Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

A3CZT7 (AROQ_SHEB5) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 45. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

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:Sbal_0470
OrganismShewanella baltica (strain OS155 / ATCC BAA-1091) [Complete proteome] [HAMAP]
Taxonomic identifier325240 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaAlteromonadalesShewanellaceaeShewanella

Protein attributes

Sequence length146 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Catalyzes a trans-dehydration via an enolate intermediate By similarity. HAMAP-Rule MF_00169

Catalytic activity

3-dehydroquinate = 3-dehydroshikimate + H2O. HAMAP-Rule MF_00169

Pathway

Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 3/7. HAMAP-Rule MF_00169

Subunit structure

Homododecamer By similarity. HAMAP-Rule MF_00169

Sequence similarities

Belongs to the type-II 3-dehydroquinase family.

Ontologies

Keywords
   Biological processAmino-acid biosynthesis
Aromatic amino acid biosynthesis
   Molecular functionLyase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological_processaromatic amino acid family biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-HAMAP

chorismate biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-UniPathway

   Molecular_function3-dehydroquinate dehydratase activity

Inferred from electronic annotation. Source: UniProtKB-HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 1461463-dehydroquinate dehydratase HAMAP-Rule MF_00169
PRO_1000023511

Regions

Region100 – 1012Substrate binding By similarity

Sites

Active site241Proton acceptor By similarity
Active site991Proton donor By similarity
Binding site731Substrate By similarity
Binding site791Substrate By similarity
Binding site861Substrate By similarity
Binding site1101Substrate By similarity
Site191Transition state stabilizer By similarity

Sequences

Sequence LengthMass (Da)Tools
A3CZT7 [UniParc].

Last modified March 20, 2007. Version 1.
Checksum: 45E65D3900A27233

FASTA14616,077
        10         20         30         40         50         60 
MSHKILLVNG PNLNLLGRRE PSVYGHQTLA DIVAELKQQA KLAEVELEHI QSNAEFELIN 

        70         80         90        100        110        120 
AIHATDAQMI IINPAAFTHT SVALRDALLG VAIPFFEVHL SNVHAREAFR HHSYFSDKAI 

       130        140 
GVICGFGSQG YEFALAAAIK RLNQPQ 

« Hide

References

[1]"Complete sequence of chromosome of Shewanella baltica OS155."
US DOE Joint Genome Institute
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S., Sims D.R., Brettin T., Bruce D., Han C., Tapia R., Brainard J., Schmutz J. expand/collapse author list , Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Brettar I., Klappenbach J., Konstantinidis K., Rodrigues J., Tiedje J., Richardson P.
Submitted (FEB-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: OS155 / ATCC BAA-1091.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000563 Genomic DNA. Translation: ABN60000.1.
RefSeqYP_001048869.1. NC_009052.1.

3D structure databases

ProteinModelPortalA3CZT7.
SMRA3CZT7. Positions 4-146.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING325240.Sbal_0470.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABN60000; ABN60000; Sbal_0470.
GeneID4842227.
KEGGsbl:Sbal_0470.
PATRIC37179647. VBISheBal55297_0686.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0757.
HOGENOMHOG000217278.
KOK03786.
OMARREPGHY.
OrthoDBEOG66MQVT.

Enzyme and pathway databases

BioCycSBAL325240:GCTA-484-MONOMER.
UniPathwayUPA00053; UER00086.

Family and domain databases

Gene3D3.40.50.9100. 1 hit.
HAMAPMF_00169. AroQ.
InterProIPR001874. DHquinase_II.
IPR018509. DHquinase_II_CS.
[Graphical view]
PANTHERPTHR21272. PTHR21272. 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. SSF52304. 1 hit.
TIGRFAMsTIGR01088. aroQ. 1 hit.
PROSITEPS01029. DEHYDROQUINASE_II. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameAROQ_SHEB5
AccessionPrimary (citable) accession number: A3CZT7
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: March 20, 2007
Last modified: May 14, 2014
This is version 45 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways