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Protein

3-dehydroquinate dehydratase

Gene

aroD

Organism
Staphylococcus aureus (strain MRSA252)
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. 3-dehydroquinate synthase (aroB)
  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 sitei703-dehydroquinateUniRule annotation1 Publication1
Active sitei133Proton donor/acceptorUniRule annotation1 Publication1
Active sitei160Schiff-base intermediate with substrateUniRule annotation1 Publication1
Binding sitei2023-dehydroquinateUniRule annotation1 Publication1
Binding sitei2253-dehydroquinateUniRule annotation1 Publication1

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:SAR0860
OrganismiStaphylococcus aureus (strain MRSA252)
Taxonomic identifieri282458 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesStaphylococcaceaeStaphylococcus

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001388111 – 2383-dehydroquinate dehydrataseAdd BLAST238

Interactioni

Subunit structurei

Homodimer.UniRule annotation1 Publication

Structurei

Secondary structure

1238
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi5 – 10Combined sources6
Helixi19 – 26Combined sources8
Turni27 – 30Combined sources4
Beta strandi32 – 37Combined sources6
Helixi46 – 56Combined sources11
Beta strandi63 – 68Combined sources6
Helixi72 – 74Combined sources3
Helixi82 – 91Combined sources10
Helixi92 – 94Combined sources3
Beta strandi100 – 104Combined sources5
Helixi111 – 123Combined sources13
Beta strandi127 – 136Combined sources10
Helixi141 – 152Combined sources12
Beta strandi157 – 163Combined sources7
Helixi168 – 184Combined sources17
Beta strandi186 – 193Combined sources8
Helixi196 – 198Combined sources3
Helixi199 – 203Combined sources5
Helixi205 – 208Combined sources4
Beta strandi212 – 218Combined sources7
Helixi228 – 235Combined sources8

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1SFJX-ray2.40A/B1-238[»]
1SFLX-ray1.90A/B1-238[»]
ProteinModelPortaliQ6GII7.
SMRiQ6GII7.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ6GII7.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni35 – 373-dehydroquinate bindingUniRule annotation3

Sequence similaritiesi

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

Phylogenomic databases

HOGENOMiHOG000105514.
KOiK03785.
OMAiLFTFRSK.

Family and domain databases

CDDicd00502. DHQase_I. 1 hit.
Gene3Di3.20.20.70. 1 hit.
HAMAPiMF_00214. AroD. 1 hit.
InterProiIPR013785. Aldolase_TIM.
IPR001381. DHquinase_I.
[Graphical view]
PfamiPF01487. DHquinase_I. 1 hit.
[Graphical view]
TIGRFAMsiTIGR01093. aroD. 1 hit.

Sequencei

Sequence statusi: Complete.

Q6GII7-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTHVEVVATI TPQLYIEETL IQKINHRIDA IDVLELRIDQ FENVTVDQVA
60 70 80 90 100
EMITKLKVMQ DSFKLLVTYR TKLQGGYGQF TNDSYLNLIS DLANINGIDM
110 120 130 140 150
IDIEWQADID IEKHQRIITH LQQYNKEVII SHHNFESTPP LDELQFIFFK
160 170 180 190 200
MQKFNPEYVK LAVMPHNKND VLNLLQAMST FSDTMDCKVV GISMSKLGLI
210 220 230
SRTAQGVFGG ALTYGCIGEP QAPGQIDVTD LKAQVTLY
Length:238
Mass (Da):27,053
Last modified:July 19, 2004 - v1
Checksum:iA88C60679FCCBCF4
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BX571856 Genomic DNA. Translation: CAG39869.1.
RefSeqiWP_000150036.1. NC_002952.2.

Genome annotation databases

EnsemblBacteriaiCAG39869; CAG39869; SAR0860.
KEGGisar:SAR0860.
PATRICi19545257. VBIStaAur71814_0861.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BX571856 Genomic DNA. Translation: CAG39869.1.
RefSeqiWP_000150036.1. NC_002952.2.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1SFJX-ray2.40A/B1-238[»]
1SFLX-ray1.90A/B1-238[»]
ProteinModelPortaliQ6GII7.
SMRiQ6GII7.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCAG39869; CAG39869; SAR0860.
KEGGisar:SAR0860.
PATRICi19545257. VBIStaAur71814_0861.

Phylogenomic databases

HOGENOMiHOG000105514.
KOiK03785.
OMAiLFTFRSK.

Enzyme and pathway databases

UniPathwayiUPA00053; UER00086.

Miscellaneous databases

EvolutionaryTraceiQ6GII7.

Family and domain databases

CDDicd00502. DHQase_I. 1 hit.
Gene3Di3.20.20.70. 1 hit.
HAMAPiMF_00214. AroD. 1 hit.
InterProiIPR013785. Aldolase_TIM.
IPR001381. DHquinase_I.
[Graphical view]
PfamiPF01487. DHquinase_I. 1 hit.
[Graphical view]
TIGRFAMsiTIGR01093. aroD. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiAROD_STAAR
AccessioniPrimary (citable) accession number: Q6GII7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 21, 2004
Last sequence update: July 19, 2004
Last modified: November 2, 2016
This is version 83 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

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.