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P58687 (AROD_SALTY) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 89. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
3-dehydroquinate dehydratase

Short name=3-dehydroquinase
EC=4.2.1.10
Alternative name(s):
Type I DHQase
Gene names
Name:aroD
Ordered Locus Names:STM1358
OrganismSalmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) [Reference proteome] [HAMAP]
Taxonomic identifier99287 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeSalmonella

Protein attributes

Sequence length252 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Catalytic activity

3-dehydroquinate = 3-dehydroshikimate + H2O. Ref.3 Ref.4

Pathway

Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 3/7. HAMAP-Rule MF_00214

Subunit structure

Homodimer. Ref.3 Ref.4

Sequence similarities

Belongs to the type-I 3-dehydroquinase family.

Ontologies

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 2522523-dehydroquinate dehydratase HAMAP-Rule MF_00214
PRO_0000138806

Regions

Region46 – 483Substrate binding HAMAP-Rule MF_00214

Sites

Active site1431Proton donor/acceptor Ref.2 Ref.3 Ref.4
Active site1701Schiff-base intermediate with substrate Ref.2 Ref.3 Ref.4
Binding site821Substrate
Binding site2131Substrate
Binding site2321Substrate
Binding site2361Substrate

Experimental info

Mutagenesis1701K → M: Abolishes enzyme activity. Ref.4
Mutagenesis2321S → A: Reduces enzyme activity 50-fold. Ref.3
Mutagenesis2361Q → A: Nearly abolishes enzyme activity. Ref.3

Secondary structure

.................................................. 252
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P58687 [UniParc].

Last modified January 31, 2002. Version 1.
Checksum: 10BB561E38EA0A75

FASTA25227,325
        10         20         30         40         50         60 
MKTVTVRDLV VGEGAPKIIV SLMGKTITDV KSEALAYREA DFDILEWRVD HFANVTTAES 

        70         80         90        100        110        120 
VLEAAGAIRE IITDKPLLFT FRSAKEGGEQ ALTTGQYIDL NRAAVDSGLV DMIDLELFTG 

       130        140        150        160        170        180 
DDEVKATVGY AHQHNVAVIM SNHDFHKTPA AEEIVQRLRK MQELGADIPK IAVMPQTKAD 

       190        200        210        220        230        240 
VLTLLTATVE MQERYADRPI ITMSMSKTGV ISRLAGEVFG SAATFGAVKK ASAPGQISVA 

       250 
DLRTVLTILH QA 

« Hide

References

« Hide 'large scale' references
[1]"Complete genome sequence of Salmonella enterica serovar Typhimurium LT2."
McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P., Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D., Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E. expand/collapse author list , Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R., Wilson R.K.
Nature 413:852-856(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: LT2 / SGSC1412 / ATCC 700720.
[2]"New insights into the mechanism of the Schiff base hydrolysis catalyzed by type I dehydroquinate dehydratase from S. enterica: a theoretical study."
Yao Y., Li Z.S.
Org. Biomol. Chem. 10:7037-7044(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACTIVE SITE.
[3]"A conserved surface loop in type I dehydroquinate dehydratases positions an active site arginine and functions in substrate binding."
Light S.H., Minasov G., Shuvalova L., Peterson S.N., Caffrey M., Anderson W.F., Lavie A.
Biochemistry 50:2357-2363(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.03 ANGSTROMS) IN COMPLEXES WITH SUBSTRATE ANALOGS, CATALYTIC ACTIVITY, ACTIVE SITE, SUBUNIT, MUTAGENESIS OF SER-232 AND GLN-236.
[4]"Insights into the mechanism of type I dehydroquinate dehydratases from structures of reaction intermediates."
Light S.H., Minasov G., Shuvalova L., Duban M.E., Caffrey M., Anderson W.F., Lavie A.
J. Biol. Chem. 286:3531-3539(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.60 ANGSTROMS) OF WILD-TYPE AND MUTANT MET-170 IN COMPLEX WITH 3-DEHYDROQUINIC ACID, CATALYTIC ACTIVITY, ACTIVE SITE, SUBUNIT, MUTAGENESIS OF LYS-170.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE006468 Genomic DNA. Translation: AAL20283.1.
RefSeqNP_460324.1. NC_003197.1.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3L2IX-ray1.85A/B1-252[»]
3LB0X-ray1.65A/B1-252[»]
3M7WX-ray1.95A/B/C/D/E/F1-252[»]
3NNTX-ray1.60A/B1-252[»]
3O1NX-ray1.03A/B1-252[»]
3OEXX-ray1.90A/B/C/D1-252[»]
3S42X-ray1.45A/B1-252[»]
4GFSX-ray1.80A/B1-252[»]
4GUFX-ray1.50A/B1-252[»]
4GUGX-ray1.62A/B1-252[»]
4GUHX-ray1.95A/B1-252[»]
4GUIX-ray1.78A/B1-252[»]
4GUJX-ray1.50A/B1-252[»]
4IUOX-ray1.80A/B1-252[»]
ProteinModelPortalP58687.
SMRP58687. Positions 1-252.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING99287.STM1358.

Proteomic databases

PRIDEP58687.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAL20283; AAL20283; STM1358.
GeneID1252876.
KEGGstm:STM1358.
PATRIC32381199. VBISalEnt20916_1442.

Phylogenomic databases

HOGENOMHOG000105514.
KOK03785.
OMAEGMPKII.
OrthoDBEOG6P33BK.
PhylomeDBP58687.

Enzyme and pathway databases

BioCycSENT99287:GCTI-1368-MONOMER.
UniPathwayUPA00053; UER00086.

Family and domain databases

Gene3D3.20.20.70. 1 hit.
HAMAPMF_00214. AroD.
InterProIPR018508. 3-dehydroquinate_DH_AS.
IPR013785. Aldolase_TIM.
IPR001381. DHquinase_I.
[Graphical view]
PfamPF01487. DHquinase_I. 1 hit.
[Graphical view]
TIGRFAMsTIGR01093. aroD. 1 hit.
PROSITEPS01028. DEHYDROQUINASE_I. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP58687.

Entry information

Entry nameAROD_SALTY
AccessionPrimary (citable) accession number: P58687
Entry history
Integrated into UniProtKB/Swiss-Prot: January 31, 2002
Last sequence update: January 31, 2002
Last modified: July 9, 2014
This is version 89 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways