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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)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei70 – 7013-dehydroquinateUniRule annotation1 Publication
Active sitei133 – 1331Proton donor/acceptorUniRule annotation1 Publication
Active sitei160 – 1601Schiff-base intermediate with substrateUniRule annotation1 Publication
Binding sitei202 – 20213-dehydroquinateUniRule annotation1 Publication
Binding sitei225 – 22513-dehydroquinateUniRule annotation1 Publication

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

BioCyciSAUR282458:GJA5-863-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:SAR0860
OrganismiStaphylococcus aureus (strain MRSA252)
Taxonomic identifieri282458 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesStaphylococcaceaeStaphylococcus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 2382383-dehydroquinate dehydratasePRO_0000138811Add
BLAST

Interactioni

Subunit structurei

Homodimer.UniRule annotation1 Publication

Structurei

Secondary structure

1
238
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi5 – 106Combined sources
Helixi19 – 268Combined sources
Turni27 – 304Combined sources
Beta strandi32 – 376Combined sources
Helixi46 – 5611Combined sources
Beta strandi63 – 686Combined sources
Helixi72 – 743Combined sources
Helixi82 – 9110Combined sources
Helixi92 – 943Combined sources
Beta strandi100 – 1045Combined sources
Helixi111 – 12313Combined sources
Beta strandi127 – 13610Combined sources
Helixi141 – 15212Combined sources
Beta strandi157 – 1637Combined sources
Helixi168 – 18417Combined sources
Beta strandi186 – 1938Combined sources
Helixi196 – 1983Combined sources
Helixi199 – 2035Combined sources
Helixi205 – 2084Combined sources
Beta strandi212 – 2187Combined sources
Helixi228 – 2358Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1SFJX-ray2.40A/B1-238[»]
1SFLX-ray1.90A/B1-238[»]
ProteinModelPortaliQ6GII7.
SMRiQ6GII7. Positions 3-238.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ6GII7.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni35 – 3733-dehydroquinate bindingUniRule annotation

Sequence similaritiesi

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

Phylogenomic databases

HOGENOMiHOG000105514.
KOiK03785.
OMAiLFTFRSK.
OrthoDBiEOG6P33BK.

Family and domain databases

Gene3Di3.20.20.70. 1 hit.
HAMAPiMF_00214. AroD.
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
EntryMethodResolution (Å)ChainPositionsPDBsum
1SFJX-ray2.40A/B1-238[»]
1SFLX-ray1.90A/B1-238[»]
ProteinModelPortaliQ6GII7.
SMRiQ6GII7. Positions 3-238.
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.
OrthoDBiEOG6P33BK.

Enzyme and pathway databases

UniPathwayiUPA00053; UER00086.
BioCyciSAUR282458:GJA5-863-MONOMER.

Miscellaneous databases

EvolutionaryTraceiQ6GII7.

Family and domain databases

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

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: MRSA252.
  2. "Crystal structures of Staphylococcus aureus type I dehydroquinase from enzyme turnover experiments."
    Nichols C.E., Lockyer M., Hawkins A.R., Stammers D.K.
    Proteins 56:625-628(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.40 ANGSTROMS) IN COMPLEX WITH 3-DEHYDROSHIKIMATE, ACTIVE SITE, SUBUNIT.
    Strain: MRSA252.

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: March 16, 2016
This is version 80 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.