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Q59ZB1 (ADE_CANAL) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 40. 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
Name:AAH1
ORF Names:CaO19.2251, CaO19.9791
OrganismCandida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Taxonomic identifier237561 [NCBI]
Taxonomic lineageEukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › mitosporic Saccharomycetales › Candida

Protein attributes

Sequence length356 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.

Catalytic activity

Adenine + H2O = hypoxanthine + NH3.

Cofactor

Binds 1 zinc ion per subunit By similarity.

Subcellular location

Cytoplasm By similarity. Nucleus By similarity.

Sequence similarities

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

Ontologies

Keywords
   Biological processNucleotide metabolism
   Cellular componentCytoplasm
Nucleus
   LigandMetal-binding
Zinc
   Molecular functionHydrolase
Gene Ontology (GO)
   Biological processpurine ribonucleoside monophosphate biosynthetic process

Inferred from electronic annotation. Source: InterPro

   Cellular componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

nucleus

Inferred from electronic annotation. Source: UniProtKB-SubCell

   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 – 356356Adenine deaminase
PRO_0000256232

Sites

Active site2141Proton donor By similarity
Metal binding231Zinc; catalytic By similarity
Metal binding251Zinc; catalytic By similarity
Metal binding2111Zinc; catalytic By similarity
Metal binding2921Zinc; catalytic By similarity
Binding site2931Substrate By similarity
Site2351Important for catalytic activity By similarity

Natural variations

Natural variant2731K → T in allele CaO19.9791.
Natural variant2841N → T in allele CaO19.9791.

Sequences

Sequence LengthMass (Da)Tools
Q59ZB1 [UniParc].

Last modified April 26, 2005. Version 1.
Checksum: B22B1ED9D27A9F19

FASTA35640,782
        10         20         30         40         50         60 
MAQYECSEHM ENFLRELPKC EHHVHLEGTL EPSLLFKLAK RNNITLPETF PKTVEECNDR 

        70         80         90        100        110        120 
YNRFADLQDF LDHYYIGMGV LITENDFYDL AMDYFTKAHS DGCLHSEVFF DPQGHVERNI 

       130        140        150        160        170        180 
DIDVVVQGFN RACKDANTKY GTTNKLIMCL LRHLPAENGL QTIHSASKYY QDGIIHGLGL 

       190        200        210        220        230        240 
DSSEKPFPPN LFTECYAHIK DNFPEVGLTA HAGEEGDHTF VSDALNLLKV SRIDHGVNSH 

       250        260        270        280        290        300 
QSEELMQRLA EQKTLLSLCP LSNVKLQVVK DVKELPIDKF FQMNVPFSIN SDDPAYFGGY 

       310        320        330        340        350 
ILDNYKAVHT RFGFTKDQWK IIALNGIKGS WCDDQRKNEL ISLVEEVYKK YNIEGC

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References

[1]"The diploid genome sequence of Candida albicans."
Jones T., Federspiel N.A., Chibana H., Dungan J., Kalman S., Magee B.B., Newport G., Thorstenson Y.R., Agabian N., Magee P.T., Davis R.W., Scherer S.
Proc. Natl. Acad. Sci. U.S.A. 101:7329-7334(2004) [PubMed: 15123810] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: SC5314 / ATCC MYA-2876.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AACQ01000095 Genomic DNA. Translation: EAK95800.1.
AACQ01000096 Genomic DNA. Translation: EAK95736.1.
RefSeqXP_714779.1. XM_709686.1.
XP_714841.1. XM_709748.1.

3D structure databases

HSSPHSSP built from PDB template 2AMX based on UniProtKB Q7RMV2.
ProteinModelPortalQ59ZB1.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ59ZB1.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID3643529.
3643578.
KEGGcal:CaO19.2251.
cal:CaO19.9791.

Organism-specific databases

CGDCAL0006286. AAH1.

Phylogenomic databases

PhylomeDBQ59ZB1.

Family and domain databases

InterProIPR006650. A/AMP_deam_AS.
IPR001365. 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.
PROSITEPS00485. A_DEAMINASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameADE_CANAL
AccessionPrimary (citable) accession number: Q59ZB1
Secondary accession number(s): Q59Z49
Entry history
Integrated into UniProtKB/Swiss-Prot: October 31, 2006
Last sequence update: April 26, 2005
Last modified: January 25, 2012
This is version 40 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Candida albicans

Candida albicans: entries and gene names

SIMILARITY comments

Index of protein domains and families

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