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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
  • cellular amino acid biosynthetic process Source: UniProtKB-KW
  • 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

BioCyciMTBH37RV:G185E-6777-MONOMER.
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)DescriptionActionsGraphical viewLength
ChainiPRO_00001407571 – 3623-dehydroquinate synthaseAdd BLAST362

Proteomic databases

PaxDbiP9WPX9.

Interactioni

Subunit structurei

Monomer.By similarity

Protein-protein interaction databases

STRINGi83332.Rv2538c.

Structurei

Secondary structure

1362
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi8 – 12Combined sources5
Beta strandi14 – 16Combined sources3
Beta strandi18 – 24Combined sources7
Helixi27 – 34Combined sources8
Beta strandi38 – 44Combined sources7
Helixi46 – 48Combined sources3
Helixi49 – 61Combined sources13
Beta strandi65 – 70Combined sources6
Helixi74 – 78Combined sources5
Helixi80 – 93Combined sources14
Beta strandi100 – 106Combined sources7
Helixi107 – 119Combined sources13
Helixi120 – 122Combined sources3
Beta strandi125 – 130Combined sources6
Helixi133 – 137Combined sources5
Turni138 – 140Combined sources3
Beta strandi144 – 149Combined sources6
Beta strandi152 – 159Combined sources8
Beta strandi163 – 168Combined sources6
Helixi169 – 174Combined sources6
Helixi177 – 193Combined sources17
Helixi196 – 204Combined sources9
Helixi206 – 209Combined sources4
Beta strandi212 – 215Combined sources4
Helixi216 – 233Combined sources18
Helixi241 – 246Combined sources6
Helixi249 – 258Combined sources10
Turni259 – 261Combined sources3
Helixi265 – 282Combined sources18
Helixi288 – 300Combined sources13
Helixi312 – 320Combined sources9
Beta strandi331 – 337Combined sources7
Beta strandi341 – 346Combined sources6
Helixi349 – 360Combined sources12

3D structure databases

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

Family & Domainsi

Sequence similaritiesi

Belongs to the dehydroquinate synthase family.Curated

Phylogenomic databases

eggNOGiENOG4105D49. Bacteria.
COG0337. LUCA.
KOiK01735.
OMAiTHLGYGN.
PhylomeDBiP9WPX9.

Family and domain databases

HAMAPiMF_00110. DHQ_synthase. 1 hit.
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)DescriptionActionsGraphical viewLength
Sequence conflicti99D → N in CAA42095 (PubMed:1910148).Curated1

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
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3QBDX-ray2.47A/B1-362[»]
3QBEX-ray2.07A1-362[»]
ProteinModelPortaliP9WPX9.
SMRiP9WPX9.
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.
OMAiTHLGYGN.
PhylomeDBiP9WPX9.

Enzyme and pathway databases

UniPathwayiUPA00053; UER00085.
BioCyciMTBH37RV:G185E-6777-MONOMER.
ReactomeiR-MTU-964903. Chorismate via Shikimate Pathway.

Family and domain databases

HAMAPiMF_00110. DHQ_synthase. 1 hit.
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...

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: November 2, 2016
This is version 22 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.