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

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P0AB91 (AROG_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 72. History...

Clusters with 100%, 90%, 50% identity |

Documents (4) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

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 names

Name:	aroG
Ordered Locus Names:	b0754, JW0737

Organism

Escherichia coli (strain K12) [Reference proteome] [HAMAP]

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia ›

Protein attributes

Sequence length	350 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Stereospecific condensation of phosphoenolpyruvate (PEP) and D-erythrose-4-phosphate (E4P) giving rise to 3-deoxy-D-arabino-heptulosonate-7-phosphate (DAHP).
Catalytic activity	Phosphoenolpyruvate + D-erythrose 4-phosphate + H₂O = 3-deoxy-D-arabino-hept-2-ulosonate 7-phosphate + phosphate.
Pathway	Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 1/7.
Subunit structure	Homotetramer.
Miscellaneous	There are 3 DAHP synthases, AroG is feedback-inhibited by Phe. The other 2 DAHP synthases are Tyr- and Trp-sensitive, respectively.
Sequence similarities	Belongs to the class-I DAHP synthase family.

Ontologies

Keywords
Biological process	Amino-acid biosynthesis Aromatic amino acid biosynthesis
Molecular function	Transferase
PTM	Acetylation
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	aromatic amino acid family biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW chorismate biosynthetic process Inferred from electronic annotation. Source: UniProtKB-UniPathway
Molecular_function	3-deoxy-7-phosphoheptulonate synthase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 350

350

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

PRO_0000140835

Amino acid modifications

Modified residue

244

N6-acetyllysine Ref.6

Secondary structure

350

Helix Strand Turn

Details...

Sequences

Sequence

Length

Mass (Da)

Tools

P0AB91 [UniParc].

Last modified July 21, 1986. Version 1.
Checksum: 7477D361962E8710
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FASTA

350

38,010

        10         20         30         40         50         60 
MNYQNDDLRI KEIKELLPPV ALLEKFPATE NAANTVAHAR KAIHKILKGN DDRLLVVIGP 

        70         80         90        100        110        120 
CSIHDPVAAK EYATRLLALR EELKDELEIV MRVYFEKPRT TVGWKGLIND PHMDNSFQIN 

       130        140        150        160        170        180 
DGLRIARKLL LDINDSGLPA AGEFLDMITP QYLADLMSWG AIGARTTESQ VHRELASGLS 

       190        200        210        220        230        240 
CPVGFKNGTD GTIKVAIDAI NAAGAPHCFL SVTKWGHSAI VNTSGNGDCH IILRGGKEPN 

       250        260        270        280        290        300 
YSAKHVAEVK EGLNKAGLPA QVMIDFSHAN SSKQFKKQMD VCADVCQQIA GGEKAIIGVM 

       310        320        330        340        350 
VESHLVEGNQ SLESGEPLAY GKSITDACIG WEDTDALLRQ LANAVKARRG

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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]	"A 718-kb DNA sequence of the Escherichia coli K-12 genome corresponding to the 12.7-28.0 min region on the linkage map." Oshima T., Aiba H., Baba T., Fujita K., Hayashi K., Honjo A., Ikemoto K., Inada T., Itoh T., Kajihara M., Kanai K., Kashimoto K., Kimura S., Kitagawa M., Makino K., Masuda S., Miki T., Mizobuchi K. Horiuchi T. DNA Res. 3:137-155(1996) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[3]	"The complete genome sequence of Escherichia coli K-12." Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y. Science 277:1453-1474(1997) [PubMed] [Europe PMC] [Abstract] 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, 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).
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

J01591 Genomic DNA. Translation: AAA23492.1.
U00096 Genomic DNA. Translation: AAC73841.1.
AP009048 Genomic DNA. Translation: BAA35416.1.

PIR

ADECHF. A01106.

RefSeq

NP_415275.1. NC_000913.2.
YP_489027.1. NC_007779.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1GG1	X-ray	2.00	A/B/C/D	1-350	[»]
1KFL	X-ray	2.80	A/B/C/D/E/F/G/H	1-350	[»]
1N8F	X-ray	1.75	A/B/C/D	1-350	[»]
1QR7	X-ray	2.60	A/B/C/D	1-350	[»]

ProteinModelPortal

P0AB91.

SMR

P0AB91. Positions 8-350.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-35898N.

IntAct

P0AB91. 3 interactions.

STRING

511145.b0754.

2D gel databases

SWISS-2DPAGE

P0AB91.

Proteomic databases

PaxDb

P0AB91.

PRIDE

P0AB91.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

AAC73841; AAC73841; b0754.
BAA35416; BAA35416; BAA35416.

GeneID

12932715.
945605.

KEGG

ecj:Y75_p0727.
eco:b0754.

PATRIC

32116707. VBIEscCol129921_0779.

Organism-specific databases

EchoBASE

EB0077.

EcoGene

EG10079. aroG.

Phylogenomic databases

eggNOG

COG0722.

HOGENOM

HOG000220501.

K01626.

OMA

MDNSFKL.

ProtClustDB

PRK09261.

Enzyme and pathway databases

BioCyc

EcoCyc:AROG-MONOMER.
ECOL316407:JW0737-MONOMER.
MetaCyc:AROG-MONOMER.

BRENDA

2.5.1.54. 2026.

SABIO-RK

P0AB91.

UniPathway

UPA00053; UER00084.

Gene expression databases

Genevestigator

P0AB91.

Family and domain databases

Gene3D

3.20.20.70. 1 hit.

InterPro

IPR013785. Aldolase_TIM.
IPR006218. DAHP1/KDSA.
IPR006219. DHAP_synth_1.
[Graphical view]

PANTHER

PTHR21225. PTHR21225. 1 hit.

Pfam

PF00793. DAHP_synth_1. 1 hit.
[Graphical view]

PIRSF

PIRSF001361. DAHP_synthase. 1 hit.

TIGRFAMs

TIGR00034. aroFGH. 1 hit.

ProtoNet

Search...

Other

BindingDB

P0AB91.

ChEMBL

CHEMBL4911.

EvolutionaryTrace

P0AB91.

Entry information

Entry name

AROG_ECOLI

Accession

Primary (citable) accession number: P0AB91
Secondary accession number(s): P00886

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 21, 1986
Last sequence update:	July 21, 1986
Last modified:	May 1, 2013
This is version 72 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program

Relevant documents

Escherichia coli

Escherichia coli (strain K12): entries and cross-references to EcoGene

PATHWAY comments

Index of metabolic and biosynthesis pathways

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Amino acid modifications

Secondary structure

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

2D gel databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents