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Protein

3-dehydroquinate dehydratase

Gene

aroQ

Organism
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes a trans-dehydration via an enolate intermediate.By similarity

Catalytic activityi

3-dehydroquinate = 3-dehydroshikimate + H2O.

Pathwayi: chorismate biosynthesis

This protein is involved in step 3 of the subpathway that synthesizes chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate.
Proteins known to be involved in the 7 steps of the subpathway in this organism are:
  1. Phospho-2-dehydro-3-deoxyheptonate aldolase AroG (aroG)
  2. 3-dehydroquinate synthase (LH57_13905), 3-dehydroquinate synthase (aroB)
  3. 3-dehydroquinate dehydratase (aroQ)
  4. no protein annotated in this organism
  5. Shikimate kinase (aroK), Shikimate kinase (LH57_13910)
  6. 3-phosphoshikimate 1-carboxyvinyltransferase (aroA), 3-phosphoshikimate 1-carboxyvinyltransferase (LH57_17660)
  7. Chorismate synthase (aroC), Chorismate synthase (LH57_13915)
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
Sitei20 – 201Transition state stabilizer
Active sitei25 – 251Proton acceptor
Binding sitei76 – 761Substrate
Binding sitei82 – 821Substrate
Binding sitei89 – 891Substrate
Active sitei102 – 1021Proton donor
Binding sitei113 – 1131Substrate

GO - Molecular functioni

  • 3-dehydroquinate dehydratase activity Source: MTBBASE

GO - Biological processi

  • aromatic amino acid family biosynthetic process Source: UniProtKB-HAMAP
  • chorismate biosynthetic process Source: Reactome
  • growth Source: MTBBASE
Complete GO annotation...

Keywords - Molecular functioni

Lyase

Keywords - Biological processi

Amino-acid biosynthesis, Aromatic amino acid biosynthesis

Enzyme and pathway databases

ReactomeiR-MTU-964903. Chorismate via Shikimate Pathway.
UniPathwayiUPA00053; UER00086.

Names & Taxonomyi

Protein namesi
Recommended name:
3-dehydroquinate dehydratase (EC:4.2.1.10)
Short name:
3-dehydroquinase
Alternative name(s):
Type II DHQase
Gene namesi
Name:aroQ
Synonyms:aroD
Ordered Locus Names:Rv2537c
ORF Names:MTCY159.19
OrganismiMycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Taxonomic identifieri83332 [NCBI]
Taxonomic lineageiBacteriaActinobacteriaCorynebacterialesMycobacteriaceaeMycobacteriumMycobacterium tuberculosis complex
Proteomesi
  • UP000001584 Componenti: Chromosome

Organism-specific databases

TubercuListiRv2537c.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Pathology & Biotechi

Chemistry

ChEMBLiCHEMBL3345.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 1471473-dehydroquinate dehydratasePRO_0000159910Add
BLAST

Proteomic databases

PaxDbiP9WPX7.

Interactioni

Subunit structurei

Homododecamer.3 Publications

Protein-protein interaction databases

STRINGi83332.Rv2537c.

Chemistry

BindingDBiP9WPX7.

Structurei

Secondary structure

147
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Turni1 – 33Combined sources
Beta strandi5 – 106Combined sources
Helixi14 – 163Combined sources
Turni17 – 193Combined sources
Turni23 – 253Combined sources
Beta strandi26 – 283Combined sources
Helixi30 – 4314Combined sources
Beta strandi47 – 526Combined sources
Helixi56 – 6914Combined sources
Beta strandi73 – 764Combined sources
Helixi78 – 825Combined sources
Helixi85 – 928Combined sources
Beta strandi98 – 1047Combined sources
Helixi106 – 1083Combined sources
Helixi111 – 1144Combined sources
Helixi119 – 1213Combined sources
Beta strandi122 – 1298Combined sources
Helixi132 – 14312Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1H05X-ray1.50A2-147[»]
1H0RX-ray2.10A2-147[»]
1H0SX-ray1.70A2-147[»]
2DHQX-ray2.00A2-147[»]
2XB8X-ray2.40A2-147[»]
2Y71X-ray1.50A2-147[»]
2Y76X-ray2.50A2-147[»]
2Y77X-ray1.50A2-147[»]
3N59X-ray2.52A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T/U/V/W/X1-147[»]
3N76X-ray1.90A1-147[»]
3N7AX-ray2.00A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T/U/V/W/X1-147[»]
3N86X-ray1.90A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T/U/V/W/X1-147[»]
3N87X-ray2.40A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T/U/V/W/X1-147[»]
3N8KX-ray2.25A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T/U/V/W/X1-147[»]
3N8NX-ray2.50A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T/U/V/W/X1-147[»]
4B6OX-ray2.00A2-147[»]
4B6PX-ray2.30A2-147[»]
4B6QX-ray1.54A2-147[»]
4CIVX-ray2.90A2-147[»]
4CIWX-ray2.20A2-147[»]
4CIXX-ray2.90A2-147[»]
4CIYX-ray2.10A2-147[»]
4CKWX-ray2.70A/B/C/D2-147[»]
4CKXX-ray2.60A2-147[»]
4CKYX-ray1.65A2-147[»]
4CKZX-ray2.52A/B2-147[»]
4CL0X-ray3.10A2-147[»]
4KI7X-ray2.80A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T/U/V/W/X1-147[»]
4KIJX-ray2.80A1-147[»]
4KIUX-ray2.40A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T/U/V/W/X1-147[»]
4KIWX-ray2.57A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T/U/V/W/X1-147[»]
4V0SX-ray1.55A/B2-147[»]
ProteinModelPortaliP9WPX7.
SMRiP9WPX7. Positions 1-144.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni103 – 1042Substrate binding

Sequence similaritiesi

Belongs to the type-II 3-dehydroquinase family.Curated

Phylogenomic databases

eggNOGiENOG4108Z38. Bacteria.
COG0757. LUCA.
KOiK03786.
OMAiIPTIEVH.
PhylomeDBiP9WPX7.

Family and domain databases

Gene3Di3.40.50.9100. 1 hit.
HAMAPiMF_00169. AroQ.
InterProiIPR001874. DHquinase_II.
IPR018509. DHquinase_II_CS.
[Graphical view]
PANTHERiPTHR21272. PTHR21272. 1 hit.
PfamiPF01220. DHquinase_II. 1 hit.
[Graphical view]
PIRSFiPIRSF001399. DHquinase_II. 1 hit.
ProDomiPD004527. DHquinase_II. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SUPFAMiSSF52304. SSF52304. 1 hit.
TIGRFAMsiTIGR01088. aroQ. 1 hit.
PROSITEiPS01029. DEHYDROQUINASE_II. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P9WPX7-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSELIVNVIN GPNLGRLGRR EPAVYGGTTH DELVALIERE AAELGLKAVV
60 70 80 90 100
RQSDSEAQLL DWIHQAADAA EPVILNAGGL THTSVALRDA CAELSAPLIE
110 120 130 140
VHISNVHARE EFRRHSYLSP IATGVIVGLG IQGYLLALRY LAEHVGT
Length:147
Mass (Da):15,790
Last modified:April 16, 2014 - v1
Checksum:i9EE0E1B14B4DB5F6
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti117 – 1171Y → I in CAA42096 (PubMed:1910148).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X59509 Genomic DNA. Translation: CAA42096.1.
AL123456 Genomic DNA. Translation: CCP45332.1.
PIRiE70658.
RefSeqiNP_217053.1. NC_000962.3.
WP_003413001.1. NZ_KK339370.1.

Genome annotation databases

EnsemblBacteriaiCCP45332; CCP45332; Rv2537c.
GeneIDi888397.
KEGGimtu:Rv2537c.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X59509 Genomic DNA. Translation: CAA42096.1.
AL123456 Genomic DNA. Translation: CCP45332.1.
PIRiE70658.
RefSeqiNP_217053.1. NC_000962.3.
WP_003413001.1. NZ_KK339370.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1H05X-ray1.50A2-147[»]
1H0RX-ray2.10A2-147[»]
1H0SX-ray1.70A2-147[»]
2DHQX-ray2.00A2-147[»]
2XB8X-ray2.40A2-147[»]
2Y71X-ray1.50A2-147[»]
2Y76X-ray2.50A2-147[»]
2Y77X-ray1.50A2-147[»]
3N59X-ray2.52A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T/U/V/W/X1-147[»]
3N76X-ray1.90A1-147[»]
3N7AX-ray2.00A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T/U/V/W/X1-147[»]
3N86X-ray1.90A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T/U/V/W/X1-147[»]
3N87X-ray2.40A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T/U/V/W/X1-147[»]
3N8KX-ray2.25A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T/U/V/W/X1-147[»]
3N8NX-ray2.50A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T/U/V/W/X1-147[»]
4B6OX-ray2.00A2-147[»]
4B6PX-ray2.30A2-147[»]
4B6QX-ray1.54A2-147[»]
4CIVX-ray2.90A2-147[»]
4CIWX-ray2.20A2-147[»]
4CIXX-ray2.90A2-147[»]
4CIYX-ray2.10A2-147[»]
4CKWX-ray2.70A/B/C/D2-147[»]
4CKXX-ray2.60A2-147[»]
4CKYX-ray1.65A2-147[»]
4CKZX-ray2.52A/B2-147[»]
4CL0X-ray3.10A2-147[»]
4KI7X-ray2.80A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T/U/V/W/X1-147[»]
4KIJX-ray2.80A1-147[»]
4KIUX-ray2.40A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T/U/V/W/X1-147[»]
4KIWX-ray2.57A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T/U/V/W/X1-147[»]
4V0SX-ray1.55A/B2-147[»]
ProteinModelPortaliP9WPX7.
SMRiP9WPX7. Positions 1-144.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi83332.Rv2537c.

Chemistry

BindingDBiP9WPX7.
ChEMBLiCHEMBL3345.

Proteomic databases

PaxDbiP9WPX7.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCCP45332; CCP45332; Rv2537c.
GeneIDi888397.
KEGGimtu:Rv2537c.

Organism-specific databases

TubercuListiRv2537c.

Phylogenomic databases

eggNOGiENOG4108Z38. Bacteria.
COG0757. LUCA.
KOiK03786.
OMAiIPTIEVH.
PhylomeDBiP9WPX7.

Enzyme and pathway databases

UniPathwayiUPA00053; UER00086.
ReactomeiR-MTU-964903. Chorismate via Shikimate Pathway.

Family and domain databases

Gene3Di3.40.50.9100. 1 hit.
HAMAPiMF_00169. AroQ.
InterProiIPR001874. DHquinase_II.
IPR018509. DHquinase_II_CS.
[Graphical view]
PANTHERiPTHR21272. PTHR21272. 1 hit.
PfamiPF01220. DHquinase_II. 1 hit.
[Graphical view]
PIRSFiPIRSF001399. DHquinase_II. 1 hit.
ProDomiPD004527. DHquinase_II. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SUPFAMiSSF52304. SSF52304. 1 hit.
TIGRFAMsiTIGR01088. aroQ. 1 hit.
PROSITEiPS01029. DEHYDROQUINASE_II. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The Mycobacterium tuberculosis shikimate pathway genes: evolutionary relationship between biosynthetic and catabolic 3-dehydroquinases."
    Garbe T., Servos S., Hawkins A., Dimitriadis G., Young D., Dougan G., Charles I.G.
    Mol. Gen. Genet. 228:385-392(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 25618 / H37Rv.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 25618 / H37Rv.
  3. "targetTB: a target identification pipeline for Mycobacterium tuberculosis through an interactome, reactome and genome-scale structural analysis."
    Raman K., Yeturu K., Chandra N.
    BMC Syst. Biol. 2:109-109(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION AS A DRUG TARGET [LARGE SCALE ANALYSIS].
  4. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Strain: ATCC 25618 / H37Rv.
  5. "The two types of 3-dehydroquinase have distinct structures but catalyze the same overall reaction."
    Gourley D.G., Shrive A.K., Polikarpov I., Krell T., Coggins J.R., Hawkins A.R., Isaacs N.W., Sawyer L.
    Nat. Struct. Biol. 6:521-525(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS), SUBUNIT.
  6. "Specificity of substrate recognition by type II dehydroquinases as revealed by binding of polyanions."
    Evans L.D., Roszak A.W., Noble L.J., Robinson D.A., Chalk P.A., Matthews J.L., Coggins J.R., Price N.C., Lapthorn A.J.
    FEBS Lett. 530:24-30(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) IN COMPLEX WITH POLYANION.
  7. "Structural basis for specificity of oxime based inhibitors towards type II dehydroquinase from Mycobacterium tuberculosis."
    Robinson D.A., Roszak A.W., Frederickson M., Abell C., Coggins J.R., Lapthorn A.J.
    Submitted (MAY-2004) to the PDB data bank
    Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) IN COMPLEX WITH SUBSTRATE ANALOGS.

Entry informationi

Entry nameiAROQ_MYCTU
AccessioniPrimary (citable) accession number: P9WPX7
Secondary accession number(s): L0TCT6
, P0A4Z6, P36918, P95016
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 16, 2014
Last sequence update: April 16, 2014
Last modified: March 16, 2016
This is version 20 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Miscellaneous

Was identified as a high-confidence drug target.

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Mycobacterium tuberculosis strains ATCC 25618 / H37Rv and CDC 1551 / Oshkosh
    Mycobacterium tuberculosis strains ATCC 25618 / H37Rv and CDC 1551 / Oshkosh: entries and gene names
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. 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.