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Protein

3-dehydroquinate synthase

Gene

aroB

Organism
Bacillus licheniformis (strain ATCC 14580 / DSM 13 / JCM 2505 / NBRC 12200 / NCIMB 9375 / NRRL NRS-1264 / Gibson 46)
Status
Reviewed-Annotation score: -Protein inferred from homologyi

Functioni

Catalyzes the conversion of 3-deoxy-D-arabino-heptulosonate 7-phosphate (DAHP) to dehydroquinate (DHQ).UniRule annotation

Catalytic activityi

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

Cofactori

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

Pathwayi: chorismate biosynthesis

This protein is involved in step 2 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. no protein annotated in this organism
  2. 3-dehydroquinate synthase (aroB)
  3. 3-dehydroquinate dehydratase (aroD), 3-dehydroquinate dehydratase (aroQ)
  4. Shikimate dehydrogenase (NADP(+)) (aroE)
  5. Shikimate kinase (aroK)
  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)DescriptionActionsGraphical viewLength
Binding sitei142NAD; via carbonyl oxygenUniRule annotation1
Binding sitei151NADUniRule annotation1
Metal bindingi184Cobalt or zincUniRule annotation1
Metal bindingi246Cobalt or zinc; via tele nitrogenUniRule annotation1
Metal bindingi263Cobalt or zinc; via tele nitrogenUniRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi72 – 77NADUniRule annotation6
Nucleotide bindingi106 – 110NADUniRule annotation5
Nucleotide bindingi130 – 131NADUniRule annotation2
Nucleotide bindingi169 – 172NADUniRule annotation4

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionLyase
Biological processAmino-acid biosynthesis, Aromatic amino acid biosynthesis
LigandCobalt, Metal-binding, NAD, Nucleotide-binding, Zinc

Enzyme and pathway databases

UniPathwayiUPA00053; UER00085

Names & Taxonomyi

Protein namesi
Recommended name:
3-dehydroquinate synthaseUniRule annotation (EC:4.2.3.4UniRule annotation)
Short name:
DHQSUniRule annotation
Gene namesi
Name:aroBUniRule annotation
Ordered Locus Names:BLi02405, BL02777
OrganismiBacillus licheniformis (strain ATCC 14580 / DSM 13 / JCM 2505 / NBRC 12200 / NCIMB 9375 / NRRL NRS-1264 / Gibson 46)
Taxonomic identifieri279010 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus
Proteomesi
  • UP000000606 Componenti: Chromosome

Subcellular locationi

  • Cytoplasm UniRule annotation

GO - Cellular componenti

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002310661 – 3623-dehydroquinate synthaseAdd BLAST362

Proteomic databases

PRIDEiQ65I29

Interactioni

Protein-protein interaction databases

STRINGi279010.BLi02405

Structurei

3D structure databases

ProteinModelPortaliQ65I29
SMRiQ65I29
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the sugar phosphate cyclases superfamily. Dehydroquinate synthase family.UniRule annotation

Phylogenomic databases

eggNOGiENOG4105D49 Bacteria
COG0337 LUCA
HOGENOMiHOG000007970
KOiK01735
OMAiCGFIADP

Family and domain databases

HAMAPiMF_00110 DHQ_synthase, 1 hit
InterProiView protein in InterPro
IPR016037 DHQ_synth_AroB
IPR030963 DHQ_synth_fam
IPR030960 DHQS/DOIS
PfamiView protein in Pfam
PF01761 DHQ_synthase, 1 hit
PIRSFiPIRSF001455 DHQ_synth, 1 hit
TIGRFAMsiTIGR01357 aroB, 1 hit

Sequencei

Sequence statusi: Complete.

Q65I29-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKSLQIETAS LSYPVFIGGG IRKNAAELLS SLNLPMTKLL LITDEEVDKR
60 70 80 90 100
YGEELFSLLR SKWPVKKVAV PSGEQAKSID MFMKLQTEAI QFHLDRSSCI
110 120 130 140 150
VALGGGVVGD LAGFVASTFM RGIDYVQFPT TLLSHDSAVG GKVAINHPLG
160 170 180 190 200
KNLIGAFHQP KAVVYDTECL STLPEKEMRS GLAEVIKHAF IRDESFLNEL
210 220 230 240 250
LKLDSIEAIT TGQLSEMVYK GISIKAEVVS QDEREQGIRA YLNFGHTLGH
260 270 280 290 300
AVEAEYGYGE ITHGDAVALG MQFALFVSEK VLNCPVDRTK IAAWLKNLGY
310 320 330 340 350
PESVKREVST EALIYRMMND KKTRGGIIQF VLLDKIGSVR LHSFKAEEIE
360
RWLNMWRLEG DK
Length:362
Mass (Da):40,201
Last modified:October 25, 2004 - v1
Checksum:i634A636825C01656
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE017333 Genomic DNA Translation: AAU41285.1
CP000002 Genomic DNA Translation: AAU23931.2
RefSeqiWP_011198071.1, NC_006322.1

Genome annotation databases

EnsemblBacteriaiAAU23931; AAU23931; BL02777
AAU41285; AAU41285; BLi02405
GeneIDi3029357
KEGGibld:BLi02405
bli:BL02777

Similar proteinsi

Entry informationi

Entry nameiAROB_BACLD
AccessioniPrimary (citable) accession number: Q65I29
Secondary accession number(s): Q62TH8
Entry historyiIntegrated into UniProtKB/Swiss-Prot: April 4, 2006
Last sequence update: October 25, 2004
Last modified: May 23, 2018
This is version 93 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

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

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