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Q2KWR7 (ADE_BORA1) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 41. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | 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:
Adenine deaminase

Short name=ADE
EC=3.5.4.2
Alternative name(s):
Adenine aminohydrolase
Short name=AAH
Gene names
Ordered Locus Names:BAV0774
OrganismBordetella avium (strain 197N) [Complete proteome] [HAMAP]
Taxonomic identifier360910 [NCBI]
Taxonomic lineageBacteriaProteobacteriaBetaproteobacteriaBurkholderialesAlcaligenaceaeBordetella

Protein attributes

Sequence length316 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Catalyzes the hydrolytic deamination of adenine to hypoxanthine. Plays an important role in the purine salvage pathway and in nitrogen catabolism By similarity. HAMAP MF_01962

Catalytic activity

Adenine + H2O = hypoxanthine + NH3. HAMAP MF_01962

Cofactor

Binds 1 zinc ion per subunit By similarity. HAMAP MF_01962

Sequence similarities

Belongs to the adenosine and AMP deaminases family. Adenine deaminase type 2 subfamily.

Ontologies

Keywords
   Biological processNucleotide metabolism
   LigandMetal-binding
Zinc
   Molecular functionHydrolase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological processpurine ribonucleoside monophosphate biosynthetic process

Inferred from electronic annotation. Source: InterPro

   Molecular functionadenine deaminase activity

Inferred from electronic annotation. Source: EC

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 316316Adenine deaminase HAMAP MF_01962
PRO_1000017653

Sites

Active site1971Proton donor By similarity
Metal binding141Zinc; catalytic By similarity
Metal binding161Zinc; catalytic By similarity
Metal binding1941Zinc; catalytic By similarity
Metal binding2751Zinc; catalytic By similarity
Binding site2761Substrate By similarity
Site2181Important for catalytic activity By similarity

Sequences

Sequence LengthMass (Da)Tools
Q2KWR7 [UniParc].

Last modified March 7, 2006. Version 1.
Checksum: 2700A01AF4AEB168

FASTA31635,705
        10         20         30         40         50         60 
MQDWLTALPK AELHIHLEGA LEPELLFALA QRNGVTLPWP DIDALRQAYQ YQNLQEFLDL 

        70         80         90        100        110        120 
YYQGAHVLRT EQDFYDLTWA YLRKCAEQGV THTEPFFDPQ THTDRGVPFQ VVLSGIQAAL 

       130        140        150        160        170        180 
ADGRRDLGIQ SGLILSFLRH LPEEAAMRTL DEALPYRDAF IAVGLDSSEA GFPPRLFERV 

       190        200        210        220        230        240 
FARARAEGLP AVAHAGEEGP PEYIWEALER LQVKRIDHGV RAWEDPRLIA HLVDTQIPLT 

       250        260        270        280        290        300 
VCPLSNVRLQ VFEHMGQHNV LEMLERGLNV CINSDDPAYF GGYVLENFMA LREHLGMSQE 

       310 
QARRLAANSL ASVLTA 

« Hide

References

[1]"Comparison of the genome sequence of the poultry pathogen Bordetella avium with those of B. bronchiseptica, B. pertussis, and B. parapertussis reveals extensive diversity in surface structures associated with host interaction."
Sebaihia M., Preston A., Maskell D.J., Kuzmiak H., Connell T.D., King N.D., Orndorff P.E., Miyamoto D.M., Thomson N.R., Harris D., Goble A., Lord A., Murphy L., Quail M.A., Rutter S., Squares R., Squares S., Woodward J., Parkhill J., Temple L.M.
J. Bacteriol. 188:6002-6015(2006) [PubMed: 16885469] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 197N.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AM167904 Genomic DNA. Translation: CAJ48386.1.
RefSeqYP_785305.1. NC_010645.1.

3D structure databases

ProteinModelPortalQ2KWR7.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ2KWR7.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID6264971.
GenomeReviewsGene locus BAV0774 in contig AM167904_GR.
KEGGbav:BAV0774.
NMPDRfig|521.1.peg.866.
PATRIC21127712. VBIBorAvi43433_0791.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHBG630382.
OMAFGGYVDD.
ProtClustDBPRK09358.

Enzyme and pathway databases

BioCycABAU360910:BAV0774-MONOMER.

Family and domain databases

HAMAPMF_01962. Adenine_deaminase.
[Tree]
InterProIPR001365. A/AMP_deaminase_dom.
IPR006330. A_deaminase.
[Graphical view]
KOK01488.
PANTHERPTHR11409:SF21. PTHR11409:SF21. 1 hit.
PfamPF00962. A_deaminase. 1 hit.
[Graphical view]
TIGRFAMsTIGR01430. Aden_deam. 1 hit.
ProtoNetSearch...

Entry information

Entry nameADE_BORA1
AccessionPrimary (citable) accession number: Q2KWR7
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: March 7, 2006
Last modified: January 25, 2012
This is version 41 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