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B3R3T1 (ADE_CUPTR) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 29. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
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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:RALTA_A0998
OrganismCupriavidus taiwanensis (strain R1 / LMG 19424) (Ralstonia taiwanensis (strain LMG 19424)) [Complete proteome] [HAMAP]
Taxonomic identifier164546 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Betaproteobacteria › Burkholderiales › Burkholderiaceae › Cupriavidus

Protein attributes

Sequence length351 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 – 351351Adenine deaminase HAMAP MF_01962
PRO_1000128838

Sites

Active site2031Proton donor By similarity
Metal binding201Zinc; catalytic By similarity
Metal binding221Zinc; catalytic By similarity
Metal binding2001Zinc; catalytic By similarity
Metal binding2811Zinc; catalytic By similarity
Binding site2821Substrate By similarity
Site2241Important for catalytic activity By similarity

Sequences

Sequence LengthMass (Da)Tools
B3R3T1 [UniParc].

Last modified September 2, 2008. Version 1.
Checksum: 594A3F8827C0B09E

FASTA35138,700
        10         20         30         40         50         60 
MTIDAALAEQ IRRTPKAELH VHIEGTLEPE LIFRLAQRNQ VALPYPSVDA LRAAYAFTDL 

        70         80         90        100        110        120 
QSFLDIYYAG ASVLLTEEDF FDMTMDYVKR AVADNVRHAE IFFDPQTHTA RGVPIGVVID 

       130        140        150        160        170        180 
GIADALAQAR TEYDFSSSLI LCFLRHLSEE DAFATLEAAL PYRDRFVGVG LDSSEKGNPP 

       190        200        210        220        230        240 
EKFARVFARA RELGLHLVAH AGEEGPAQYV ADALDILKAE RIDHGVRAID DAALVERLAR 

       250        260        270        280        290        300 
ERVALTVCPL SNVKLKVYPD LRDHPLKRML DAGVAITLHS DDPAYFGGYM NANWEATFDA 

       310        320        330        340        350 
LPLDAADAHK LARNSFEAAF LPAMQKAEFL AEVDHFWSAP PKSPPATAPA A

« Hide

References

[1]"Genome sequence of the beta-rhizobium Cupriavidus taiwanensis and comparative genomics of rhizobia."
Amadou C., Pascal G., Mangenot S., Glew M., Bontemps C., Capela D., Carrere S., Cruveiller S., Dossat C., Lajus A., Marchetti M., Poinsot V., Rouy Z., Servin B., Saad M., Schenowitz C., Barbe V., Batut J., Medigue C., Masson-Boivin C.
Genome Res. 18:1472-1483(2008) [PubMed: 18490699] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: R1 / LMG 19424.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CU633749 Genomic DNA. Translation: CAQ68963.1.
RefSeqYP_002005030.1. NC_010528.1.

3D structure databases

ProteinModelPortalB3R3T1.
ModBaseSearch...

Protein-protein interaction databases

STRINGB3R3T1.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID6454570.
GenomeReviewsGene locus RALTA_A0998 in contig CU633749_GR.
KEGGcti:RALTA_A0998.
PATRIC21528568. VBICupTai42494_0962.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHBG630382.
OMASYIYEAL.
ProtClustDBPRK09358.

Family and domain databases

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

Entry information

Entry nameADE_CUPTR
AccessionPrimary (citable) accession number: B3R3T1
Entry history
Integrated into UniProtKB/Swiss-Prot: April 14, 2009
Last sequence update: September 2, 2008
Last modified: January 25, 2012
This is version 29 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

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