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Q9I6Y4 (ADE_PSEAE) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 70. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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:PA0148
OrganismPseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228) [Reference proteome] [HAMAP]
Taxonomic identifier208964 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Gammaproteobacteria › Pseudomonadales › Pseudomonadaceae › Pseudomonas ›

Protein attributes

Sequence length316 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

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-Rule MF_01962

Catalytic activity

Adenine + H2O = hypoxanthine + NH3. HAMAP-Rule MF_01962

Cofactor

Binds 1 zinc ion per subunit By similarity.

Sequence similarities

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 316316Adenine deaminase HAMAP-Rule MF_01962
PRO_0000194377

Sites

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

Secondary structure

1 .............................................................. 316
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q9I6Y4 [UniParc].

Last modified March 1, 2001. Version 1.
Checksum: EFB41B00CBFDED4A

FASTA31636,163
        10         20         30         40         50         60 
MYEWLNALPK AELHLHLEGT LEPELLFALA ERNRIALPWN DVETLRKAYA FNNLQEFLDL 

        70         80         90        100        110        120 
YYAGADVLRT EQDFYDLTWA YLQKCKAQNV VHVEPFFDPQ THTDRGIPFE VVLAGIRAAL 

       130        140        150        160        170        180 
RDGEKLLGIR HGLILSFLRH LSEEQAQKTL DQALPFRDAF IAVGLDSSEV GHPPSKFQRV 

       190        200        210        220        230        240 
FDRARSEGFL TVAHAGEEGP PEYIWEALDL LKVERIDHGV RAFEDERLMR RLIDEQIPLT 

       250        260        270        280        290        300 
VCPLSNTKLC VFDDMSQHTI LDMLERGVKV TVNSDDPAYF GGYVTENFHA LQQSLGMTEE 

       310 
QARRLAQNSL DARLVK

« Hide

References

« Hide 'large scale' references
[1]"Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic pathogen."
Stover C.K., Pham X.-Q.T., Erwin A.L., Mizoguchi S.D., Warrener P., Hickey M.J., Brinkman F.S.L., Hufnagle W.O., Kowalik D.J., Lagrou M., Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y., Brody L.L., Coulter S.N., Folger K.R. expand/collapse author list , Kas A., Larbig K., Lim R.M., Smith K.A., Spencer D.H., Wong G.K.-S., Wu Z., Paulsen I.T., Reizer J., Saier M.H. Jr., Hancock R.E.W., Lory S., Olson M.V.
Nature 406:959-964(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228.
[2]"The crystal structure of adenosine deaminase in complex with adenine, chloropurine and hypoxanthine from pseudomonas aeruginosa."
New York structural genomix research consortium (NYSGXRC)
Submitted (DEC-2010) to the PDB data bank
Cited for: X-RAY CRYSTALLOGRAPHY (2.49 ANGSTROMS) OF 2-316 IN COMPLEX WITH ADENINE; CHLOROPURINE AND HYPOXANTHINE.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AE004091 Genomic DNA. Translation: AAG03538.1.
PIRH83625.
RefSeqNP_248838.1. NC_002516.2.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3OU8X-ray2.51A/B2-316[»]
3PANX-ray2.63A/B2-316[»]
3PAOX-ray2.49A/B2-316[»]
3PBMX-ray2.59A/B2-316[»]
ProteinModelPortalQ9I6Y4.
SMRQ9I6Y4. Positions 2-315.
ModBaseSearch...

Protein-protein interaction databases

STRING208964.PA0148.

Protocols and materials databases

DNASU879249.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID879249.
KEGGpae:PA0148.
PATRIC19834504. VBIPseAer58763_0154.

Organism-specific databases

PseudoCAPPA0148.

Phylogenomic databases

eggNOGCOG1816.
HOGENOMHOG000218813.
KOK01488.
OMAFTNLQSF.
ProtClustDBPRK09358.

Family and domain databases

HAMAPMF_01962. Adenine_deaminase.
InterProIPR001365. A/AMP_deaminase_dom.
IPR006330. Ado/ade_deaminase.
[Graphical view]
PfamPF00962. A_deaminase. 1 hit.
[Graphical view]
TIGRFAMsTIGR01430. aden_deam. 1 hit.
ProtoNetSearch...

Other

EvolutionaryTraceQ9I6Y4.

Entry information

Entry nameADE_PSEAE
AccessionPrimary (citable) accession number: Q9I6Y4
Entry history
Integrated into UniProtKB/Swiss-Prot: March 5, 2002
Last sequence update: March 1, 2001
Last modified: May 1, 2013
This is version 70 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

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