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Q59087 (3DHQ_ACIAD) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 78. 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:
Catabolic 3-dehydroquinate dehydratase

Short name=3-dehydroquinase
EC=4.2.1.10
Gene names
Name:quiB
Ordered Locus Names:ACIAD1713
OrganismAcinetobacter sp. (strain ADP1) [Complete proteome] [HAMAP]
Taxonomic identifier62977 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesMoraxellaceaeAcinetobacter

Protein attributes

Sequence length272 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Catalyzes the catabolic dehydration of dehydroquinate to dehydroshikimate. HAMAP MF_00214

Catalytic activity

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

Pathway

Aromatic compound metabolism; 3,4-dihydroxybenzoate biosynthesis; 3,4-dihydroxybenzoate from 3-dehydroquinate: step 1/2. HAMAP MF_00214

Induction

By protocatechuate. HAMAP MF_00214

Sequence similarities

Belongs to the type-I 3-dehydroquinase family.

Sequence caution

The sequence AAC37158.1 differs from that shown. Reason: Erroneous initiation.

The sequence CAG68555.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
   Biological processQuinate metabolism
   LigandSchiff base
   Molecular functionLyase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological processquinate metabolic process

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular function3-dehydroquinate dehydratase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 272272Catabolic 3-dehydroquinate dehydratase HAMAP MF_00214
PRO_0000138842

Sites

Active site1631Proton acceptor By similarity
Active site1901Schiff-base intermediate with substrate By similarity

Sequences

Sequence LengthMass (Da)Tools
Q59087 [UniParc].

Last modified December 1, 2000. Version 2.
Checksum: 98646DC5E88BF6D3

FASTA27229,899
        10         20         30         40         50         60 
MSLPILSTTY AAENTVPASK STYVVKNLNI GDLPVKTLVP ITAKTREQAL AQAKVIAENK 

        70         80         90        100        110        120 
DADIAEFRID LLEFASDTKK VIALGQELNQ ILKDKPLLAT IRTSNEGGKL KVTDQEYEKI 

       130        140        150        160        170        180 
YSEYLKKPFM QLLDIEMFRD QAAVAKLTKL AHQKKVLVVM SNHDFDKTPS EQEIVSRLLK 

       190        200        210        220        230        240 
QDQMGADILK IAVMPKSKQD VFTLMNATLK VSEQSTKPLL TMSMGRLGTI SRIATANMGG 

       250        260        270 
SLSFGMIGEA SAPGQIDVTA LKQFLKTVQP TP 

« Hide

References

« Hide 'large scale' references
[1]"Unusual ancestry of dehydratases associated with quinate catabolism in Acinetobacter calcoaceticus."
Elsemore D.A., Ornston L.N.
J. Bacteriol. 177:5971-5978(1995) [PubMed: 7592351] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], CHARACTERIZATION.
[2]"Unique features revealed by the genome sequence of Acinetobacter sp. ADP1, a versatile and naturally transformation competent bacterium."
Barbe V., Vallenet D., Fonknechten N., Kreimeyer A., Oztas S., Labarre L., Cruveiller S., Robert C., Duprat S., Wincker P., Ornston L.N., Weissenbach J., Marliere P., Cohen G.N., Medigue C.
Nucleic Acids Res. 32:5766-5779(2004) [PubMed: 15514110] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ADP1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
L05770 Genomic DNA. Translation: AAC37158.1. Different initiation.
CR543861 Genomic DNA. Translation: CAG68555.1. Different initiation.
RefSeqYP_046377.1. NC_005966.1.

3D structure databases

ProteinModelPortalQ59087.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ59087.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID2879575.
GenomeReviewsGene locus ACIAD1713 in contig CR543861_GR.
KEGGaci:ACIAD1713.
NMPDRfig|62977.3.peg.1639.
PATRIC20741196. VBIAciSp98416_1544.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0710.
HOGENOMHBG732926.
PhylomeDBQ59087.
ProtClustDBPRK02412.

Enzyme and pathway databases

BioCycASP62977:ACIAD1713-MONOMER.
MetaCyc:MONOMER-33.

Family and domain databases

HAMAPMF_00214. AroD.
[Tree]
InterProIPR018508. 3-dehydroquinate_DH_AS.
IPR013785. Aldolase_TIM.
IPR001381. DHquinase_I.
[Graphical view]
Gene3DG3DSA:3.20.20.70. Aldolase_TIM. 1 hit.
KOK03785.
PfamPF01487. DHquinase_I. 1 hit.
[Graphical view]
TIGRFAMsTIGR01093. AroD. 1 hit.
PROSITEPS01028. DEHYDROQUINASE_I. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry name3DHQ_ACIAD
AccessionPrimary (citable) accession number: Q59087
Secondary accession number(s): Q6FBK7
Entry history
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: December 1, 2000
Last modified: January 25, 2012
This is version 78 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families