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Q9P6I7 (ADE_SCHPO) Reviewed, UniProtKB/Swiss-Prot

Last modified December 14, 2011. Version 62. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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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
Name:aah1
Synonyms:dea2
ORF Names:SPBC1198.02
OrganismSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Taxonomic identifier284812 [NCBI]
Taxonomic lineageEukaryota › Fungi › Dikarya › Ascomycota › Taphrinomycotina › Schizosaccharomycetes › Schizosaccharomycetales › Schizosaccharomycetaceae › Schizosaccharomyces

Protein attributes

Sequence length367 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. Also exhibits a low activity towards N(6)-substituted adenines that are commonly known as the plant hormones cytokinins. Ref.1 Ref.4

Catalytic activity

Adenine + H2O = hypoxanthine + NH3.

Cofactor

Binds 1 zinc ion per subunit By similarity.

Subcellular location

Cytoplasm. Nucleus Ref.3.

Sequence similarities

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

Biophysicochemical properties

Kinetic parameters:

KM=32 µM for adenine Ref.4

pH dependence:

Optimum pH is 6.7.

Temperature dependence:

Optimum temperature is 33 degrees Celsius.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 367367Adenine deaminase
PRO_0000256237

Sites

Active site2121Proton donor By similarity
Metal binding191Zinc; catalytic By similarity
Metal binding211Zinc; catalytic By similarity
Metal binding2091Zinc; catalytic By similarity
Metal binding2901Zinc; catalytic By similarity
Binding site2911Substrate By similarity
Site2331Important for catalytic activity By similarity

Experimental info

Mutagenesis1501R → H in dea2-1: Abolishes adenine deaminase activity. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q9P6I7 [UniParc].

Last modified October 1, 2000. Version 1.
Checksum: 4470A2EF23405B85

FASTA36741,199
        10         20         30         40         50         60 
MSNLPIYNFI RKLPKCEHHV HLEGCLSPDL VFRLAKKNGI TLPSDDAAYT TPSTLLASYE 

        70         80         90        100        110        120 
HFGCLDDFLR YYYIAVSVLI EASDFEALAY EYFSIAHSQG VHHAEVFFDP QTHTSRGISY 

       130        140        150        160        170        180 
DVVVSGFSAA CERANRDFGM STNLIMCFLR HLPSEAAHET FAEALKRNDF ENGIVAGVGL 

       190        200        210        220        230        240 
DSSEVDFPPE LFQEVYKLAA EKGIRRTGHA GEEGDPSYIR SGLDNLSLQR IDHGIRLVED 

       250        260        270        280        290        300 
KELMKRVAEE NIMLTMCPLS NLKLRCVNSI AELPVREFLE AGVPFSINCD DPAYFGGYTL 

       310        320        330        340        350        360 
ENYFAIQKHF NLTVKEWVFI ANAAINGSWI SGKRKEELLS SVQKCVKEYT AEIQQPKTLE 


TAVEVQA

« Hide

References

« Hide 'large scale' references
[1]"Sub-families of alpha/beta barrel enzymes: a new adenine deaminase family."
Ribard C., Rochet M., Labedan B., Daignan-Fornier B., Alzari P., Scazzocchio C., Oestreicher N.
J. Mol. Biol. 334:1117-1131(2003) [PubMed: 14643670] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, MUTAGENESIS OF ARG-150.
[2]"The genome sequence of Schizosaccharomyces pombe."
Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A., Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S., Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M. expand/collapse author list , Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S., Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S., Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D., Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P., Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K., O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M., Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N., Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A., Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R., Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A., Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A., Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H., Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C., Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A., Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M., del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S., Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R., Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G., Nurse P.
Nature 415:871-880(2002) [PubMed: 11859360] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 972 / ATCC 24843.
[3]"ORFeome cloning and global analysis of protein localization in the fission yeast Schizosaccharomyces pombe."
Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S., Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S., Yoshida M.
Nat. Biotechnol. 24:841-847(2006) [PubMed: 16823372] [Abstract]
Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
[4]"Hydrolytic cleavage of N6-substituted adenine derivatives by eukaryotic adenine and adenosine deaminases."
Pospisilova H., Sebela M., Novak O., Frebort I.
Biosci. Rep. 28:335-347(2008) [PubMed: 18673302] [Abstract]
Cited for: FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CU329671 Genomic DNA. Translation: CAB91177.1.
RefSeqNP_595071.1. NM_001020977.1.

3D structure databases

HSSPHSSP built from PDB template 2AMX based on UniProtKB Q7RMV2.
ProteinModelPortalQ9P6I7.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ9P6I7.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiSPBC1198.02.1; SPBC1198.02.1:pep; SPBC1198.02.
GeneID2540066.
GenomeReviewsGene locus aah1 in contig CU329671_GR.
KEGGspo:SPBC1198.02.
NMPDRfig|4896.1.peg.937.

Organism-specific databases

GeneDB_SpombeSPBC1198.02.

Phylogenomic databases

eggNOGfuNOG04795.
GeneTreeEFGT00050000005551.
HOGENOMHBG630382.
OMARIGHERF.
OrthoDBEOG4P5PJR.

Gene expression databases

ArrayExpressQ9P6I7.

Family and domain databases

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_SCHPO
AccessionPrimary (citable) accession number: Q9P6I7
Entry history
Integrated into UniProtKB/Swiss-Prot: October 31, 2006
Last sequence update: October 1, 2000
Last modified: December 14, 2011
This is version 62 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Schizosaccharomyces pombe

Schizosaccharomyces pombe: entries and gene names

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents