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

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Reviewed, UniProtKB/Swiss-Prot P0AB91 (AROG_ECOLI)

Last modified November 3, 2009. Version 43. History...

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Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein names

Recommended name:
    Phospho-2-dehydro-3-deoxyheptonate aldolase, Phe-sensitive
    EC=2.5.1.54
Alternative name(s):
    Phospho-2-keto-3-deoxyheptonate aldolase
    3-deoxy-D-arabino-heptulosonate 7-phosphate synthase
    DAHP synthetase

Gene names

Name:	aroG
Ordered Locus Names:	b0754, JW0737

Organism

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

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

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Protein attributes

Sequence length	350 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

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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 synthetase family.

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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
Gene Ontology (GO)
Biological process	aromatic amino acid family biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	3-deoxy-7-phosphoheptulonate synthase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

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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...

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Sequences

Sequence

Length

Mass (Da)

Tools

P0AB91-1 [UniParc].

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

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

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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: 6125934] [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: 8905232] [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: 9278503] [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: 16738553] [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: 9298646] [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: 18723842] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-244, MASS SPECTROMETRY.
[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: 10425687] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS).
+	Additional computationally mapped references.

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Cross-references

Sequence databases

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

PIR

ADECHF. A01106.

RefSeq

AP_001385.1.
NP_415275.1.

3D structure databases

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	[»]

ModBase

Search...

Protein-protein interaction databases

STRING

P0AB91.

2-D gel databases

SWISS-2DPAGE

P0AB91.

Genome annotation databases

GeneID

945605.

GenomeReviews

Gene locus JW0737 in contig AP009048_GR.
Gene locus b0754 in contig U00096_GR.

KEGG

ecj:JW0737.
eco:b0754.

Organism-specific databases

EchoBASE

EB0077.

EcoGene

EG10079. aroG.

CMR

Search...

Phylogenomic databases

HOGENOM

P0AB91.

OMA

MDNSFKL.

Enzyme and pathway databases

BioCyc

EcoCyc:AROG-MON.
MetaCyc:AROG-MON.

BRENDA

2.5.1.54. 246.

Gene expression databases

Genevestigator

P0AB91.

Family and domain databases

InterPro

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

Gene3D

G3DSA:3.20.20.70. Aldolase_TIM. 1 hit.

PANTHER

PTHR21225. AroFGH. 1 hit.

Pfam

PF00793. DAHP_synth_1. 1 hit.
[Graphical view]

PIRSF

PIRSF001361. DAHP_synthase. 1 hit.

TIGRFAMs

TIGR00034. aroFGH. 1 hit.

ProtoNet

Search...

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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:	November 3, 2009
This is version 43 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

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