ADE_SCHPO
ID ADE_SCHPO Reviewed; 367 AA.
AC Q9P6I7;
DT 31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 123.
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; Synonyms=dea2; ORFNames=SPBC1198.02;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND MUTAGENESIS OF ARG-150.
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
RN [3]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=16823372; DOI=10.1038/nbt1222;
RA Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S.,
RA Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S.,
RA Yoshida M.;
RT "ORFeome cloning and global analysis of protein localization in the fission
RT yeast Schizosaccharomyces pombe.";
RL Nat. Biotechnol. 24:841-847(2006).
RN [4]
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: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=32 uM for adenine {ECO:0000269|PubMed:18673302};
CC pH dependence:
CC Optimum pH is 6.7. {ECO:0000269|PubMed:18673302};
CC Temperature dependence:
CC Optimum temperature is 33 degrees Celsius.
CC {ECO:0000269|PubMed:18673302};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03145,
CC ECO:0000269|PubMed:16823372}. Nucleus {ECO:0000255|HAMAP-Rule:MF_03145,
CC ECO:0000269|PubMed:16823372}.
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; CU329671; CAB91177.1; -; Genomic_DNA.
DR RefSeq; NP_595071.1; NM_001020977.2.
DR AlphaFoldDB; Q9P6I7; -.
DR SMR; Q9P6I7; -.
DR BioGRID; 276604; 1.
DR STRING; 4896.SPBC1198.02.1; -.
DR MaxQB; Q9P6I7; -.
DR PaxDb; Q9P6I7; -.
DR EnsemblFungi; SPBC1198.02.1; SPBC1198.02.1:pep; SPBC1198.02.
DR GeneID; 2540066; -.
DR KEGG; spo:SPBC1198.02; -.
DR PomBase; SPBC1198.02; -.
DR VEuPathDB; FungiDB:SPBC1198.02; -.
DR eggNOG; KOG1097; Eukaryota.
DR HOGENOM; CLU_039228_7_0_1; -.
DR OMA; NHFTIHA; -.
DR PhylomeDB; Q9P6I7; -.
DR BRENDA; 3.5.4.2; 5613.
DR BRENDA; 3.5.4.4; 5613.
DR PRO; PR:Q9P6I7; -.
DR Proteomes; UP000002485; Chromosome II.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0005634; C:nucleus; HDA:PomBase.
DR GO; GO:0000034; F:adenine deaminase activity; IDA:PomBase.
DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0006146; P:adenine catabolic process; IDA:PomBase.
DR GO; GO:0043103; P:hypoxanthine salvage; IDA:PomBase.
DR GO; GO:0009117; P:nucleotide metabolic process; IEA:UniProtKB-KW.
DR CDD; cd01320; ADA; 1.
DR HAMAP; MF_01962; Adenine_deaminase; 1.
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.
PE 1: Evidence at protein level;
KW Cytoplasm; Hydrolase; Metal-binding; Nucleotide metabolism; Nucleus;
KW Reference proteome; Zinc.
FT CHAIN 1..367
FT /note="Adenine deaminase"
FT /id="PRO_0000256237"
FT ACT_SITE 212
FT /note="Proton donor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03145"
FT BINDING 19
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03145"
FT BINDING 21
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03145"
FT BINDING 209
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03145"
FT BINDING 290
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03145"
FT BINDING 291
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03145"
FT SITE 233
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03145"
FT MUTAGEN 150
FT /note="R->H: In dea2-1: Abolishes adenine deaminase
FT activity."
FT /evidence="ECO:0000269|PubMed:14643670"
SQ SEQUENCE 367 AA; 41199 MW; 4470A2EF23405B85 CRC64;
MSNLPIYNFI RKLPKCEHHV HLEGCLSPDL VFRLAKKNGI TLPSDDAAYT TPSTLLASYE
HFGCLDDFLR YYYIAVSVLI EASDFEALAY EYFSIAHSQG VHHAEVFFDP QTHTSRGISY
DVVVSGFSAA CERANRDFGM STNLIMCFLR HLPSEAAHET FAEALKRNDF ENGIVAGVGL
DSSEVDFPPE LFQEVYKLAA EKGIRRTGHA GEEGDPSYIR SGLDNLSLQR IDHGIRLVED
KELMKRVAEE NIMLTMCPLS NLKLRCVNSI AELPVREFLE AGVPFSINCD DPAYFGGYTL
ENYFAIQKHF NLTVKEWVFI ANAAINGSWI SGKRKEELLS SVQKCVKEYT AEIQQPKTLE
TAVEVQA
