ID   ADEC_ESCF3              Reviewed;         588 AA.
AC   B7LK09;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   10-FEB-2009, sequence version 1.
DT   03-AUG-2022, entry version 75.
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=EFER_3962;
OS   Escherichia fergusonii (strain ATCC 35469 / DSM 13698 / CCUG 18766 / IAM
OS   14443 / JCM 21226 / LMG 7866 / NBRC 102419 / NCTC 12128 / CDC 0568-73).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=585054;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35469 / DSM 13698 / BCRC 15582 / CCUG 18766 / IAM 14443 / JCM
RC   21226 / LMG 7866 / NBRC 102419 / NCTC 12128 / CDC 0568-73;
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; CU928158; CAQ91396.1; -; Genomic_DNA.
DR   RefSeq; WP_000371693.1; NC_011740.1.
DR   AlphaFoldDB; B7LK09; -.
DR   SMR; B7LK09; -.
DR   EnsemblBacteria; CAQ91396; CAQ91396; EFER_3962.
DR   KEGG; efe:EFER_3962; -.
DR   HOGENOM; CLU_027935_0_0_6; -.
DR   OMA; TDHECFT; -.
DR   OrthoDB; 751534at2; -.
DR   BioCyc; EFER585054:EFER_RS19795-MON; -.
DR   Proteomes; UP000000745; 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.
DR   TIGRFAMs; TIGR01178; ade; 1.
PE   3: Inferred from homology;
KW   Hydrolase; Manganese.
FT   CHAIN           1..588
FT                   /note="Adenine deaminase"
FT                   /id="PRO_1000146240"
SQ   SEQUENCE   588 AA;  63874 MW;  AD0A2FB482527CC7 CRC64;
     MDQAINHKIH YISRQQRQEI LAIARGEAVA DYLIENVVIL DLINGGEIAG PIAIKGRYIA
     GIGSEYNDAP TLQRIDAHGA IAVPGFIDAH LHIESSMMTP VTFETATLPR GLTTVICDPH
     EIVNVMGEAG FAWFARCAEQ ARQNQYLQVS SCVPALEGCD VNGASFTLEQ MLAWRDHPQV
     TGLAEMMDYP GVISGQNALL DKLDAFRHLT LDGHCPGLGG KELNAYIAAG IENCHESYLL
     EEGRRKLQLG MSLMIREGSA ARNLNALAPL INEFNSPQCM LCTDDRNPWE IAHEGHIDAL
     IRRLIEQHNV PLHVAYRVAS WSTARHFGLN HLGLLAPGKQ ADIVLLSDAR KVTVQQVLVK
     GEPIDAQTLQ AEESARLAQS APPYGNTIAR QPVSASDFAL QFTPGKRYRV IDVIHNELIT
     HSRSSVYSEN GFDRDDVCFI AVLERYGQRL DPACGLLGGF GLNEGALAAT VSHDSHNIVV
     IGRSAEEMAL AVNQVIQDGG GLCVVRNGQV QSHLPLPIAG LMSTDTAQSL AEQIDALKAA
     ARECGPLPDE PFIQMAFLSL PVIPALKLTS QGLFDGEKFA FTTLEVTE