ID   ADEC_ECO57              Reviewed;         588 AA.
AC   Q7A9L5; Q8XC38;
DT   16-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 98.
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};
GN   OrderedLocusNames=Z5155, ECs4602;
OS   Escherichia coli O157:H7.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83334;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=O157:H7 / EDL933 / ATCC 700927 / EHEC;
RX   PubMed=11206551; DOI=10.1038/35054089;
RA   Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D., Rose D.J.,
RA   Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A., Posfai G.,
RA   Hackett J., Klink S., Boutin A., Shao Y., Miller L., Grotbeck E.J.,
RA   Davis N.W., Lim A., Dimalanta E.T., Potamousis K., Apodaca J.,
RA   Anantharaman T.S., Lin J., Yen G., Schwartz D.C., Welch R.A.,
RA   Blattner F.R.;
RT   "Genome sequence of enterohaemorrhagic Escherichia coli O157:H7.";
RL   Nature 409:529-533(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=O157:H7 / Sakai / RIMD 0509952 / EHEC;
RX   PubMed=11258796; DOI=10.1093/dnares/8.1.11;
RA   Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K.,
RA   Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T., Iida T.,
RA   Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T., Kuhara S.,
RA   Shiba T., Hattori M., Shinagawa H.;
RT   "Complete genome sequence of enterohemorrhagic Escherichia coli O157:H7 and
RT   genomic comparison with a laboratory strain K-12.";
RL   DNA Res. 8:11-22(2001).
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; AE005174; AAG58864.1; -; Genomic_DNA.
DR   EMBL; BA000007; BAB38025.1; -; Genomic_DNA.
DR   PIR; B91204; B91204.
DR   PIR; D86050; D86050.
DR   RefSeq; NP_312629.1; NC_002695.1.
DR   RefSeq; WP_001065705.1; NZ_SWKA01000005.1.
DR   AlphaFoldDB; Q7A9L5; -.
DR   SMR; Q7A9L5; -.
DR   STRING; 155864.EDL933_4989; -.
DR   EnsemblBacteria; AAG58864; AAG58864; Z5155.
DR   EnsemblBacteria; BAB38025; BAB38025; ECs_4602.
DR   GeneID; 915433; -.
DR   KEGG; ece:Z5155; -.
DR   KEGG; ecs:ECs_4602; -.
DR   PATRIC; fig|386585.9.peg.4810; -.
DR   eggNOG; COG1001; Bacteria.
DR   HOGENOM; CLU_027935_0_0_6; -.
DR   OMA; TDHECFT; -.
DR   Proteomes; UP000000558; Chromosome.
DR   Proteomes; UP000002519; 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; Reference proteome.
FT   CHAIN           1..588
FT                   /note="Adenine deaminase"
FT                   /id="PRO_0000142421"
SQ   SEQUENCE   588 AA;  63691 MW;  FBC865E0D9FE96A1 CRC64;
     MNNSINHKFH HISRAEYQEL LAVSRGDAVA DYIIDNVSIL DLINGGEISG PIVIKGRYIA
     GVGAEYTDAP ALQRIDAHGA TAVPGFIDAH LHIESSMMTP VTFETATLPR GLTTVICDPH
     EIVNVMGEAG FAWFARCAEQ ARQNQYLQVS SCVPALEGCD VNGASFTLEQ MLAWRDHPQV
     TGLAEMMDYP GVISGQNALL DKLDAFRHLT LDGHCPGLGG KELNAYIAAG IENCHESYQL
     EEGRRKLQLG MSLMIREGSA ARNLNALAPL INEFNSPQCM LCTDDRNPWE IAHEGHIDAL
     IRRLIEQHNV PLHVAYRVAS WSTARHFGLN HLGLLAPGKQ ADIVLLSDAR KVTVQQVLVK
     GEPIDAQTLQ AEESAKLAQS APPYGNTIAR QPVSASDFAL QFTPGKRYRV IDVIHNELIT
     HSHSSVYSEN GFERNDVCFI AVLERYGQRL APACGLLGGF GLNEGALAAT VSHDSHNIVV
     IGRSAEEMAL AVNQVIQDGG GLCVVRNGQV QSHLPLPIAG LMSTDTAQSL AEQIDALKAA
     ARECGPLPDE PFIQMAFLSL PVIPALKLTS QGLFDGEKFA FTTLEVTE