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Protein

Adenine deaminase

Gene

AAH1

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.UniRule annotation4 Publications

Catalytic activityi

Adenine + H2O = hypoxanthine + NH3.UniRule annotation

Cofactori

Zn2+UniRule annotationNote: Binds 1 zinc ion per subunit.UniRule annotation

Kineticsi

  1. KM=55 µM for adenine1 Publication

    pH dependencei

    Optimum pH is 7.0.1 Publication

    Temperature dependencei

    Optimum temperature is 30-37 degrees Celsius.1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi16 – 161Zinc; catalyticUniRule annotation
    Metal bindingi18 – 181Zinc; catalyticUniRule annotation
    Metal bindingi204 – 2041Zinc; catalyticUniRule annotation
    Active sitei207 – 2071Proton donorUniRule annotation
    Sitei228 – 2281Important for catalytic activityUniRule annotation
    Metal bindingi285 – 2851Zinc; catalyticUniRule annotation
    Binding sitei286 – 2861SubstrateUniRule annotation

    GO - Molecular functioni

    • adenine deaminase activity Source: UniProtKB
    • zinc ion binding Source: UniProtKB-HAMAP

    GO - Biological processi

    • adenine catabolic process Source: UniProtKB
    • hypoxanthine salvage Source: SGD
    • nucleotide metabolic process Source: UniProtKB-KW
    • purine-containing compound salvage Source: SGD
    • purine ribonucleoside monophosphate biosynthetic process Source: InterPro
    Complete GO annotation...

    Keywords - Molecular functioni

    Hydrolase

    Keywords - Biological processi

    Nucleotide metabolism

    Keywords - Ligandi

    Metal-binding, Zinc

    Enzyme and pathway databases

    BioCyciYEAST:YNL141W-MONOMER.
    BRENDAi3.5.4.2. 984.
    3.5.4.4. 984.
    ReactomeiREACT_275169. Abacavir metabolism.
    REACT_278671. Purine salvage.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Adenine deaminaseUniRule annotation (EC:3.5.4.2UniRule annotation)
    Short name:
    ADEUniRule annotation
    Alternative name(s):
    Adenine aminohydrolaseUniRule annotation
    Short name:
    AAHUniRule annotation
    Gene namesi
    Name:AAH1UniRule annotation
    Ordered Locus Names:YNL141W
    ORF Names:N1208, N1825
    OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
    Taxonomic identifieri559292 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
    ProteomesiUP000002311 Componenti: Chromosome XIV

    Organism-specific databases

    CYGDiYNL141w.
    EuPathDBiFungiDB:YNL141W.
    SGDiS000005085. AAH1.

    Subcellular locationi

    GO - Cellular componenti

    Complete GO annotation...

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi69 – 691I → T in aah1-2; impairs AAH1 degradation during postdiauxic growth and leads to weak interaction with SAF1. 1 Publication
    Mutagenesisi72 – 721N → K in aah1-3; impairs AAH1 degradation during postdiauxic growth and leads to weak interaction with SAF1. 1 Publication
    Mutagenesisi219 – 2191D → G in aah1-4; impairs AAH1 degradation during postdiauxic growth and leads to weak interaction with SAF1. 1 Publication
    Mutagenesisi237 – 2371E → V in aah1-6; impairs AAH1 degradation during postdiauxic growth and leads to weak interaction with SAF1. 1 Publication
    Mutagenesisi329 – 3291K → E in aah1-7; impairs AAH1 degradation during postdiauxic growth. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 347347Adenine deaminasePRO_0000194360Add
    BLAST

    Post-translational modificationi

    Probably ubiquitinated when cells enter quiescence in response to nutrient limitation, since it is specifically degraded via a process requiring the F-box protein SAF1 and components of the SKP1-Cullin-F-box complex.1 Publication

    Keywords - PTMi

    Ubl conjugation

    Proteomic databases

    MaxQBiP53909.
    PaxDbiP53909.
    PeptideAtlasiP53909.

    Expressioni

    Inductioni

    Reduced when grown in a poor nitrogen source medium and strongly down-regulated when cells enter quiescence under nutrient-limiting conditions.1 Publication

    Interactioni

    Protein-protein interaction databases

    BioGridi35686. 142 interactions.
    DIPiDIP-4342N.
    IntActiP53909. 4 interactions.
    MINTiMINT-499127.

    Structurei

    3D structure databases

    ProteinModelPortaliP53909.
    SMRiP53909. Positions 5-321.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

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

    Phylogenomic databases

    eggNOGiCOG1816.
    GeneTreeiENSGT00730000111151.
    InParanoidiP53909.
    KOiK01488.
    OMAiNDEYAVA.
    OrthoDBiEOG7647CH.

    Family and domain databases

    HAMAPiMF_01962. Adenine_deaminase.
    InterProiIPR006650. A/AMP_deam_AS.
    IPR001365. A/AMP_deaminase_dom.
    IPR028892. ADE.
    IPR006330. Ado/ade_deaminase.
    [Graphical view]
    PfamiPF00962. A_deaminase. 1 hit.
    [Graphical view]
    TIGRFAMsiTIGR01430. aden_deam. 1 hit.
    PROSITEiPS00485. A_DEAMINASE. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P53909-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MVSVEFLQEL PKCEHHLHLE GTLEPDLLFP LAKRNDIILP EGFPKSVEEL
    60 70 80 90 100
    NEKYKKFRDL QDFLDYYYIG TNVLISEQDF FDLAWAYFKK VHKQGLVHAE
    110 120 130 140 150
    VFYDPQSHTS RGISIETVTK GFQRACDKAF SEFGITSKLI MCLLRHIEPE
    160 170 180 190 200
    ECLKTIEEAT PFIKDGTISA LGLDSAEKPF PPHLFVECYG KAASLNKDLK
    210 220 230 240 250
    LTAHAGEEGP AQFVSDALDL LQVTRIDHGI NSQYDEELLD RLSRDQTMLT
    260 270 280 290 300
    ICPLSNVKLQ VVQSVSELPL QKFLDRDVPF SLNSDDPAYF GGYILDVYTQ
    310 320 330 340
    VSKDFPHWDH ETWGRIAKNA IKGSWCDDKR KNGLLSRVDE VVTKYSH
    Length:347
    Mass (Da):39,635
    Last modified:October 1, 1996 - v1
    Checksum:iE25573A9F9EB7BB6
    GO

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    Z46843 Genomic DNA. Translation: CAA86885.1.
    Z71417 Genomic DNA. Translation: CAA96024.1.
    BK006947 Genomic DNA. Translation: DAA10407.1.
    PIRiS55143.
    RefSeqiNP_014258.1. NM_001182979.1.

    Genome annotation databases

    EnsemblFungiiYNL141W; YNL141W; YNL141W.
    GeneIDi855581.
    KEGGisce:YNL141W.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    Z46843 Genomic DNA. Translation: CAA86885.1.
    Z71417 Genomic DNA. Translation: CAA96024.1.
    BK006947 Genomic DNA. Translation: DAA10407.1.
    PIRiS55143.
    RefSeqiNP_014258.1. NM_001182979.1.

    3D structure databases

    ProteinModelPortaliP53909.
    SMRiP53909. Positions 5-321.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    BioGridi35686. 142 interactions.
    DIPiDIP-4342N.
    IntActiP53909. 4 interactions.
    MINTiMINT-499127.

    Proteomic databases

    MaxQBiP53909.
    PaxDbiP53909.
    PeptideAtlasiP53909.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblFungiiYNL141W; YNL141W; YNL141W.
    GeneIDi855581.
    KEGGisce:YNL141W.

    Organism-specific databases

    CYGDiYNL141w.
    EuPathDBiFungiDB:YNL141W.
    SGDiS000005085. AAH1.

    Phylogenomic databases

    eggNOGiCOG1816.
    GeneTreeiENSGT00730000111151.
    InParanoidiP53909.
    KOiK01488.
    OMAiNDEYAVA.
    OrthoDBiEOG7647CH.

    Enzyme and pathway databases

    BioCyciYEAST:YNL141W-MONOMER.
    BRENDAi3.5.4.2. 984.
    3.5.4.4. 984.
    ReactomeiREACT_275169. Abacavir metabolism.
    REACT_278671. Purine salvage.

    Miscellaneous databases

    NextBioi979709.
    PROiP53909.

    Family and domain databases

    HAMAPiMF_01962. Adenine_deaminase.
    InterProiIPR006650. A/AMP_deam_AS.
    IPR001365. A/AMP_deaminase_dom.
    IPR028892. ADE.
    IPR006330. Ado/ade_deaminase.
    [Graphical view]
    PfamiPF00962. A_deaminase. 1 hit.
    [Graphical view]
    TIGRFAMsiTIGR01430. aden_deam. 1 hit.
    PROSITEiPS00485. A_DEAMINASE. 1 hit.
    [Graphical view]
    ProtoNetiSearch...

    Publicationsi

    « Hide 'large scale' publications
    1. "A 43.5 kb segment of yeast chromosome XIV, which contains MFA2, MEP2, CAP/SRV2, NAM9, FKB1/FPR1/RBP1, MOM22 and CPT1, predicts an adenosine deaminase gene and 14 new open reading frames."
      Mallet L., Bussereau F., Jacquet M.
      Yeast 11:1195-1209(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: ATCC 204508 / S288c.
    2. "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] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION.
    3. "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIV and its evolutionary implications."
      Philippsen P., Kleine K., Poehlmann R., Duesterhoeft A., Hamberg K., Hegemann J.H., Obermaier B., Urrestarazu L.A., Aert R., Albermann K., Altmann R., Andre B., Baladron V., Ballesta J.P.G., Becam A.-M., Beinhauer J.D., Boskovic J., Buitrago M.J.
      , Bussereau F., Coster F., Crouzet M., D'Angelo M., Dal Pero F., De Antoni A., del Rey F., Doignon F., Domdey H., Dubois E., Fiedler T.A., Fleig U., Floeth M., Fritz C., Gaillardin C., Garcia-Cantalejo J.M., Glansdorff N., Goffeau A., Gueldener U., Herbert C.J., Heumann K., Heuss-Neitzel D., Hilbert H., Hinni K., Iraqui Houssaini I., Jacquet M., Jimenez A., Jonniaux J.-L., Karpfinger-Hartl L., Lanfranchi G., Lepingle A., Levesque H., Lyck R., Maftahi M., Mallet L., Maurer C.T.C., Messenguy F., Mewes H.-W., Moestl D., Nasr F., Nicaud J.-M., Niedenthal R.K., Pandolfo D., Pierard A., Piravandi E., Planta R.J., Pohl T.M., Purnelle B., Rebischung C., Remacha M.A., Revuelta J.L., Rinke M., Saiz J.E., Sartorello F., Scherens B., Sen-Gupta M., Soler-Mira A., Urbanus J.H.M., Valle G., Van Dyck L., Verhasselt P., Vierendeels F., Vissers S., Voet M., Volckaert G., Wach A., Wambutt R., Wedler H., Zollner A., Hani J.
      Nature 387:93-98(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 204508 / S288c.
    4. Cited for: GENOME REANNOTATION.
      Strain: ATCC 204508 / S288c.
    5. "Adenine deaminase and adenine utilization in Saccharomyces cerevisiae."
      Deeley M.C.
      J. Bacteriol. 174:3102-3110(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INDUCTION.
    6. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
    7. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
    8. "Skp1-Cullin-F-box-dependent degradation of Aah1p requires its interaction with the F-box protein Saf1p."
      Escusa S., Laporte D., Massoni A., Boucherie H., Dautant A., Daignan-Fornier B.
      J. Biol. Chem. 282:20097-20103(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH SAF1, UBIQUITINATION, MUTAGENESIS OF ILE-69; ASN-72; ASP-219; GLU-237 AND LYS-329.
    9. "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] [Europe PMC] [Abstract]
      Cited for: FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES.

    Entry informationi

    Entry nameiADE_YEAST
    AccessioniPrimary (citable) accession number: P53909
    Secondary accession number(s): D6W141
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1996
    Last sequence update: October 1, 1996
    Last modified: July 22, 2015
    This is version 127 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programFungal Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    Present with 20700 molecules/cell in log phase SD medium.1 Publication

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. SIMILARITY comments
      Index of protein domains and families
    2. Yeast
      Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
    3. Yeast chromosome XIV
      Yeast (Saccharomyces cerevisiae) chromosome XIV: entries and gene names

    External Data

    Dasty 3

    Similar proteinsi

    Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
    100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
    90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
    50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.