3-dehydroquinate dehydratase - Helicobacter pylori

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Reviewed, UniProtKB/Swiss-Prot Q48255 (AROQ_HELPY)

Last modified February 9, 2010. Version 73. 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:
    3-dehydroquinate dehydratase
      Short name=3-dehydroquinase
    EC=4.2.1.10
Alternative name(s):
    Type II DHQase

Gene names

Name:	aroQ
Ordered Locus Names:	HP_1038

Organism

Helicobacter pylori (Campylobacter pylori) [Complete proteome] [HAMAP]

Taxonomic identifier

210 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Epsilonproteobacteria › Campylobacterales › Helicobacteraceae › Helicobacter

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Protein attributes

Sequence length	167 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level.

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General annotation (Comments)

Function	Catalyzes a trans-dehydration via an enolate intermediate By similarity. HAMAP MF_00169
Catalytic activity	3-dehydroquinate = 3-dehydroshikimate + H₂O. HAMAP MF_00169
Pathway	Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 3/7. HAMAP MF_00169
Subunit structure	Homododecamer. Ref.3 Ref.4
Sequence similarities	Belongs to the type-II 3-dehydroquinase family.

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Ontologies

Keywords
Biological process	Amino-acid biosynthesis Aromatic amino acid biosynthesis
Molecular function	Lyase
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: HAMAP
Molecular function	3-dehydroquinate dehydratase activity Inferred from electronic annotation. Source: HAMAP
Complete GO annotation...

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Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 167

167

3-dehydroquinate dehydratase HAMAP MF_00169

PRO_0000159905

Regions

Region

103 – 104

Substrate binding HAMAP MF_00169

Sites

Active site

Proton acceptor HAMAP MF_00169

Active site

102

Proton donor HAMAP MF_00169

Binding site

Substrate HAMAP MF_00169

Binding site

Substrate HAMAP MF_00169

Binding site

Substrate HAMAP MF_00169

Binding site

113

Substrate HAMAP MF_00169

Site

Transition state stabilizer HAMAP MF_00169

Experimental info

Sequence conflict

156

K → Q in CAA67380. Ref.1

Secondary structure

167

Helix Strand Turn

Details...

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Sequences

Sequence

Length

Mass (Da)

Tools

Q48255-1 [UniParc].

Last modified November 1, 1997. Version 2.
Checksum: 1AEC60B924987F07
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FASTA

167

18,483

        10         20         30         40         50         60 
MKILVIQGPN LNMLGHRDPR LYGMVTLDQI HEIMQTFVKQ GNLDVELEFF QTNFEGEIID 

        70         80         90        100        110        120 
KIQESVGSDY EGIIINPGAF SHTSIAIADA IMLAGKPVIE VHLTNIQARE EFRKNSYTGA 

       130        140        150        160 
ACGGVIMGFG PLGYNMALMA MVNILAEMKA FQEAQKNNPN NPINNQK

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References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Cloning, sequencing, expression, purification and preliminary characterization of a type II dehydroquinase from Helicobacter pylori." Bottomley J.R., Clayton C.L., Chalk P.A., Kleanthous C. Biochem. J. 319:559-565(1996) [PubMed: 8912695] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PARTIAL PROTEIN SEQUENCE. Strain: ATCC 43504 / NCTC 11637 / JCM 7653 / RPH 13487.
[2]	"The complete genome sequence of the gastric pathogen Helicobacter pylori." Tomb J.-F., White O., Kerlavage A.R., Clayton R.A., Sutton G.G., Fleischmann R.D., Ketchum K.A., Klenk H.-P., Gill S.R., Dougherty B.A., Nelson K.E., Quackenbush J., Zhou L., Kirkness E.F., Peterson S.N., Loftus B.J., Richardson D.L., Dodson R.J. Venter J.C. Nature 388:539-547(1997) [PubMed: 9252185] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 700392 / 26695.
[3]	"Crystal structure of the type II 3-dehydroquinase from Helicobacter pylori." Lee B.I., Kwak J.E., Suh S.W. Proteins 51:616-617(2003) [PubMed: 12784220] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 10-167 IN COMPLEX WITH SUBSTRATE, SUBUNIT.
[4]	"Crystal structures of Helicobacter pylori type II dehydroquinase inhibitor complexes: new directions for inhibitor design." Robinson D.A., Stewart K.A., Price N.C., Chalk P.A., Coggins J.R., Lapthorn A.J. J. Med. Chem. 49:1282-1290(2006) [PubMed: 16480265] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) IN COMPLEXES WITH SUBSTRATE ANALOGS, SUBUNIT.

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Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AE000511 Genomic DNA. Translation: AAD08081.1.
X98878 Genomic DNA. Translation: CAA67380.1.

PIR

S72447.

RefSeq

NP_207828.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1J2Y	X-ray	2.60	A	1-167	[»]
2C4V	X-ray	2.50	A	1-167	[»]
2C4W	X-ray	1.55	A	1-167	[»]
2C57	X-ray	3.10	A/B/C/D/E/F/G/H/I/J/K/L	1-167	[»]
2WKS	X-ray	2.95	A/B/C/D/E/F	1-167	[»]

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-3328N.

Genome annotation databases

GeneID

899573.

GenomeReviews

Gene locus HP_1038 in contig AE000511_GR.

KEGG

hpy:HP1038.

NMPDR

fig|85962.1.peg.1025.

TIGR

HP_1038.

Phylogenomic databases

HOGENOM

HBG284657.

OMA

EPGIYGG.

Enzyme and pathway databases

BRENDA

4.2.1.10. 1131.

Family and domain databases

HAMAP

MF_00169. AroQ.
[Tree]

InterPro

IPR001874. DHquinase_II.
IPR018509. DHquinase_II_CS.
[Graphical view]

Gene3D

G3DSA:3.40.50.9100. DHquinase_II. 1 hit.

PANTHER

PTHR21272. DHquinase_II. 1 hit.

Pfam

PF01220. DHquinase_II. 1 hit.
[Graphical view]

PIRSF

PIRSF001399. DHquinase_II. 1 hit.

ProDom

PD004527. DHquinase_II. 1 hit.
[Graphical view] [Entries sharing at least one domain]

TIGRFAMs

TIGR01088. aroQ. 1 hit.

PROSITE

PS01029. DEHYDROQUINASE_II. 1 hit.
[Graphical view]

ProtoNet

Search...

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Entry information

Entry name

AROQ_HELPY

Accession

Primary (citable) accession number: Q48255

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1997
Last sequence update:	November 1, 1997
Last modified:	February 9, 2010
This is version 73 of the entry and version 2 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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