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Q3B2Q0 (ADE_PELLD) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 42. 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:Plut_1524
OrganismPelodictyon luteolum (strain DSM 273) (Chlorobium luteolum (strain DSM 273)) [Complete proteome] [HAMAP]
Taxonomic identifier319225 [NCBI]
Taxonomic lineageBacteriaChlorobiChlorobiaChlorobialesChlorobiaceaeChlorobium/Pelodictyon groupPelodictyon

Protein attributes

Sequence length341 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 – 341341Adenine deaminase HAMAP MF_01962
PRO_1000081927

Sites

Active site2001Proton donor By similarity
Metal binding171Zinc; catalytic By similarity
Metal binding191Zinc; catalytic By similarity
Metal binding1971Zinc; catalytic By similarity
Metal binding2781Zinc; catalytic By similarity
Binding site2791Substrate By similarity
Site2211Important for catalytic activity By similarity

Sequences

Sequence LengthMass (Da)Tools
Q3B2Q0 [UniParc].

Last modified November 22, 2005. Version 1.
Checksum: C98C6EC13A50AA52

FASTA34138,253
        10         20         30         40         50         60 
MTTVPCFIAG LPKAELHLHI EGTLEPAMML RLAERNRQPP PFPDVETAEK AYRFTNLQSF 

        70         80         90        100        110        120 
LDIYYRSTEV LVTEEDFYDL TLAYLEKAAS QKIGHAEIFF DPQAHTVRGI AFATVLRGME 

       130        140        150        160        170        180 
EACREAHSRL GISTRLIMCI LRHLSEQEGM TMLNEAVRWK RWITGIGLDS SERGNPPSKF 

       190        200        210        220        230        240 
HNLYREARRE GFFLTAHAGE EGSAASVKET LDLLHVDRID HGVRCMDDPA LVKELVRRAV 

       250        260        270        280        290        300 
PLTVCPLSNV KLQVFGSMQE HNLKAMLEKG LMVTLNSDDP AYFGGYLNDN FTAAAEALDL 

       310        320        330        340 
SFSDIIRLAA NSFNASMLSI VQKKIHLLEL ADYARGFAPG H 

« Hide

References

[1]"Complete sequence of Pelodictyon luteolum DSM 273."
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T., Hammon N., Israni S., Pitluck S., Bryant D., Schmutz J., Larimer F., Land M., Kyrpides N., Ivanova N., Richardson P.
Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: DSM 273.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000096 Genomic DNA. Translation: ABB24381.1.
RefSeqYP_375424.1. NC_007512.1.

3D structure databases

ProteinModelPortalQ3B2Q0.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ3B2Q0.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID3745150.
GenomeReviewsGene locus Plut_1524 in contig CP000096_GR.
KEGGplt:Plut_1524.
NMPDRfig|319225.3.peg.1506.
PATRIC21380686. VBIChlLut1287_1601.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG1816.
HOGENOMHBG630382.
OMAFGGYVDD.
PhylomeDBQ3B2Q0.
ProtClustDBPRK09358.

Enzyme and pathway databases

BioCycPLUT319225:PLUT_1524-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_PELLD
AccessionPrimary (citable) accession number: Q3B2Q0
Entry history
Integrated into UniProtKB/Swiss-Prot: May 20, 2008
Last sequence update: November 22, 2005
Last modified: January 25, 2012
This is version 42 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