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Protein

3-dehydroquinate dehydratase

Gene

aroQ

Organism
Helicobacter pylori (strain ATCC 700392 / 26695) (Campylobacter pylori)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes a trans-dehydration via an enolate intermediate.By similarity

Catalytic activityi

3-dehydroquinate = 3-dehydroshikimate + H2O.

Pathwayi: chorismate biosynthesis

This protein is involved in step 3 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. no protein annotated in this organism
  2. 3-dehydroquinate synthase (aroB)
  3. 3-dehydroquinate dehydratase (aroQ)
  4. Shikimate dehydrogenase (NADP(+)) (aroE)
  5. Shikimate kinase (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.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei17 – 171Transition state stabilizer
Active sitei22 – 221Proton acceptor
Binding sitei76 – 761Substrate1 Publication
Binding sitei82 – 821Substrate1 Publication
Binding sitei89 – 891Substrate1 Publication
Active sitei102 – 1021Proton donor
Binding sitei113 – 1131Substrate1 Publication

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Lyase

Keywords - Biological processi

Amino-acid biosynthesis, Aromatic amino acid biosynthesis

Enzyme and pathway databases

BioCyciHPY:HP1038-MONOMER.
BRENDAi4.2.1.10. 2604.
UniPathwayiUPA00053; UER00086.

Names & Taxonomyi

Protein namesi
Recommended name:
3-dehydroquinate dehydratase (EC:4.2.1.10)
Short name:
3-dehydroquinase
Alternative name(s):
Type II DHQase
Gene namesi
Name:aroQ
Ordered Locus Names:HP_1038
OrganismiHelicobacter pylori (strain ATCC 700392 / 26695) (Campylobacter pylori)
Taxonomic identifieri85962 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaEpsilonproteobacteriaCampylobacteralesHelicobacteraceaeHelicobacter
Proteomesi
  • UP000000429 Componenti: Chromosome

Pathology & Biotechi

Chemistry

ChEMBLiCHEMBL4680.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 1671673-dehydroquinate dehydratasePRO_0000159905Add
BLAST

Proteomic databases

PaxDbiQ48255.
PRIDEiQ48255.

Interactioni

Subunit structurei

Homododecamer.2 Publications

Protein-protein interaction databases

DIPiDIP-3328N.
IntActiQ48255. 2 interactions.
MINTiMINT-180311.
STRINGi85962.HP1038.

Chemistry

BindingDBiQ48255.

Structurei

Secondary structure

167
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi1 – 77Combined sources
Helixi11 – 133Combined sources
Turni14 – 163Combined sources
Helixi20 – 223Combined sources
Helixi27 – 4014Combined sources
Beta strandi45 – 517Combined sources
Helixi55 – 6612Combined sources
Beta strandi67 – 693Combined sources
Beta strandi72 – 765Combined sources
Helixi78 – 825Combined sources
Helixi85 – 928Combined sources
Beta strandi94 – 963Combined sources
Beta strandi98 – 1047Combined sources
Helixi106 – 1083Combined sources
Helixi111 – 1133Combined sources
Helixi117 – 1215Combined sources
Beta strandi122 – 1298Combined sources
Helixi132 – 15221Combined sources
Turni153 – 1564Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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[»]
4B6RX-ray2.00A/B/C1-167[»]
4B6SX-ray1.90A/B/C1-167[»]
ProteinModelPortaliQ48255.
SMRiQ48255. Positions 1-158.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ48255.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni103 – 1042Substrate binding

Sequence similaritiesi

Belongs to the type-II 3-dehydroquinase family.Curated

Phylogenomic databases

eggNOGiENOG4108Z38. Bacteria.
COG0757. LUCA.
KOiK03786.
OMAiIPTIEVH.
OrthoDBiEOG66MQVT.

Family and domain databases

Gene3Di3.40.50.9100. 1 hit.
HAMAPiMF_00169. AroQ.
InterProiIPR001874. DHquinase_II.
IPR018509. DHquinase_II_CS.
[Graphical view]
PANTHERiPTHR21272. PTHR21272. 1 hit.
PfamiPF01220. DHquinase_II. 1 hit.
[Graphical view]
PIRSFiPIRSF001399. DHquinase_II. 1 hit.
ProDomiPD004527. DHquinase_II. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SUPFAMiSSF52304. SSF52304. 1 hit.
TIGRFAMsiTIGR01088. aroQ. 1 hit.
PROSITEiPS01029. DEHYDROQUINASE_II. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q48255-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKILVIQGPN LNMLGHRDPR LYGMVTLDQI HEIMQTFVKQ GNLDVELEFF
60 70 80 90 100
QTNFEGEIID KIQESVGSDY EGIIINPGAF SHTSIAIADA IMLAGKPVIE
110 120 130 140 150
VHLTNIQARE EFRKNSYTGA ACGGVIMGFG PLGYNMALMA MVNILAEMKA
160
FQEAQKNNPN NPINNQK
Length:167
Mass (Da):18,483
Last modified:November 1, 1997 - v2
Checksum:i1AEC60B924987F07
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti156 – 1561K → Q in CAA67380 (PubMed:8912695).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE000511 Genomic DNA. Translation: AAD08081.1.
X98878 Genomic DNA. Translation: CAA67380.1.
PIRiS72447.
RefSeqiNP_207828.1. NC_000915.1.
WP_000699284.1. NC_018939.1.

Genome annotation databases

EnsemblBacteriaiAAD08081; AAD08081; HP_1038.
GeneIDi899573.
KEGGiheo:C694_05370.
hpy:HP1038.
PATRICi20593413. VBIHelPyl33062_1087.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE000511 Genomic DNA. Translation: AAD08081.1.
X98878 Genomic DNA. Translation: CAA67380.1.
PIRiS72447.
RefSeqiNP_207828.1. NC_000915.1.
WP_000699284.1. NC_018939.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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[»]
4B6RX-ray2.00A/B/C1-167[»]
4B6SX-ray1.90A/B/C1-167[»]
ProteinModelPortaliQ48255.
SMRiQ48255. Positions 1-158.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-3328N.
IntActiQ48255. 2 interactions.
MINTiMINT-180311.
STRINGi85962.HP1038.

Chemistry

BindingDBiQ48255.
ChEMBLiCHEMBL4680.

Proteomic databases

PaxDbiQ48255.
PRIDEiQ48255.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAD08081; AAD08081; HP_1038.
GeneIDi899573.
KEGGiheo:C694_05370.
hpy:HP1038.
PATRICi20593413. VBIHelPyl33062_1087.

Phylogenomic databases

eggNOGiENOG4108Z38. Bacteria.
COG0757. LUCA.
KOiK03786.
OMAiIPTIEVH.
OrthoDBiEOG66MQVT.

Enzyme and pathway databases

UniPathwayiUPA00053; UER00086.
BioCyciHPY:HP1038-MONOMER.
BRENDAi4.2.1.10. 2604.

Miscellaneous databases

EvolutionaryTraceiQ48255.
PROiQ48255.

Family and domain databases

Gene3Di3.40.50.9100. 1 hit.
HAMAPiMF_00169. AroQ.
InterProiIPR001874. DHquinase_II.
IPR018509. DHquinase_II_CS.
[Graphical view]
PANTHERiPTHR21272. PTHR21272. 1 hit.
PfamiPF01220. DHquinase_II. 1 hit.
[Graphical view]
PIRSFiPIRSF001399. DHquinase_II. 1 hit.
ProDomiPD004527. DHquinase_II. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SUPFAMiSSF52304. SSF52304. 1 hit.
TIGRFAMsiTIGR01088. aroQ. 1 hit.
PROSITEiPS01029. DEHYDROQUINASE_II. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PARTIAL PROTEIN SEQUENCE.
    Strain: ATCC 43504 / NCTC 11637 / JCM 7653 / RPH 13487.
  2. 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] [Europe PMC] [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] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) IN COMPLEXES WITH SUBSTRATE ANALOGS, SUBUNIT.

Entry informationi

Entry nameiAROQ_HELPY
AccessioniPrimary (citable) accession number: Q48255
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1997
Last modified: June 8, 2016
This is version 115 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

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

Documents

  1. Helicobacter pylori
    Helicobacter pylori (strain 26695): entries and gene names
  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.