY.
    Strain: K12 / JW1106 and K12 / MG1655 / ATCC 47076.
  7. "Crystal structure of phenylalanine-regulated 3-deoxy-D-arabino-heptulosonate-7-phosphate synthase from Escherichia coli."
    Shumilin I.A., Kretsinger R.H., Bauerle R.H.
    Structure 7:865-875(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS).

Entry informationi

Entry nameiAROG_ECOLI
AccessioniPrimary (citable) accession number: P0AB91
Secondary accession number(s): P00886
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 21, 1986
Last modified: March 16, 2016
This is version 92 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Miscellaneous

There are 3 DAHP synthases, AroG is feedback-inhibited by Phe. The other 2 DAHP synthases are Tyr- and Trp-sensitive, respectively.

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.