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Protein

3-dehydroquinate dehydratase

Gene

aroD

Organism
Streptococcus pyogenes serotype M1
Status
Reviewed-Annotation score: Annotation score: 3 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 sitei623-dehydroquinateUniRule annotation1
Active sitei118Proton donor/acceptorUniRule annotation1
Active sitei143Schiff-base intermediate with substrateUniRule annotation1
Binding sitei1863-dehydroquinateUniRule annotation1
Binding sitei2053-dehydroquinateUniRule annotation1
Binding sitei2093-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:SPy_0809, M5005_Spy0624
OrganismiStreptococcus pyogenes serotype M1
Taxonomic identifieri301447 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliLactobacillalesStreptococcaceaeStreptococcus
Proteomesi
  • UP000000750 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001388181 – 2283-dehydroquinate dehydrataseAdd BLAST228

Proteomic databases

PaxDbiP63590.
PRIDEiP63590.

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Protein-protein interaction databases

STRINGi160490.SPy_0809.

Structurei

Secondary structure

1228
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi2 – 7Combined sources6
Helixi12 – 16Combined sources5
Helixi20 – 23Combined sources4
Beta strandi27 – 32Combined sources6
Helixi33 – 35Combined sources3
Helixi38 – 40Combined sources3
Helixi41 – 51Combined sources11
Turni52 – 54Combined sources3
Beta strandi55 – 60Combined sources6
Helixi64 – 66Combined sources3
Helixi74 – 88Combined sources15
Beta strandi91 – 96Combined sources6
Turni97 – 100Combined sources4
Helixi101 – 107Combined sources7
Beta strandi111 – 121Combined sources11
Helixi127 – 136Combined sources10
Beta strandi140 – 146Combined sources7
Helixi151 – 167Combined sources17
Beta strandi172 – 177Combined sources6
Helixi179 – 182Combined sources4
Helixi183 – 187Combined sources5
Helixi189 – 192Combined sources4
Beta strandi196 – 198Combined sources3
Helixi212 – 222Combined sources11

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2OCZX-ray1.85A1-228[»]
ProteinModelPortaliP63590.
SMRiP63590.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP63590.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni30 – 323-dehydroquinate bindingUniRule annotation3

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiENOG4105FF2. Bacteria.
COG0710. LUCA.
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.

P63590-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MRIVAPVMPR HFDEAQAIDI SKYEDVNLIE WRADFLPKDE IVAVAPAIFE
60 70 80 90 100
KFAGKEIIFT LRTVQEGGNI TLSSQEYVDI IKEINAIYNP DYIDFEYFTH
110 120 130 140 150
KSVFQEMLDF PNLILSYHNF EETPENLMEA FSEMTKLAPR VVKIAVMPQS
160 170 180 190 200
EQDVLDLMNY TRGFKTLNPE QEFATISMGK LGRLSRFAGD VIGSSWTYVS
210 220
LDHVSGPGQV TLNDMKRIIE VLEMDISN
Length:228
Mass (Da):26,101
Last modified:October 11, 2004 - v1
Checksum:iC1E41938E1A2E424
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE004092 Genomic DNA. Translation: AAK33746.1.
CP000017 Genomic DNA. Translation: AAZ51242.1.
RefSeqiNP_269025.1. NC_002737.2.

Genome annotation databases

EnsemblBacteriaiAAK33746; AAK33746; SPy_0809.
AAZ51242; AAZ51242; M5005_Spy0624.
GeneIDi900982.
KEGGispy:SPy_0809.
spz:M5005_Spy0624.
PATRICi19715248. VBIStrPyo79812_0692.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE004092 Genomic DNA. Translation: AAK33746.1.
CP000017 Genomic DNA. Translation: AAZ51242.1.
RefSeqiNP_269025.1. NC_002737.2.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2OCZX-ray1.85A1-228[»]
ProteinModelPortaliP63590.
SMRiP63590.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi160490.SPy_0809.

Proteomic databases

PaxDbiP63590.
PRIDEiP63590.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAK33746; AAK33746; SPy_0809.
AAZ51242; AAZ51242; M5005_Spy0624.
GeneIDi900982.
KEGGispy:SPy_0809.
spz:M5005_Spy0624.
PATRICi19715248. VBIStrPyo79812_0692.

Phylogenomic databases

eggNOGiENOG4105FF2. Bacteria.
COG0710. LUCA.
HOGENOMiHOG000105514.
KOiK03785.
OMAiLFTFRSK.

Enzyme and pathway databases

UniPathwayiUPA00053; UER00086.

Miscellaneous databases

EvolutionaryTraceiP63590.

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_STRP1
AccessioniPrimary (citable) accession number: P63590
Secondary accession number(s): Q48ZH6, Q9A0E5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 11, 2004
Last sequence update: October 11, 2004
Last modified: November 2, 2016
This is version 87 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.