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Protein

3-dehydroquinate dehydratase

Gene

aroD

Organism
Shigella boydii serotype 4 (strain Sb227)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Protein inferred from homologyi

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

Pathway: 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. Phospho-2-dehydro-3-deoxyheptonate aldolase (aroF), Phospho-2-dehydro-3-deoxyheptonate aldolase (aroH), Phospho-2-dehydro-3-deoxyheptonate aldolase (aroG)
  2. 3-dehydroquinate synthase (aroB)
  3. 3-dehydroquinate dehydratase (aroD)
  4. Quinate/shikimate dehydrogenase (ydiB), Shikimate dehydrogenase (NADP(+)) (aroE)
  5. Shikimate kinase 1 (aroK), Shikimate kinase 2 (aroL)
  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 sitei21 – 2113-dehydroquinateUniRule annotation
Binding sitei82 – 8213-dehydroquinateUniRule annotation
Active sitei143 – 1431Proton donor/acceptorUniRule annotation
Active sitei170 – 1701Schiff-base intermediate with substrateUniRule annotation
Binding sitei213 – 21313-dehydroquinateUniRule annotation
Binding sitei232 – 23213-dehydroquinateUniRule annotation
Binding sitei236 – 23613-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

BioCyciSBOY300268:GJFL-1435-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:SBO_1438
OrganismiShigella boydii serotype 4 (strain Sb227)
Taxonomic identifieri300268 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeShigella
ProteomesiUP000007067 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 2522523-dehydroquinate dehydratasePRO_1000043180Add
BLAST

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Structurei

3D structure databases

ProteinModelPortaliQ321F0.
SMRiQ321F0. Positions 1-252.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni46 – 4833-dehydroquinate bindingUniRule annotation

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiCOG0710.
HOGENOMiHOG000105514.
KOiK03785.
OMAiLFTFRSK.
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.

Q321F0-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKTVTVKDLV IGTGAPKIIV SLMAKDIARV KSEALAYREA DFDILEWRVD
60 70 80 90 100
HFADLSNVES VMAAAKILRE TMPEKPLLFT FRSAKEGGEQ AISTEAYIAL
110 120 130 140 150
NRAAIDSGLV DMIDLELFTG DDQVKETVAC AHAHDVKVVM SNHDFHKTPE
160 170 180 190 200
AEEIIARLRK MQSFDADIPK IALMPQSTSD VLTLLAATLE MQEQYADRPI
210 220 230 240 250
ITMSMAKTGV ISRLAGEVFG SAATFGAVKK ASAPGQISVN DLRTVLTILH

QA
Length:252
Mass (Da):27,460
Last modified:December 6, 2005 - v1
Checksum:i144849291EB9004B
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000036 Genomic DNA. Translation: ABB66058.1.
RefSeqiWP_000860174.1. NC_007613.1.
YP_407886.1. NC_007613.1.

Genome annotation databases

EnsemblBacteriaiABB66058; ABB66058; SBO_1438.
KEGGisbo:SBO_1438.
PATRICi18681872. VBIShiBoy33460_1871.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000036 Genomic DNA. Translation: ABB66058.1.
RefSeqiWP_000860174.1. NC_007613.1.
YP_407886.1. NC_007613.1.

3D structure databases

ProteinModelPortaliQ321F0.
SMRiQ321F0. Positions 1-252.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiABB66058; ABB66058; SBO_1438.
KEGGisbo:SBO_1438.
PATRICi18681872. VBIShiBoy33460_1871.

Phylogenomic databases

eggNOGiCOG0710.
HOGENOMiHOG000105514.
KOiK03785.
OMAiLFTFRSK.
OrthoDBiEOG6P33BK.

Enzyme and pathway databases

UniPathwayiUPA00053; UER00086.
BioCyciSBOY300268:GJFL-1435-MONOMER.

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

  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Sb227.

Entry informationi

Entry nameiAROD_SHIBS
AccessioniPrimary (citable) accession number: Q321F0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: December 6, 2005
Last modified: June 24, 2015
This is version 59 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

Complete proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.