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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)DescriptionActionsGraphical viewLength
Binding sitei613-dehydroquinateUniRule annotation1 Publication1
Active sitei116Proton donor/acceptorUniRule annotation1 Publication1
Active sitei142Schiff-base intermediate with substrateUniRule annotation1 Publication1
Binding sitei1803-dehydroquinateUniRule annotation1 Publication1
Binding sitei2033-dehydroquinateUniRule annotation1

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

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

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001387921 – 2193-dehydroquinate dehydrataseAdd BLAST219

Interactioni

Subunit structurei

Homodimer.UniRule annotation1 Publication

Protein-protein interaction databases

STRINGi224324.aq_021.

Structurei

Secondary structure

1219
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi2 – 7Combined sources6
Helixi12 – 22Combined sources11
Beta strandi25 – 30Combined sources6
Helixi31 – 33Combined sources3
Helixi39 – 51Combined sources13
Beta strandi55 – 59Combined sources5
Helixi63 – 65Combined sources3
Helixi73 – 80Combined sources8
Turni81 – 83Combined sources3
Beta strandi84 – 90Combined sources7
Helixi94 – 96Combined sources3
Helixi97 – 106Combined sources10
Beta strandi110 – 119Combined sources10
Helixi124 – 136Combined sources13
Beta strandi139 – 146Combined sources8
Helixi150 – 160Combined sources11
Beta strandi167 – 174Combined sources8
Helixi175 – 178Combined sources4
Helixi179 – 182Combined sources4
Helixi183 – 186Combined sources4
Beta strandi190 – 192Combined sources3
Beta strandi194 – 197Combined sources4
Helixi206 – 216Combined sources11

3D structure databases

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

Miscellaneous databases

EvolutionaryTraceiO66440.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni28 – 303-dehydroquinate bindingUniRule annotation3

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiENOG4105FF2. Bacteria.
COG0710. LUCA.
HOGENOMiHOG000105515.
InParanoidiO66440.
KOiK03785.
OMAiHNFEMTP.
OrthoDBiPOG091H02LE.

Family and domain databases

CDDicd00502. DHQase_I. 1 hit.
Gene3Di3.20.20.70. 1 hit.
HAMAPiMF_00214. AroD. 1 hit.
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
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2EGZX-ray1.75A/C1-219[»]
2YSWX-ray2.25A/B/C1-219[»]
ProteinModelPortaliO66440.
SMRiO66440.
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.
OMAiHNFEMTP.
OrthoDBiPOG091H02LE.

Enzyme and pathway databases

UniPathwayiUPA00053; UER00086.

Miscellaneous databases

EvolutionaryTraceiO66440.

Family and domain databases

CDDicd00502. DHQase_I. 1 hit.
Gene3Di3.20.20.70. 1 hit.
HAMAPiMF_00214. AroD. 1 hit.
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...

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 30, 2016
This is version 104 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.