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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 (LH57_11870), Phospho-2-dehydro-3-deoxyheptonate aldolase AroG (aroG)
  2. 3-dehydroquinate synthase (aroB), 3-dehydroquinate synthase (aroB)
  3. 3-dehydroquinate dehydratase (aroQ), 3-dehydroquinate dehydratase (aroQ)
  4. no protein annotated in this organism
  5. Shikimate kinase (aroK), Shikimate kinase (aroK)
  6. 3-phosphoshikimate 1-carboxyvinyltransferase (aroA), 3-phosphoshikimate 1-carboxyvinyltransferase (aroA)
  7. Chorismate synthase (aroC), 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
Sitei20Transition state stabilizer1
Active sitei25Proton acceptor1
Binding sitei76Substrate1
Binding sitei82Substrate1
Binding sitei89Substrate1
Active sitei102Proton donor1
Binding sitei113Substrate1

GO - Molecular functioni

  • 3-dehydroquinate dehydratase activity Source: MTBBASE

GO - Biological processi

  • aromatic amino acid family biosynthetic process Source: UniProtKB-HAMAP
  • cellular amino acid biosynthetic process Source: UniProtKB-KW
  • 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

BioCyciMTBH37RV:G185E-6776-MONOMER.
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 databases

ChEMBLiCHEMBL3345.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001599101 – 1473-dehydroquinate dehydrataseAdd BLAST147

Proteomic databases

PaxDbiP9WPX7.

Interactioni

Subunit structurei

Homododecamer.3 Publications

Protein-protein interaction databases

STRINGi83332.Rv2537c.

Chemistry databases

BindingDBiP9WPX7.

Structurei

Secondary structure

1147
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Turni1 – 3Combined sources3
Beta strandi5 – 10Combined sources6
Helixi14 – 16Combined sources3
Turni17 – 19Combined sources3
Turni23 – 25Combined sources3
Beta strandi26 – 28Combined sources3
Helixi30 – 43Combined sources14
Beta strandi47 – 52Combined sources6
Helixi56 – 69Combined sources14
Beta strandi73 – 76Combined sources4
Helixi78 – 82Combined sources5
Helixi85 – 92Combined sources8
Beta strandi98 – 104Combined sources7
Helixi106 – 108Combined sources3
Helixi111 – 114Combined sources4
Helixi119 – 121Combined sources3
Beta strandi122 – 129Combined sources8
Helixi132 – 143Combined sources12

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni103 – 104Substrate binding2

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiENOG4108Z38. Bacteria.
COG0757. LUCA.
KOiK03786.
OMAiRREPGHY.
PhylomeDBiP9WPX7.

Family and domain databases

CDDicd00466. DHQase_II. 1 hit.
Gene3Di3.40.50.9100. 1 hit.
HAMAPiMF_00169. AroQ. 1 hit.
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)DescriptionActionsGraphical viewLength
Sequence conflicti117Y → I in CAA42096 (PubMed:1910148).Curated1

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
PDB 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.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi83332.Rv2537c.

Chemistry databases

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.
OMAiRREPGHY.
PhylomeDBiP9WPX7.

Enzyme and pathway databases

UniPathwayiUPA00053; UER00086.
BioCyciMTBH37RV:G185E-6776-MONOMER.
ReactomeiR-MTU-964903. Chorismate via Shikimate Pathway.

Miscellaneous databases

PROiP9WPX7.

Family and domain databases

CDDicd00466. DHQase_II. 1 hit.
Gene3Di3.40.50.9100. 1 hit.
HAMAPiMF_00169. AroQ. 1 hit.
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...

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: November 2, 2016
This is version 24 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.