ID   ADEC_SALRD              Reviewed;         545 AA.
AC   Q2S006;
DT   26-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT   26-JUN-2007, sequence version 2.
DT   25-MAY-2022, entry version 90.
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=SRU_2375;
OS   Salinibacter ruber (strain DSM 13855 / M31).
OC   Bacteria; Bacteroidetes; Bacteroidetes Order II. Incertae sedis;
OC   Rhodothermaceae; Salinibacter.
OX   NCBI_TaxID=309807;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 13855 / CECT 5946 / M31;
RX   PubMed=16330755; DOI=10.1073/pnas.0509073102;
RA   Mongodin E.F., Nelson K.E., Daugherty S., DeBoy R.T., Wister J., Khouri H.,
RA   Weidman J., Walsh D.A., Papke R.T., Sanchez Perez G., Sharma A.K.,
RA   Nesbo C.L., MacLeod D., Bapteste E., Doolittle W.F., Charlebois R.L.,
RA   Legault B., Rodriguez-Valera F.;
RT   "The genome of Salinibacter ruber: convergence and gene exchange among
RT   hyperhalophilic bacteria and archaea.";
RL   Proc. Natl. Acad. Sci. U.S.A. 102:18147-18152(2005).
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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=ABC46110.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; CP000159; ABC46110.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; YP_446475.1; NC_007677.1.
DR   AlphaFoldDB; Q2S006; -.
DR   SMR; Q2S006; -.
DR   STRING; 309807.SRU_2375; -.
DR   EnsemblBacteria; ABC46110; ABC46110; SRU_2375.
DR   KEGG; sru:SRU_2375; -.
DR   PATRIC; fig|309807.25.peg.2474; -.
DR   eggNOG; COG1001; Bacteria.
DR   HOGENOM; CLU_027935_0_0_10; -.
DR   Proteomes; UP000008674; Chromosome.
DR   GO; GO:0000034; F:adenine deaminase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006146; P:adenine catabolic process; IEA:InterPro.
DR   CDD; cd01295; AdeC; 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; 2.
DR   SUPFAM; SSF51556; SSF51556; 1.
DR   TIGRFAMs; TIGR01178; ade; 1.
PE   3: Inferred from homology;
KW   Hydrolase; Manganese; Reference proteome.
FT   CHAIN           1..545
FT                   /note="Adenine deaminase"
FT                   /id="PRO_0000292399"
SQ   SEQUENCE   545 AA;  58292 MW;  278FF7DDE66321D7 CRC64;
     MPASFSIAGR LVDLHARAIR PATVHVQDGV IARIEPAETV PERHLLPGFI DAHVHVESAM
     LPPSEFARAA VRHGTVGTVS DPHEIANVLG VEGVEYMIAD GRPVPFHFAF GAPSCVPATP
     FETSGAELGP DAVSALLDRD DVPYLSEMMD YPGAIDGAPN VLAKIRAAQV RDKPVDGHAP
     GLRGDDVAQY AAAGIETDHE CVSIEEAREK LEAGMKIAIR EGSAAKNFDE LIPLMDEAPD
     RLMFCSDDRH PDALAEGHID TLVRRALNRG YDRFDVLRAA CVHPVEHYGL DVGLLREGDP
     ADFIVVDDLD ALNVQETYVE GALVAEEGET HIEHVASDVV NRFDAEPVAP ADFRVPAGGD
     RLRVITAVDN QLGTGEEVVT TPTDDGYAVA DPDRDVLKLA VVNRYTEEST PAVAFVRGFG
     LDGGALASSV AHDSHNVVAV GARDDALARA VNAVVRAEGG ISAAAEGTQV LPLPIAGLMS
     DEPYDVVARR YTRLTDYVRA ELGSAMDAPF MTLSFLSLLV IPQLKLSDRG LFDGAAFEFV
     DRFVD