ID   ADEC_PARD8              Reviewed;         545 AA.
AC   A6LG60;
DT   11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT   24-JUL-2007, sequence version 1.
DT   03-AUG-2022, entry version 82.
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=BDI_2966;
OS   Parabacteroides distasonis (strain ATCC 8503 / DSM 20701 / CIP 104284 / JCM
OS   5825 / NCTC 11152).
OC   Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Tannerellaceae;
OC   Parabacteroides.
OX   NCBI_TaxID=435591;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 8503 / DSM 20701 / CIP 104284 / JCM 5825 / NCTC 11152;
RX   PubMed=17579514; DOI=10.1371/journal.pbio.0050156;
RA   Xu J., Mahowald M.A., Ley R.E., Lozupone C.A., Hamady M., Martens E.C.,
RA   Henrissat B., Coutinho P.M., Minx P., Latreille P., Cordum H.,
RA   Van Brunt A., Kim K., Fulton R.S., Fulton L.A., Clifton S.W., Wilson R.K.,
RA   Knight R.D., Gordon J.I.;
RT   "Evolution of symbiotic bacteria in the distal human intestine.";
RL   PLoS Biol. 5:1574-1586(2007).
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; CP000140; ABR44674.1; -; Genomic_DNA.
DR   RefSeq; WP_011967083.1; NC_009615.1.
DR   AlphaFoldDB; A6LG60; -.
DR   SMR; A6LG60; -.
DR   STRING; 435591.BDI_2966; -.
DR   EnsemblBacteria; ABR44674; ABR44674; BDI_2966.
DR   KEGG; pdi:BDI_2966; -.
DR   PATRIC; fig|435591.13.peg.2928; -.
DR   eggNOG; COG1001; Bacteria.
DR   HOGENOM; CLU_027935_0_0_10; -.
DR   OMA; TDHECFT; -.
DR   OrthoDB; 751534at2; -.
DR   BioCyc; PDIS435591:G1G5A-3043-MON; -.
DR   Proteomes; UP000000566; Chromosome.
DR   GO; GO:0000034; F:adenine deaminase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006146; P:adenine catabolic process; IEA:InterPro.
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; 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; 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_0000300159"
SQ   SEQUENCE   545 AA;  60358 MW;  0928A6DDF9BE8C5F CRC64;
     MNEAKTLVIR GNLVDIINRR TFGAEISILN GHIGKVIPTG QDEGSYLLPG FIDAHVHIES
     SMVTPAAFIH AAVRHGSIGA VADPHEIANV MGTEGVEYML DNAKGIPFYT WFGVPSCVPA
     TIMETSGAII DADETARLLE REDLHFLAEM MNYPGVLNKD PEVMRKIEAA KNAGKPIDGH
     YPLATGPKLK AYIESGISTD HETIYLEKGR EKCELGMHVL IREGSAAKNF DALHPLLKEY
     PEQIMFCTDD AHPSFLNKGH INRMVKKSLD LGYDLYDVLR AASYNPAMHY KIPAGFLREG
     DSADFIQVNN LKNLTIQATY IQGTCVYDGE KCTLPFHKPI LRNNFHTKPI PLEKLAVKAK
     GKQMRVIVCE DRELITKEEL YPVHTFDGFV ESDTERDILK LVILNRYQTA PPAIAFIKGT
     GLKLGAIAQS ISHDSHNIIA IGVTDFELMQ AINVVIKAKG GIAVSCMDEV TLLPLPVAGL
     MSDESLEETS RRYEEIEEKI KRLKSPMDSL QMTLSFMGLL AIPSLKLSNK GLFNSETFQF
     TSLFV