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Protein

3-dehydroquinate dehydratase

Gene

aroD

Organism
Aquifex aeolicus (strain VF5)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Involved in the third step of the chorismate pathway, which leads to the biosynthesis of aromatic amino acids. Catalyzes the cis-dehydration of 3-dehydroquinate (DHQ) and introduces the first double bond of the aromatic ring to yield 3-dehydroshikimate.UniRule annotation

Catalytic activityi

3-dehydroquinate = 3-dehydroshikimate + H2O.UniRule annotation

Pathwayi: chorismate biosynthesis

This protein is involved in step 3 of the subpathway that synthesizes chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate.UniRule annotation
Proteins known to be involved in the 7 steps of the subpathway in this organism are:
  1. no protein annotated in this organism
  2. no protein annotated in this organism
  3. 3-dehydroquinate dehydratase (aroD)
  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
Binding sitei61 – 6113-dehydroquinateUniRule annotation1 Publication
Active sitei116 – 1161Proton donor/acceptorUniRule annotation1 Publication
Active sitei142 – 1421Schiff-base intermediate with substrateUniRule annotation1 Publication
Binding sitei180 – 18013-dehydroquinateUniRule annotation1 Publication
Binding sitei203 – 20313-dehydroquinateUniRule annotation

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Lyase

Keywords - Biological processi

Amino-acid biosynthesis, Aromatic amino acid biosynthesis

Keywords - Ligandi

Schiff base

Enzyme and pathway databases

BioCyciAAEO224324:GJBH-14-MONOMER.
UniPathwayiUPA00053; UER00086.

Names & Taxonomyi

Protein namesi
Recommended name:
3-dehydroquinate dehydrataseUniRule annotation (EC:4.2.1.10UniRule annotation)
Short name:
3-dehydroquinaseUniRule annotation
Alternative name(s):
Type I DHQaseUniRule annotation
Type I dehydroquinaseUniRule annotation
Short name:
DHQ1UniRule annotation
Gene namesi
Name:aroDUniRule annotation
Ordered Locus Names:aq_021
OrganismiAquifex aeolicus (strain VF5)
Taxonomic identifieri224324 [NCBI]
Taxonomic lineageiBacteriaAquificaeAquificalesAquificaceaeAquifex
Proteomesi
  • UP000000798 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 2192193-dehydroquinate dehydratasePRO_0000138792Add
BLAST

Interactioni

Subunit structurei

Homodimer.UniRule annotation1 Publication

Protein-protein interaction databases

STRINGi224324.aq_021.

Structurei

Secondary structure

1
219
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi2 – 76Combined sources
Helixi12 – 2211Combined sources
Beta strandi25 – 306Combined sources
Helixi31 – 333Combined sources
Helixi39 – 5113Combined sources
Beta strandi55 – 595Combined sources
Helixi63 – 653Combined sources
Helixi73 – 808Combined sources
Turni81 – 833Combined sources
Beta strandi84 – 907Combined sources
Helixi94 – 963Combined sources
Helixi97 – 10610Combined sources
Beta strandi110 – 11910Combined sources
Helixi124 – 13613Combined sources
Beta strandi139 – 1468Combined sources
Helixi150 – 16011Combined sources
Beta strandi167 – 1748Combined sources
Helixi175 – 1784Combined sources
Helixi179 – 1824Combined sources
Helixi183 – 1864Combined sources
Beta strandi190 – 1923Combined sources
Beta strandi194 – 1974Combined sources
Helixi206 – 21611Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2EGZX-ray1.75A/C1-219[»]
2YSWX-ray2.25A/B/C1-219[»]
ProteinModelPortaliO66440.
SMRiO66440. Positions 1-219.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO66440.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni28 – 3033-dehydroquinate bindingUniRule annotation

Sequence similaritiesi

Belongs to the type-I 3-dehydroquinase family.UniRule annotation

Phylogenomic databases

eggNOGiENOG4105FF2. Bacteria.
COG0710. LUCA.
HOGENOMiHOG000105515.
InParanoidiO66440.
KOiK03785.
OMAiARVMCIT.
OrthoDBiEOG6P33BK.

Family and domain databases

Gene3Di3.20.20.70. 1 hit.
HAMAPiMF_00214. AroD.
InterProiIPR018508. 3-dehydroquinate_DH_AS.
IPR013785. Aldolase_TIM.
IPR001381. DHquinase_I.
[Graphical view]
PfamiPF01487. DHquinase_I. 1 hit.
[Graphical view]
TIGRFAMsiTIGR01093. aroD. 1 hit.
PROSITEiPS01028. DEHYDROQUINASE_I. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

O66440-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLIAVPLDDT NFSENLKKAK EKGADIVELR VDQFSDTSLN YVKEKLEEVH
60 70 80 90 100
SQGLKTILTI RSPEEGGREV KNREELFEEL SPLSDYTDIE LSSRGLLVKL
110 120 130 140 150
YNITKEAGKK LIISYHNFEL TPPNWIIREV LREGYRYGGI PKIAVKANSY
160 170 180 190 200
EDVARLLCIS RQVEGEKILI SMGDYGKISR LAGYVFGSVI TYCSLEKAFA
210
PGQIPLEEMV ELRKKFYRL
Length:219
Mass (Da):24,971
Last modified:August 1, 1998 - v1
Checksum:i144C4D5240C86F46
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE000657 Genomic DNA. Translation: AAC06389.1.
PIRiE70301.
RefSeqiNP_212999.1. NC_000918.1.
WP_010879937.1. NC_000918.1.

Genome annotation databases

EnsemblBacteriaiAAC06389; AAC06389; aq_021.
GeneIDi1192637.
KEGGiaae:aq_021.
PATRICi20957747. VBIAquAeo85532_0014.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE000657 Genomic DNA. Translation: AAC06389.1.
PIRiE70301.
RefSeqiNP_212999.1. NC_000918.1.
WP_010879937.1. NC_000918.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2EGZX-ray1.75A/C1-219[»]
2YSWX-ray2.25A/B/C1-219[»]
ProteinModelPortaliO66440.
SMRiO66440. Positions 1-219.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi224324.aq_021.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC06389; AAC06389; aq_021.
GeneIDi1192637.
KEGGiaae:aq_021.
PATRICi20957747. VBIAquAeo85532_0014.

Phylogenomic databases

eggNOGiENOG4105FF2. Bacteria.
COG0710. LUCA.
HOGENOMiHOG000105515.
InParanoidiO66440.
KOiK03785.
OMAiARVMCIT.
OrthoDBiEOG6P33BK.

Enzyme and pathway databases

UniPathwayiUPA00053; UER00086.
BioCyciAAEO224324:GJBH-14-MONOMER.

Miscellaneous databases

EvolutionaryTraceiO66440.

Family and domain databases

Gene3Di3.20.20.70. 1 hit.
HAMAPiMF_00214. AroD.
InterProiIPR018508. 3-dehydroquinate_DH_AS.
IPR013785. Aldolase_TIM.
IPR001381. DHquinase_I.
[Graphical view]
PfamiPF01487. DHquinase_I. 1 hit.
[Graphical view]
TIGRFAMsiTIGR01093. aroD. 1 hit.
PROSITEiPS01028. DEHYDROQUINASE_I. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: VF5.
  2. "Crystal structure of type I 3-dehydroquinate dehydratase of Aquifex aeolicus suggests closing of active site flap is not essential for enzyme action."
    Devi A.S., Ebihara A., Kuramitsu S., Yokoyama S., Kumarevel T.S., Ponnuraj K.
    Biochem. Biophys. Res. Commun. 432:350-354(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS) IN COMPLEX WITH SUBSTRATE ANALOGS, ACTIVE SITE, SUBUNIT.

Entry informationi

Entry nameiAROD_AQUAE
AccessioniPrimary (citable) accession number: O66440
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: August 1, 1998
Last modified: November 11, 2015
This is version 100 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. 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.