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Q321F0 (AROD_SHIBS) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 54. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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:SBO_1438
OrganismShigella boydii serotype 4 (strain Sb227) [Complete proteome] [HAMAP]
Taxonomic identifier300268 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeShigella

Protein attributes

Sequence length252 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Catalytic activity

3-dehydroquinate = 3-dehydroshikimate + H2O. HAMAP-Rule MF_00214

Pathway

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

Subunit structure

Homodimer By similarity. HAMAP-Rule MF_00214

Sequence similarities

Belongs to the type-I 3-dehydroquinase family.

Ontologies

Keywords
   Biological processAmino-acid biosynthesis
Aromatic amino acid biosynthesis
   LigandSchiff base
   Molecular functionLyase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological_processaromatic amino acid family biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-HAMAP

chorismate biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-UniPathway

   Molecular_function3-dehydroquinate dehydratase activity

Inferred from electronic annotation. Source: UniProtKB-HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 2522523-dehydroquinate dehydratase HAMAP-Rule MF_00214
PRO_1000043180

Regions

Region46 – 483Substrate binding By similarity

Sites

Active site1431Proton donor/acceptor By similarity
Active site1701Schiff-base intermediate with substrate By similarity
Binding site821Substrate By similarity
Binding site2131Substrate By similarity
Binding site2321Substrate By similarity
Binding site2361Substrate By similarity

Sequences

Sequence LengthMass (Da)Tools
Q321F0 [UniParc].

Last modified December 6, 2005. Version 1.
Checksum: 144849291EB9004B

FASTA25227,460
        10         20         30         40         50         60 
MKTVTVKDLV IGTGAPKIIV SLMAKDIARV KSEALAYREA DFDILEWRVD HFADLSNVES 

        70         80         90        100        110        120 
VMAAAKILRE TMPEKPLLFT FRSAKEGGEQ AISTEAYIAL NRAAIDSGLV DMIDLELFTG 

       130        140        150        160        170        180 
DDQVKETVAC AHAHDVKVVM SNHDFHKTPE AEEIIARLRK MQSFDADIPK IALMPQSTSD 

       190        200        210        220        230        240 
VLTLLAATLE MQEQYADRPI ITMSMAKTGV ISRLAGEVFG SAATFGAVKK ASAPGQISVN 

       250 
DLRTVLTILH QA 

« Hide

References

[1]"Genome dynamics and diversity of Shigella species, the etiologic agents of bacillary dysentery."
Yang F., Yang J., Zhang X., Chen L., Jiang Y., Yan Y., Tang X., Wang J., Xiong Z., Dong J., Xue Y., Zhu Y., Xu X., Sun L., Chen S., Nie H., Peng J., Xu J. expand/collapse author list , Wang Y., Yuan Z., Wen Y., Yao Z., Shen Y., Qiang B., Hou Y., Yu J., Jin Q.
Nucleic Acids Res. 33:6445-6458(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Sb227.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000036 Genomic DNA. Translation: ABB66058.1.
RefSeqYP_407886.1. NC_007613.1.

3D structure databases

ProteinModelPortalQ321F0.
SMRQ321F0. Positions 1-252.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING300268.SBO_1438.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABB66058; ABB66058; SBO_1438.
GeneID3780421.
KEGGsbo:SBO_1438.
PATRIC18681872. VBIShiBoy33460_1871.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0710.
HOGENOMHOG000105514.
KOK03785.
OMAEGMPKII.
OrthoDBEOG6P33BK.

Enzyme and pathway databases

BioCycSBOY300268:GJFL-1435-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...

Entry information

Entry nameAROD_SHIBS
AccessionPrimary (citable) accession number: Q321F0
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: December 6, 2005
Last modified: May 14, 2014
This is version 54 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

PATHWAY comments

Index of metabolic and biosynthesis pathways