ID   ADEC_ENTFA              Reviewed;         579 AA.
AC   Q835Z6;
DT   16-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   03-AUG-2022, entry version 92.
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=EF_1222;
OS   Enterococcus faecalis (strain ATCC 700802 / V583).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Enterococcaceae;
OC   Enterococcus.
OX   NCBI_TaxID=226185;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700802 / V583;
RX   PubMed=12663927; DOI=10.1126/science.1080613;
RA   Paulsen I.T., Banerjei L., Myers G.S.A., Nelson K.E., Seshadri R.,
RA   Read T.D., Fouts D.E., Eisen J.A., Gill S.R., Heidelberg J.F., Tettelin H.,
RA   Dodson R.J., Umayam L.A., Brinkac L.M., Beanan M.J., Daugherty S.C.,
RA   DeBoy R.T., Durkin S.A., Kolonay J.F., Madupu R., Nelson W.C.,
RA   Vamathevan J.J., Tran B., Upton J., Hansen T., Shetty J., Khouri H.M.,
RA   Utterback T.R., Radune D., Ketchum K.A., Dougherty B.A., Fraser C.M.;
RT   "Role of mobile DNA in the evolution of vancomycin-resistant Enterococcus
RT   faecalis.";
RL   Science 299:2071-2074(2003).
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; AE016830; AAO81019.1; -; Genomic_DNA.
DR   RefSeq; NP_814949.1; NC_004668.1.
DR   RefSeq; WP_010706582.1; NZ_KE136528.1.
DR   AlphaFoldDB; Q835Z6; -.
DR   SMR; Q835Z6; -.
DR   STRING; 226185.EF_1222; -.
DR   EnsemblBacteria; AAO81019; AAO81019; EF_1222.
DR   KEGG; efa:EF1222; -.
DR   PATRIC; fig|226185.45.peg.2277; -.
DR   eggNOG; COG1001; Bacteria.
DR   HOGENOM; CLU_027935_0_0_9; -.
DR   OMA; MVTACAY; -.
DR   Proteomes; UP000001415; 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   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..579
FT                   /note="Adenine deaminase"
FT                   /id="PRO_0000142423"
SQ   SEQUENCE   579 AA;  64897 MW;  BF99804BF7CEC732 CRC64;
     MNVDVLLKNV WLYQTVTQTF VQRNVAIKND KFYYIYEEEN VNLQPQKTIN AENQWMIPGL
     IDAHMHIESS MTTPTIFSKA VVRYGVTTVI ADAHEMANVF GLEGLKAFMA AETELDIFHA
     IPSSVPSTTP ELETTGGIIG LAEVAELLKE PKVICLGEAM NFKGISYEPD SLIRQIIDLC
     QKQRPTMPLE GHCPKIEDQE LADFLYSGIT SDHTHQFPKT LKEKIEAGVF IQFQNKSITP
     ENIQVIVDND FYNYASIITD DVMADDLLKG HLNENVKKAV HAGLPIEKAI YMATYTPAKR
     MGLHDRGEIA PGKKADFLLL NDLESFDINT VYKSGKVVFE KGEPFHYPEK IEEFPATYQQ
     TIQCKKLTEE DLLLKVATTK ETVRCNVIQK QEIGTFTERI TKEIPVENGL LQWQKANCAL
     LIVMERYGKN GNISFSLMDQ PLSEKGAIAT TWAHDHHNLM VMGNTIEDIL LAQNELLAMQ
     GGYLVASDQQ VMATCPLPIG GILSQAPIEQ LGASLQKVRQ AMQALGYQNM NEIMSFSTLS
     LPVSPAIKVT DFGMMDTKSQ RFYPLVFPED GVLLHENTH