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P46380 (AROQ_AMYME) Reviewed, UniProtKB/Swiss-Prot

Last modified May 31, 2011. Version 60. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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
OrganismAmycolatopsis methanolica
Taxonomic identifier1814 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesPseudonocardineaePseudonocardiaceaeAmycolatopsis

Protein attributes

Sequence length20 AA.
Sequence statusFragment.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Catalyzes a trans-dehydration via an enolate intermediate. Is involved in both the catabolism of quinate and the biosynthesis of aromatic amino acids. 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.

Sequence similarities

Belongs to the type-II 3-dehydroquinase family.

Biophysicochemical properties

pH dependence:

Optimum pH is 9.0. HAMAP MF_00169

Temperature dependence:

Optimum temperature is 76 degrees Celsius. Thermostable.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – ›20›203-dehydroquinate dehydratase HAMAP MF_00169
PRO_0000159865

Sites

Site171Transition state stabilizer By similarity

Experimental info

Non-terminal residue201

Sequences

Sequence LengthMass (Da)Tools
P46380 [UniParc].

Last modified November 1, 1995. Version 1.
Checksum: C24AA183E5CFDF0A

FASTA202,197
        10         20 
MKVFVLNGPN LGRLGKREPA 

« Hide

References

[1]"Purification and characterization of a dual function 3-dehydroquinate dehydratase from Amycolatopsis methanolica."
Euverink G.J.W., Hessels G.I., Vrijbloed J.W., Coggins J.R., Dijkhuizen L.
J. Gen. Microbiol. 138:2449-2457(1992) [PubMed: 1479361] [Abstract]
Cited for: PROTEIN SEQUENCE.
Strain: DSM 44096 / JCM 8087 / NBRC 15065 / NCIMB 11946.

Cross-references

Sequence databases

PIRA47687.

3D structure databases

ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Enzyme and pathway databases

BioCycMetaCyc:MONOMER-15327.

Family and domain databases

HAMAPMF_00169. AroQ.
[Tree]
InterProIPR001874. DHquinase_II.
[Graphical view]
Gene3DG3DSA:3.40.50.9100. DHquinase_II. 1 hit.
PfamPF01220. DHquinase_II. 1 hit.
[Graphical view]
PROSITEPS01029. DEHYDROQUINASE_II. Partial match.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameAROQ_AMYME
AccessionPrimary (citable) accession number: P46380
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 1, 1995
Last modified: May 31, 2011
This is version 60 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families