ID   ADEC_BACSU              Reviewed;         577 AA.
AC   P39761;
DT   01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT   16-JUN-2009, sequence version 2.
DT   03-AUG-2022, entry version 135.
DE   RecName: Full=Adenine deaminase;
DE            Short=Adenase;
DE            Short=Adenine aminase;
DE            EC=3.5.4.2;
GN   Name=adeC; Synonyms=ade, yzaD; OrderedLocusNames=BSU14520;
OS   Bacillus subtilis (strain 168).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=224308;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=168 / JH642;
RA   Kobayashi K., Sato T., Kobayashi Y.;
RT   "The nucleotide sequence analysis of kinC region.";
RL   Submitted (JUL-1994) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], CATALYTIC ACTIVITY, AND COFACTOR.
RC   STRAIN=168;
RX   PubMed=8550522; DOI=10.1128/jb.178.3.846-853.1996;
RA   Nygaard P., Duckert P., Saxild H.H.;
RT   "Role of adenine deaminase in purine salvage and nitrogen metabolism and
RT   characterization of the ade gene in Bacillus subtilis.";
RL   J. Bacteriol. 178:846-853(1996).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=168;
RX   PubMed=8969500; DOI=10.1099/13500872-142-11-3033;
RA   Winters P., Caldwell R.M., Enfield L., Ferrari E.;
RT   "The ampS-nprE (124 degrees-127 degrees) region of the Bacillus subtilis
RT   168 chromosome: sequencing of a 27 kb segment and identification of several
RT   genes in the area.";
RL   Microbiology 142:3033-3037(1996).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=168;
RX   PubMed=9384377; DOI=10.1038/36786;
RA   Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA   Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA   Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA   Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA   Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA   Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA   Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA   Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA   Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA   Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA   Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA   Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA   Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA   Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA   Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA   Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA   Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA   Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA   Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA   Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA   Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA   Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA   Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA   Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA   Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA   Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA   Yoshikawa H., Danchin A.;
RT   "The complete genome sequence of the Gram-positive bacterium Bacillus
RT   subtilis.";
RL   Nature 390:249-256(1997).
RN   [5]
RP   SEQUENCE REVISION TO 262-265.
RX   PubMed=19383706; DOI=10.1099/mic.0.027839-0;
RA   Barbe V., Cruveiller S., Kunst F., Lenoble P., Meurice G., Sekowska A.,
RA   Vallenet D., Wang T., Moszer I., Medigue C., Danchin A.;
RT   "From a consortium sequence to a unified sequence: the Bacillus subtilis
RT   168 reference genome a decade later.";
RL   Microbiology 155:1758-1775(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:0000269|PubMed:8550522};
CC   -!- COFACTOR:
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000269|PubMed:8550522};
CC   -!- SIMILARITY: Belongs to the metallo-dependent hydrolases superfamily.
CC       Adenine deaminase family. {ECO:0000305}.
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DR   EMBL; D37799; BAA07052.1; -; Genomic_DNA.
DR   EMBL; X83795; CAA58726.1; -; Genomic_DNA.
DR   EMBL; AF012285; AAC24927.1; -; Genomic_DNA.
DR   EMBL; AL009126; CAB13325.2; -; Genomic_DNA.
DR   PIR; B69583; B69583.
DR   RefSeq; NP_389335.2; NC_000964.3.
DR   RefSeq; WP_003245362.1; NZ_JNCM01000035.1.
DR   AlphaFoldDB; P39761; -.
DR   SMR; P39761; -.
DR   STRING; 224308.BSU14520; -.
DR   PRIDE; P39761; -.
DR   EnsemblBacteria; CAB13325; CAB13325; BSU_14520.
DR   GeneID; 939477; -.
DR   KEGG; bsu:BSU14520; -.
DR   PATRIC; fig|224308.179.peg.1582; -.
DR   eggNOG; COG1001; Bacteria.
DR   InParanoid; P39761; -.
DR   OMA; TDHECFT; -.
DR   PhylomeDB; P39761; -.
DR   BioCyc; BSUB:BSU14520-MON; -.
DR   BioCyc; MetaCyc:BSU14520-MON; -.
DR   Proteomes; UP000001570; Chromosome.
DR   GO; GO:0000034; F:adenine deaminase activity; IBA:GO_Central.
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   1: Evidence at protein level;
KW   Hydrolase; Manganese; Reference proteome.
FT   CHAIN           1..577
FT                   /note="Adenine deaminase"
FT                   /id="PRO_0000142404"
FT   CONFLICT        193
FT                   /note="A -> G (in Ref. 2; CAA58726)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        231
FT                   /note="D -> Y (in Ref. 2; CAA58726)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        262..265
FT                   /note="ARRF -> RTPV (in Ref. 1; BAA07052 and 3; AAC24927)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   577 AA;  62892 MW;  5AC8BCFAC7FE8CA9 CRC64;
     MNKEALVNRL NASAKRQKAD IVIKNGKIMD VYNQEWIYED IAITDGVIVG LGEYEGENII
     DAEGQMIVPG FIDGHVHIES SMVTPIEFAK AVLPHGVTTV VTDPHEIANV SGEKGIEFML
     EQARHTPLNI HFMLPSSVPA ASFERSGAIL KAADLKPFYE EEEVLGLAEV MDYVSVQQAE
     KDMVQKLLDA RVAGKRIDGH LAGLSTDLIN IYRTAFVLND HEVTSKEEAL DRIRRGMYVM
     MREGSVAKNT LNVLPAVNEK NARRFFFCTD DKHVDDLLSE GSVNHQVKMA IQAGLNPFLA
     YQLGSLNAAE CYGLDTKGAI APGFDADLLF VSDLENVTVT MTMVKGQTVA EDSKAVYQDH
     ASTAAPDQAL LDSVKLAAPL NKQDFHMPID SEQQINVIQI IPNQLETRLV QVPAPVAREF
     EPDTELDLLK IAVVERHKGL KETGLGVVKG FGFKSGAIAT TISHDSHNII AVGTNDEDIA
     AAVNKLQEIG GGLTIIKNGE ELHSVPLPIA GLLSDQSAEQ VNQSLLTLHD KLSLIGFTGG
     FNPFLTLSFL ALPVIPDIKM TTTGLFDVKS FQHISLQ