ID   ADEC_CENSY              Reviewed;         609 AA.
AC   A0RZ37;
DT   24-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT   09-JAN-2007, sequence version 1.
DT   25-MAY-2022, entry version 59.
DE   RecName: Full=Adenine deaminase {ECO:0000255|HAMAP-Rule:MF_01518};
DE            Short=Adenase {ECO:0000255|HAMAP-Rule:MF_01518};
DE            Short=Adenine aminase {ECO:0000255|HAMAP-Rule:MF_01518};
DE            EC=3.5.4.2 {ECO:0000255|HAMAP-Rule:MF_01518};
GN   Name=ade {ECO:0000255|HAMAP-Rule:MF_01518}; OrderedLocusNames=CENSYa_2000;
OS   Cenarchaeum symbiosum (strain A).
OC   Archaea; Thaumarchaeota; Cenarchaeales; Cenarchaeaceae; Cenarchaeum.
OX   NCBI_TaxID=414004;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=A;
RX   PubMed=17114289; DOI=10.1073/pnas.0608549103;
RA   Hallam S.J., Konstantinidis K.T., Putnam N., Schleper C., Watanabe Y.,
RA   Sugahara J., Preston C., de la Torre J., Richardson P.M., DeLong E.F.;
RT   "Genomic analysis of the uncultivated marine crenarchaeote Cenarchaeum
RT   symbiosum.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:18296-18301(2006).
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_01518};
CC   -!- COFACTOR:
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01518};
CC   -!- SIMILARITY: Belongs to the metallo-dependent hydrolases superfamily.
CC       Adenine deaminase family. {ECO:0000255|HAMAP-Rule:MF_01518}.
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DR   EMBL; DP000238; ABK78604.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0RZ37; -.
DR   SMR; A0RZ37; -.
DR   STRING; 414004.CENSYa_2000; -.
DR   EnsemblBacteria; ABK78604; ABK78604; CENSYa_2000.
DR   KEGG; csy:CENSYa_2000; -.
DR   PATRIC; fig|414004.10.peg.1832; -.
DR   HOGENOM; CLU_027935_0_0_2; -.
DR   OMA; TDHECFT; -.
DR   Proteomes; UP000000758; Chromosome.
DR   GO; GO:0000034; F:adenine deaminase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006146; P:adenine catabolic process; IEA:InterPro.
DR   Gene3D; 2.30.40.10; -; 1.
DR   HAMAP; MF_01518; Adenine_deamin; 1.
DR   InterPro; IPR006679; Adenine_deam.
DR   InterPro; IPR026912; Adenine_deam_C.
DR   InterPro; IPR006680; Amidohydro-rel.
DR   InterPro; IPR011059; Metal-dep_hydrolase_composite.
DR   InterPro; IPR032466; Metal_Hydrolase.
DR   PANTHER; PTHR11113:SF2; PTHR11113:SF2; 1.
DR   Pfam; PF13382; Adenine_deam_C; 1.
DR   Pfam; PF01979; Amidohydro_1; 1.
DR   SUPFAM; SSF51338; SSF51338; 1.
DR   SUPFAM; SSF51556; SSF51556; 1.
PE   3: Inferred from homology;
KW   Hydrolase; Manganese; Reference proteome.
FT   CHAIN           1..609
FT                   /note="Adenine deaminase"
FT                   /id="PRO_0000296735"
SQ   SEQUENCE   609 AA;  65675 MW;  FF49B1F1A9D637B7 CRC64;
     MRPLSRSISR LAAVAMGDRK ADLIIQNCSL VSVYTGEVIE GTEIAVSGDR IAYVGPDASH
     ARGAGTVIHN AQGRYAAPGF ADPHIHVDQF VTPAELAAQS VLHGTTSLFS DPIDMVGVAG
     YRGFRTLMNM SKDLPARFFH VVPGGLPVDG RFSHSNTLSP EEERSAIGLP DVLGMGEVFS
     WTKVTSRDPG TMRSIGTMLD GGCIINGHTA GASGKKLSAY VSAGILSCHE PVNAEQAEER
     LRLGMWVMMR EGSIRRDLAE ILPPMLKKEA GLDRLMFCTD GIDPVDMGEK GHIDHCVREA
     VRLGADPVRA IAMASRNCFD YYNMARDLGG ISPGRIADIQ MLYDLESFRP EDVFVGGNRM
     VSGGKLVSRQ HPVKAPSWTR RTIRLGRLTA ADFAVHSRKK TEQVNTITMK TEIITEQGSA
     ELSVKEGNVE PSRDSDVWKV AAFDRLSGNG GRTVGFLENF GADIGALASS WSFHENDLVV
     LGSSEIEMAK AANAVMDKGG GIAVVQKGRV SAMLPLQICG IISSDPFGKV SEGLSKLTSV
     MTDAGCTFQR PHLVPVFLPF LALPSVRILY SGMVDVRRRS YIPVIAGART ASQRPKTLRN
     IKKGPKSVR