ADE_YEAST
ID ADE_YEAST Reviewed; 347 AA.
AC P53909; D6W141;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 175.
DE RecName: Full=Adenine deaminase {ECO:0000255|HAMAP-Rule:MF_03145};
DE Short=ADE {ECO:0000255|HAMAP-Rule:MF_03145};
DE EC=3.5.4.2 {ECO:0000255|HAMAP-Rule:MF_03145};
DE AltName: Full=Adenine aminohydrolase {ECO:0000255|HAMAP-Rule:MF_03145};
DE Short=AAH {ECO:0000255|HAMAP-Rule:MF_03145};
GN Name=AAH1 {ECO:0000255|HAMAP-Rule:MF_03145}; OrderedLocusNames=YNL141W;
GN ORFNames=N1208, N1825;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=8619318; DOI=10.1002/yea.320111210;
RA Mallet L., Bussereau F., Jacquet M.;
RT "A 43.5 kb segment of yeast chromosome XIV, which contains MFA2, MEP2,
RT CAP/SRV2, NAM9, FKB1/FPR1/RBP1, MOM22 and CPT1, predicts an adenosine
RT deaminase gene and 14 new open reading frames.";
RL Yeast 11:1195-1209(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RX PubMed=14643670; DOI=10.1016/j.jmb.2003.10.005;
RA Ribard C., Rochet M., Labedan B., Daignan-Fornier B., Alzari P.,
RA Scazzocchio C., Oestreicher N.;
RT "Sub-families of alpha/beta barrel enzymes: a new adenine deaminase
RT family.";
RL J. Mol. Biol. 334:1117-1131(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169873;
RA Philippsen P., Kleine K., Poehlmann R., Duesterhoeft A., Hamberg K.,
RA Hegemann J.H., Obermaier B., Urrestarazu L.A., Aert R., Albermann K.,
RA Altmann R., Andre B., Baladron V., Ballesta J.P.G., Becam A.-M.,
RA Beinhauer J.D., Boskovic J., Buitrago M.J., Bussereau F., Coster F.,
RA Crouzet M., D'Angelo M., Dal Pero F., De Antoni A., del Rey F., Doignon F.,
RA Domdey H., Dubois E., Fiedler T.A., Fleig U., Floeth M., Fritz C.,
RA Gaillardin C., Garcia-Cantalejo J.M., Glansdorff N., Goffeau A.,
RA Gueldener U., Herbert C.J., Heumann K., Heuss-Neitzel D., Hilbert H.,
RA Hinni K., Iraqui Houssaini I., Jacquet M., Jimenez A., Jonniaux J.-L.,
RA Karpfinger-Hartl L., Lanfranchi G., Lepingle A., Levesque H., Lyck R.,
RA Maftahi M., Mallet L., Maurer C.T.C., Messenguy F., Mewes H.-W., Moestl D.,
RA Nasr F., Nicaud J.-M., Niedenthal R.K., Pandolfo D., Pierard A.,
RA Piravandi E., Planta R.J., Pohl T.M., Purnelle B., Rebischung C.,
RA Remacha M.A., Revuelta J.L., Rinke M., Saiz J.E., Sartorello F.,
RA Scherens B., Sen-Gupta M., Soler-Mira A., Urbanus J.H.M., Valle G.,
RA Van Dyck L., Verhasselt P., Vierendeels F., Vissers S., Voet M.,
RA Volckaert G., Wach A., Wambutt R., Wedler H., Zollner A., Hani J.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIV and its
RT evolutionary implications.";
RL Nature 387:93-98(1997).
RN [4]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [5]
RP FUNCTION, AND INDUCTION.
RX PubMed=1577682; DOI=10.1128/jb.174.10.3102-3110.1992;
RA Deeley M.C.;
RT "Adenine deaminase and adenine utilization in Saccharomyces cerevisiae.";
RL J. Bacteriol. 174:3102-3110(1992).
RN [6]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=14562095; DOI=10.1038/nature02026;
RA Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA Weissman J.S., O'Shea E.K.;
RT "Global analysis of protein localization in budding yeast.";
RL Nature 425:686-691(2003).
RN [7]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [8]
RP FUNCTION, INTERACTION WITH SAF1, UBIQUITINATION, AND MUTAGENESIS OF ILE-69;
RP ASN-72; ASP-219; GLU-237 AND LYS-329.
RX PubMed=17517885; DOI=10.1074/jbc.m702425200;
RA Escusa S., Laporte D., Massoni A., Boucherie H., Dautant A.,
RA Daignan-Fornier B.;
RT "Skp1-Cullin-F-box-dependent degradation of Aah1p requires its interaction
RT with the F-box protein Saf1p.";
RL J. Biol. Chem. 282:20097-20103(2007).
RN [9]
RP FUNCTION, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=18673302; DOI=10.1042/bsr20080081;
RA Pospisilova H., Sebela M., Novak O., Frebort I.;
RT "Hydrolytic cleavage of N6-substituted adenine derivatives by eukaryotic
RT adenine and adenosine deaminases.";
RL Biosci. Rep. 28:335-347(2008).
CC -!- FUNCTION: Catalyzes the hydrolytic deamination of adenine to
CC hypoxanthine. Plays an important role in the purine salvage pathway and
CC in nitrogen catabolism. Also exhibits a low activity towards N(6)-
CC substituted adenines that are commonly known as the plant hormones
CC cytokinins. {ECO:0000255|HAMAP-Rule:MF_03145,
CC ECO:0000269|PubMed:14643670, ECO:0000269|PubMed:1577682,
CC ECO:0000269|PubMed:17517885, ECO:0000269|PubMed:18673302}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=adenine + H(+) + H2O = hypoxanthine + NH4(+);
CC Xref=Rhea:RHEA:23688, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:16708, ChEBI:CHEBI:17368, ChEBI:CHEBI:28938; EC=3.5.4.2;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_03145};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_03145};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000255|HAMAP-Rule:MF_03145};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=55 uM for adenine {ECO:0000269|PubMed:18673302};
CC pH dependence:
CC Optimum pH is 7.0. {ECO:0000269|PubMed:18673302};
CC Temperature dependence:
CC Optimum temperature is 30-37 degrees Celsius.
CC {ECO:0000269|PubMed:18673302};
CC -!- INTERACTION:
CC P53909; P38352: SAF1; NbExp=2; IntAct=EBI-2197, EBI-21172;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03145,
CC ECO:0000269|PubMed:14562095}. Nucleus {ECO:0000255|HAMAP-Rule:MF_03145,
CC ECO:0000269|PubMed:14562095}.
CC -!- INDUCTION: Reduced when grown in a poor nitrogen source medium and
CC strongly down-regulated when cells enter quiescence under nutrient-
CC limiting conditions. {ECO:0000269|PubMed:1577682}.
CC -!- PTM: Probably ubiquitinated when cells enter quiescence in response to
CC nutrient limitation, since it is specifically degraded via a process
CC requiring the F-box protein SAF1 and components of the SKP1-Cullin-F-
CC box complex. {ECO:0000269|PubMed:17517885}.
CC -!- MISCELLANEOUS: Present with 20700 molecules/cell in log phase SD
CC medium. {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the metallo-dependent hydrolases superfamily.
CC Adenosine and AMP deaminases family. Adenine deaminase type 2
CC subfamily. {ECO:0000255|HAMAP-Rule:MF_03145}.
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DR EMBL; Z46843; CAA86885.1; -; Genomic_DNA.
DR EMBL; Z71417; CAA96024.1; -; Genomic_DNA.
DR EMBL; BK006947; DAA10407.1; -; Genomic_DNA.
DR PIR; S55143; S55143.
DR RefSeq; NP_014258.1; NM_001182979.1.
DR AlphaFoldDB; P53909; -.
DR SMR; P53909; -.
DR BioGRID; 35686; 396.
DR DIP; DIP-4342N; -.
DR IntAct; P53909; 4.
DR MINT; P53909; -.
DR STRING; 4932.YNL141W; -.
DR iPTMnet; P53909; -.
DR MaxQB; P53909; -.
DR PaxDb; P53909; -.
DR PRIDE; P53909; -.
DR EnsemblFungi; YNL141W_mRNA; YNL141W; YNL141W.
DR GeneID; 855581; -.
DR KEGG; sce:YNL141W; -.
DR SGD; S000005085; AAH1.
DR VEuPathDB; FungiDB:YNL141W; -.
DR eggNOG; KOG1097; Eukaryota.
DR GeneTree; ENSGT00950000183113; -.
DR HOGENOM; CLU_039228_7_0_1; -.
DR InParanoid; P53909; -.
DR OMA; NHFTIHA; -.
DR BioCyc; YEAST:YNL141W-MON; -.
DR BRENDA; 3.5.4.2; 984.
DR BRENDA; 3.5.4.4; 984.
DR PRO; PR:P53909; -.
DR Proteomes; UP000002311; Chromosome XIV.
DR RNAct; P53909; protein.
DR GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR GO; GO:0005634; C:nucleus; HDA:SGD.
DR GO; GO:0000034; F:adenine deaminase activity; IDA:SGD.
DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0006146; P:adenine catabolic process; IDA:SGD.
DR GO; GO:0043103; P:hypoxanthine salvage; IDA:SGD.
DR GO; GO:0009117; P:nucleotide metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0009168; P:purine ribonucleoside monophosphate biosynthetic process; IEA:InterPro.
DR GO; GO:0043101; P:purine-containing compound salvage; IDA:SGD.
DR CDD; cd01320; ADA; 1.
DR HAMAP; MF_01962; Adenine_deaminase; 1.
DR InterPro; IPR006650; A/AMP_deam_AS.
DR InterPro; IPR001365; A_deaminase_dom.
DR InterPro; IPR028892; ADE.
DR InterPro; IPR006330; Ado/ade_deaminase.
DR InterPro; IPR032466; Metal_Hydrolase.
DR PANTHER; PTHR43114; PTHR43114; 1.
DR Pfam; PF00962; A_deaminase; 1.
DR SUPFAM; SSF51556; SSF51556; 1.
DR TIGRFAMs; TIGR01430; aden_deam; 1.
DR PROSITE; PS00485; A_DEAMINASE; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Hydrolase; Metal-binding; Nucleotide metabolism; Nucleus;
KW Reference proteome; Ubl conjugation; Zinc.
FT CHAIN 1..347
FT /note="Adenine deaminase"
FT /id="PRO_0000194360"
FT ACT_SITE 207
FT /note="Proton donor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03145"
FT BINDING 16
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03145"
FT BINDING 18
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03145"
FT BINDING 204
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03145"
FT BINDING 285
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03145"
FT BINDING 286
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03145"
FT SITE 228
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03145"
FT MUTAGEN 69
FT /note="I->T: In aah1-2; impairs AAH1 degradation during
FT postdiauxic growth and leads to weak interaction with
FT SAF1."
FT /evidence="ECO:0000269|PubMed:17517885"
FT MUTAGEN 72
FT /note="N->K: In aah1-3; impairs AAH1 degradation during
FT postdiauxic growth and leads to weak interaction with
FT SAF1."
FT /evidence="ECO:0000269|PubMed:17517885"
FT MUTAGEN 219
FT /note="D->G: In aah1-4; impairs AAH1 degradation during
FT postdiauxic growth and leads to weak interaction with
FT SAF1."
FT /evidence="ECO:0000269|PubMed:17517885"
FT MUTAGEN 237
FT /note="E->V: In aah1-6; impairs AAH1 degradation during
FT postdiauxic growth and leads to weak interaction with
FT SAF1."
FT /evidence="ECO:0000269|PubMed:17517885"
FT MUTAGEN 329
FT /note="K->E: In aah1-7; impairs AAH1 degradation during
FT postdiauxic growth."
FT /evidence="ECO:0000269|PubMed:17517885"
SQ SEQUENCE 347 AA; 39635 MW; E25573A9F9EB7BB6 CRC64;
MVSVEFLQEL PKCEHHLHLE GTLEPDLLFP LAKRNDIILP EGFPKSVEEL NEKYKKFRDL
QDFLDYYYIG TNVLISEQDF FDLAWAYFKK VHKQGLVHAE VFYDPQSHTS RGISIETVTK
GFQRACDKAF SEFGITSKLI MCLLRHIEPE ECLKTIEEAT PFIKDGTISA LGLDSAEKPF
PPHLFVECYG KAASLNKDLK LTAHAGEEGP AQFVSDALDL LQVTRIDHGI NSQYDEELLD
RLSRDQTMLT ICPLSNVKLQ VVQSVSELPL QKFLDRDVPF SLNSDDPAYF GGYILDVYTQ
VSKDFPHWDH ETWGRIAKNA IKGSWCDDKR KNGLLSRVDE VVTKYSH
