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Q48255 (AROQ_HELPY) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 84. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended 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
OrganismHelicobacter pylori (strain ATCC 700392 / 26695) (Campylobacter pylori)
Taxonomic identifier85962 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Epsilonproteobacteria › Campylobacterales › Helicobacteraceae › Helicobacter

Protein attributes

Sequence length167 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 1671673-dehydroquinate dehydratase HAMAP MF_00169
PRO_0000159905

Regions

Region103 – 1042Substrate binding HAMAP MF_00169

Sites

Active site221Proton acceptor
Active site1021Proton donor
Binding site761Substrate
Binding site821Substrate
Binding site891Substrate
Binding site1131Substrate
Site171Transition state stabilizer

Experimental info

Sequence conflict1561K → Q in CAA67380. Ref.1

Secondary structure

1 .................................. 167
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q48255 [UniParc].

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

FASTA16718,483
        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

« Hide

References

« Hide '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. expand/collapse author list , Khalak H.G., Glodek A., McKenney K., FitzGerald L.M., Lee N., Adams M.D., Hickey E.K., Berg D.E., Gocayne J.D., Utterback T.R., Peterson J.D., Kelley J.M., Cotton M.D., Weidman J.F., Fujii C., Bowman C., Watthey L., Wallin E., Hayes W.S., Borodovsky M., Karp P.D., Smith H.O., Fraser C.M., 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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AE000511 Genomic DNA. Translation: AAD08081.1.
X98878 Genomic DNA. Translation: CAA67380.1.
PIRS72447.
RefSeqNP_207828.1. NC_000915.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1J2YX-ray2.60A1-167[»]
2C4VX-ray2.50A1-167[»]
2C4WX-ray1.55A1-167[»]
2C57X-ray3.10A/B/C/D/E/F/G/H/I/J/K/L1-167[»]
2WKSX-ray2.95A/B/C/D/E/F1-167[»]
2XB9X-ray2.75A/B/C1-167[»]
2XD9X-ray1.95A/B/C1-167[»]
2XDAX-ray1.85A1-167[»]
ProteinModelPortalQ48255.
SMRQ48255. Positions 1-158.
ModBaseSearch...

Protein-protein interaction databases

DIPDIP-3328N.
MINTMINT-180311.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID899573.
GenomeReviewsGene locus HP_1038 in contig AE000511_GR.
KEGGhpy:HP1038.
NMPDRfig|85962.1.peg.1025.
PATRIC20593413. VBIHelPyl33062_1087.
TIGRHP_1038.

Phylogenomic databases

HOGENOMHBG284657.
OMAVDWLHEA.
ProtClustDBPRK05395.

Family and domain databases

HAMAPMF_00169. AroQ.
[Tree]
InterProIPR001874. DHquinase_II.
IPR018509. DHquinase_II_CS.
[Graphical view]
Gene3DG3DSA:3.40.50.9100. DHquinase_II. 1 hit.
KOK03786.
PANTHERPTHR21272. DHquinase_II. 1 hit.
PfamPF01220. DHquinase_II. 1 hit.
[Graphical view]
PIRSFPIRSF001399. DHquinase_II. 1 hit.
ProDomPD004527. DHquinase_II. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SUPFAMSSF52304. DHquinase_II. 1 hit.
TIGRFAMsTIGR01088. AroQ. 1 hit.
PROSITEPS01029. DEHYDROQUINASE_II. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameAROQ_HELPY
AccessionPrimary (citable) accession number: Q48255
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1997
Last modified: January 25, 2012
This is version 84 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

Helicobacter pylori

Helicobacter pylori (strain 26695): entries and gene names

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

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