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Protein

3-dehydroquinate synthase

Gene

aroB

Organism
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Catalytic activityi

3-deoxy-D-arabino-hept-2-ulosonate 7-phosphate = 3-dehydroquinate + phosphate.

Cofactori

Protein has several cofactor binding sites:
  • NAD+By similarity
  • Co2+By similarity, Zn2+By similarityNote: Binds 1 divalent metal cation per subunit. Can use either Co2+ or Zn2+.By similarity

Pathwayi: chorismate biosynthesis

This protein is involved in step 2 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.

GO - Molecular functioni

  • 3-dehydroquinate synthase activity Source: MTBBASE
  • copper ion binding Source: MTBBASE
  • zinc ion binding Source: MTBBASE

GO - Biological processi

  • aromatic amino acid family biosynthetic process Source: MTBBASE
  • chorismate biosynthetic process Source: GO_Central
  • growth Source: MTBBASE
Complete GO annotation...

Keywords - Molecular functioni

Lyase

Keywords - Biological processi

Amino-acid biosynthesis, Aromatic amino acid biosynthesis

Keywords - Ligandi

Cobalt, NAD, Zinc

Enzyme and pathway databases

ReactomeiR-MTU-964903. Chorismate via Shikimate Pathway.
UniPathwayiUPA00053; UER00085.

Names & Taxonomyi

Protein namesi
Recommended name:
3-dehydroquinate synthase (EC:4.2.3.4)
Gene namesi
Name:aroB
Ordered Locus Names:Rv2538c
ORF Names:MTCY159.18
OrganismiMycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Taxonomic identifieri83332 [NCBI]
Taxonomic lineageiBacteriaActinobacteriaCorynebacterialesMycobacteriaceaeMycobacteriumMycobacterium tuberculosis complex
Proteomesi
  • UP000001584 Componenti: Chromosome

Organism-specific databases

TubercuListiRv2538c.

Subcellular locationi

GO - Cellular componenti

  • cell wall Source: MTBBASE
  • cytoplasm Source: GO_Central
  • cytosol Source: Reactome
  • plasma membrane Source: MTBBASE
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 3623623-dehydroquinate synthasePRO_0000140757Add
BLAST

Proteomic databases

PaxDbiP9WPX9.

Interactioni

Subunit structurei

Monomer.By similarity

Protein-protein interaction databases

STRINGi83332.Rv2538c.

Structurei

Secondary structure

1
362
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi8 – 125Combined sources
Beta strandi14 – 163Combined sources
Beta strandi18 – 247Combined sources
Helixi27 – 348Combined sources
Beta strandi38 – 447Combined sources
Helixi46 – 483Combined sources
Helixi49 – 6113Combined sources
Beta strandi65 – 706Combined sources
Helixi74 – 785Combined sources
Helixi80 – 9314Combined sources
Beta strandi100 – 1067Combined sources
Helixi107 – 11913Combined sources
Helixi120 – 1223Combined sources
Beta strandi125 – 1306Combined sources
Helixi133 – 1375Combined sources
Turni138 – 1403Combined sources
Beta strandi144 – 1496Combined sources
Beta strandi152 – 1598Combined sources
Beta strandi163 – 1686Combined sources
Helixi169 – 1746Combined sources
Helixi177 – 19317Combined sources
Helixi196 – 2049Combined sources
Helixi206 – 2094Combined sources
Beta strandi212 – 2154Combined sources
Helixi216 – 23318Combined sources
Helixi241 – 2466Combined sources
Helixi249 – 25810Combined sources
Turni259 – 2613Combined sources
Helixi265 – 28218Combined sources
Helixi288 – 30013Combined sources
Helixi312 – 3209Combined sources
Beta strandi331 – 3377Combined sources
Beta strandi341 – 3466Combined sources
Helixi349 – 36012Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3QBDX-ray2.47A/B1-362[»]
3QBEX-ray2.07A1-362[»]
ProteinModelPortaliP9WPX9.
SMRiP9WPX9. Positions 6-361.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the dehydroquinate synthase family.Curated

Phylogenomic databases

eggNOGiENOG4105D49. Bacteria.
COG0337. LUCA.
KOiK01735.
OMAiIERSCAA.
PhylomeDBiP9WPX9.

Family and domain databases

HAMAPiMF_00110. DHQ_synthase.
InterProiIPR016037. DHQ_synth_AroB.
IPR030963. DHQ_synth_fam.
IPR030960. DHQS/DOIS.
[Graphical view]
PfamiPF01761. DHQ_synthase. 1 hit.
[Graphical view]
PIRSFiPIRSF001455. DHQ_synth. 1 hit.
TIGRFAMsiTIGR01357. aroB. 1 hit.

Sequencei

Sequence statusi: Complete.

P9WPX9-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTDIGAPVTV QVAVDPPYPV VIGTGLLDEL EDLLADRHKV AVVHQPGLAE
60 70 80 90 100
TAEEIRKRLA GKGVDAHRIE IPDAEAGKDL PVVGFIWEVL GRIGIGRKDA
110 120 130 140 150
LVSLGGGAAT DVAGFAAATW LRGVSIVHLP TTLLGMVDAA VGGKTGINTD
160 170 180 190 200
AGKNLVGAFH QPLAVLVDLA TLQTLPRDEM ICGMAEVVKA GFIADPVILD
210 220 230 240 250
LIEADPQAAL DPAGDVLPEL IRRAITVKAE VVAADEKESE LREILNYGHT
260 270 280 290 300
LGHAIERRER YRWRHGAAVS VGLVFAAELA RLAGRLDDAT AQRHRTILSS
310 320 330 340 350
LGLPVSYDPD ALPQLLEIMA GDKKTRAGVL RFVVLDGLAK PGRMVGPDPG
360
LLVTAYAGVC AP
Length:362
Mass (Da):38,119
Last modified:April 16, 2014 - v1
Checksum:iDDE0C08FFF978F1A
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti99 – 991D → N in CAA42095 (PubMed:1910148).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X59509 Genomic DNA. Translation: CAA42095.1.
AL123456 Genomic DNA. Translation: CCP45333.1.
PIRiS17768.
RefSeqiNP_217054.1. NC_000962.3.
WP_003413008.1. NZ_KK339370.1.

Genome annotation databases

EnsemblBacteriaiCCP45333; CCP45333; Rv2538c.
GeneIDi888392.
KEGGimtu:Rv2538c.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X59509 Genomic DNA. Translation: CAA42095.1.
AL123456 Genomic DNA. Translation: CCP45333.1.
PIRiS17768.
RefSeqiNP_217054.1. NC_000962.3.
WP_003413008.1. NZ_KK339370.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3QBDX-ray2.47A/B1-362[»]
3QBEX-ray2.07A1-362[»]
ProteinModelPortaliP9WPX9.
SMRiP9WPX9. Positions 6-361.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi83332.Rv2538c.

Proteomic databases

PaxDbiP9WPX9.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCCP45333; CCP45333; Rv2538c.
GeneIDi888392.
KEGGimtu:Rv2538c.

Organism-specific databases

TubercuListiRv2538c.

Phylogenomic databases

eggNOGiENOG4105D49. Bacteria.
COG0337. LUCA.
KOiK01735.
OMAiIERSCAA.
PhylomeDBiP9WPX9.

Enzyme and pathway databases

UniPathwayiUPA00053; UER00085.
ReactomeiR-MTU-964903. Chorismate via Shikimate Pathway.

Family and domain databases

HAMAPiMF_00110. DHQ_synthase.
InterProiIPR016037. DHQ_synth_AroB.
IPR030963. DHQ_synth_fam.
IPR030960. DHQS/DOIS.
[Graphical view]
PfamiPF01761. DHQ_synthase. 1 hit.
[Graphical view]
PIRSFiPIRSF001455. DHQ_synth. 1 hit.
TIGRFAMsiTIGR01357. aroB. 1 hit.
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.

Entry informationi

Entry nameiAROB_MYCTU
AccessioniPrimary (citable) accession number: P9WPX9
Secondary accession number(s): L0TCN7
, P0A4Z4, P36919, P95015
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 16, 2014
Last sequence update: April 16, 2014
Last modified: February 17, 2016
This is version 19 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.