ID   ADEC_SERP5              Reviewed;         595 AA.
AC   A8GAT0;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   13-NOV-2007, sequence version 1.
DT   25-MAY-2022, entry version 70.
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=Spro_1116;
OS   Serratia proteamaculans (strain 568).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Yersiniaceae; Serratia.
OX   NCBI_TaxID=399741;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=568;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA   Tice H., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Kim E., Taghavi S., Newman L.,
RA   Vangronsveld J., van der Lelie D., Richardson P.;
RT   "Complete sequence of chromosome of Serratia proteamaculans 568.";
RL   Submitted (SEP-2007) to the EMBL/GenBank/DDBJ databases.
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   -!- SUBUNIT: Homodimer. {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; CP000826; ABV40220.1; -; Genomic_DNA.
DR   RefSeq; WP_012005556.1; NC_009832.1.
DR   AlphaFoldDB; A8GAT0; -.
DR   SMR; A8GAT0; -.
DR   STRING; 399741.Spro_1116; -.
DR   EnsemblBacteria; ABV40220; ABV40220; Spro_1116.
DR   KEGG; spe:Spro_1116; -.
DR   eggNOG; COG1001; Bacteria.
DR   HOGENOM; CLU_027935_0_0_6; -.
DR   OMA; IEGHFPG; -.
DR   OrthoDB; 751534at2; -.
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.
FT   CHAIN           1..595
FT                   /note="Adenine deaminase"
FT                   /id="PRO_0000318549"
SQ   SEQUENCE   595 AA;  63138 MW;  914FFA6E2837E9A9 CRC64;
     MTTHCISTGE RQRAVKAALG QLPFDLLLTN AALIDMATGE VRNVDVGIVG ALIASVHPCG
     TLTEALQTQD LAGAYLSPGL IDTHVHVESS HLPPERYAEI VVAQGTTTIF WDPHELANVL
     GVAGVRYAVD ASRGLPLRVI CAAPSSVPST PGLEMSGADF AGQEMETMLA WPEVGGVAEV
     MDMHGVLNGS ERMLEILNAG LNSGKLIEGH ARGLSGADLQ AYLAAGVTSD HELTSGADAL
     EKLRAGLTLE IRGSHPYLLP EIVAALKTLP HLSSQITVCT DDVPPDMLLE KGGIVALLNM
     LIEQGLPATD VLRMATLNAA IRLQRNDLGL IAAGRVADLV VFDSLTQLRA QQVYVAGKLT
     AQQGKMQKPL NANPNVAAPR DTLRLQPLAA GDFVLKVPAI RHGKATLRHI KGARFTQWNE
     TTVEVRNGEV QIPQGFSLIW VQHRHGRHQA TPQLALLEGW GELRGAIATS YSHDSHNLVV
     LGRDAADMAL AANALIASGG GMALSQNGEI LAQVAMPIAG MLSDLPAAEL AQQFKNLRDL
     SARIADWEPP YRVFKAIEGT CLACNAGPHL TDLGLTDGST RQIVDPLIAC WETPA