ID   ADEC_ECO8A              Reviewed;         588 AA.
AC   B7M4F2;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   24-MAR-2009, sequence version 1.
DT   03-AUG-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=ECIAI1_3841;
OS   Escherichia coli O8 (strain IAI1).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=585034;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IAI1;
RX   PubMed=19165319; DOI=10.1371/journal.pgen.1000344;
RA   Touchon M., Hoede C., Tenaillon O., Barbe V., Baeriswyl S., Bidet P.,
RA   Bingen E., Bonacorsi S., Bouchier C., Bouvet O., Calteau A., Chiapello H.,
RA   Clermont O., Cruveiller S., Danchin A., Diard M., Dossat C., Karoui M.E.,
RA   Frapy E., Garry L., Ghigo J.M., Gilles A.M., Johnson J., Le Bouguenec C.,
RA   Lescat M., Mangenot S., Martinez-Jehanne V., Matic I., Nassif X., Oztas S.,
RA   Petit M.A., Pichon C., Rouy Z., Ruf C.S., Schneider D., Tourret J.,
RA   Vacherie B., Vallenet D., Medigue C., Rocha E.P.C., Denamur E.;
RT   "Organised genome dynamics in the Escherichia coli species results in
RT   highly diverse adaptive paths.";
RL   PLoS Genet. 5:E1000344-E1000344(2009).
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; CU928160; CAR00636.1; -; Genomic_DNA.
DR   RefSeq; WP_001065695.1; NC_011741.1.
DR   AlphaFoldDB; B7M4F2; -.
DR   SMR; B7M4F2; -.
DR   PRIDE; B7M4F2; -.
DR   KEGG; ecr:ECIAI1_3841; -.
DR   HOGENOM; CLU_027935_0_0_6; -.
DR   OMA; TDHECFT; -.
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.
DR   TIGRFAMs; TIGR01178; ade; 1.
PE   3: Inferred from homology;
KW   Hydrolase; Manganese.
FT   CHAIN           1..588
FT                   /note="Adenine deaminase"
FT                   /id="PRO_1000146235"
SQ   SEQUENCE   588 AA;  63709 MW;  273570DAD7595E48 CRC64;
     MNNSINHKFH HISRAEYQEL LAVSRGDAVA DYIIDNVSIL DLINGGEISG PIVIKGRYIA
     GVGAEYADAP ALQRIDARGA TAVPGFIDAH LHIESSMMTP VTFETATLPR GLTTVICDPH
     EIVNVMGEAG FAWFARCAEQ ARQNQYLQVS SCVPALEGCD VNGASFTLEQ MLAWRDHPQV
     TGLAEMMDYP GVISGQNALL DKLDAFRHLT LDGHCPGLGG KELNAYITAG IENCHESYQL
     EEGRRKLQLG MSLMIREGSA ARNLNALAPL INEFNSPQCM LCTDDRNPWE IAHEGHIDAL
     IRRLIEQHNV PLHVAYRVAS WSTARHFGLN HLGLLAPGKQ ADIVLLSDAR KVTVQQVLVK
     GEPIDAQTLQ AEESARLAQS APPYGNTIAR QPVSASDFAL QFTPGKRYRV IDVIHNELIT
     HSHSSVYSEN GFDRDDVSFI AVLERYGQRL APACGLLGGF GLNEGALAAT VSHDSHNIVV
     IGRSAEEMAL AVNQVIQDGG GLCVVRNGQV QSHLPLPIAG LMSTDTAQSL AEQIDALKAA
     ARECGPLPDE PFIQMAFLSL PVIPALKLTS QGLFDGEKFA FTTLEVTE