ID   ADEC_BACVZ              Reviewed;         577 AA.
AC   A7Z463;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   23-OCT-2007, sequence version 1.
DT   03-AUG-2022, entry version 87.
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=RBAM_014260;
OS   Bacillus velezensis (strain DSM 23117 / BGSC 10A6 / LMG 26770 / FZB42)
OS   (Bacillus amyloliquefaciens subsp. plantarum).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC   Bacillus amyloliquefaciens group.
OX   NCBI_TaxID=326423;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 23117 / BGSC 10A6 / LMG 26770 / FZB42;
RX   PubMed=17704766; DOI=10.1038/nbt1325;
RA   Chen X.H., Koumoutsi A., Scholz R., Eisenreich A., Schneider K.,
RA   Heinemeyer I., Morgenstern B., Voss B., Hess W.R., Reva O., Junge H.,
RA   Voigt B., Jungblut P.R., Vater J., Suessmuth R., Liesegang H.,
RA   Strittmatter A., Gottschalk G., Borriss R.;
RT   "Comparative analysis of the complete genome sequence of the plant growth-
RT   promoting bacterium Bacillus amyloliquefaciens FZB42.";
RL   Nat. Biotechnol. 25:1007-1014(2007).
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; CP000560; ABS73789.1; -; Genomic_DNA.
DR   RefSeq; WP_012117460.1; NC_009725.2.
DR   AlphaFoldDB; A7Z463; -.
DR   SMR; A7Z463; -.
DR   STRING; 326423.RBAM_014260; -.
DR   PRIDE; A7Z463; -.
DR   EnsemblBacteria; ABS73789; ABS73789; RBAM_014260.
DR   KEGG; bay:RBAM_014260; -.
DR   HOGENOM; CLU_027935_0_0_9; -.
DR   OMA; TDHECFT; -.
DR   Proteomes; UP000001120; 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..577
FT                   /note="Adenine deaminase"
FT                   /id="PRO_1000068607"
SQ   SEQUENCE   577 AA;  62496 MW;  F22BF739CDAB3E09 CRC64;
     MNKETLAERL NASAGRQKAD TVIKNGKIMD VFNQEWISAD IAITGGVIVG LGEYEGEEVI
     DAEGQMIVPG FIDGHVHIES SMVTPIEFAK AVLPHGVTTV ITDPHEIANV SGAKGISFMI
     EQAKKAPLNI RFMLPSCVPA ASFERSGAVL KAEDLKPFYQ EKEVLGLAEV MDYVSVAEGE
     EDMLQKLLDA KRHGKRIDGH LAGLSSDIIN IYRTAMVSND HEVTTKEEAL DRIRRGMYVM
     LREGSVAKNT LNVLPAVNEK NARRFFFCTD DKHVDDLLSE GSVNHQVKMA IKAGLDPFLA
     YQLASLNAAE CYGLETKGAV APGFDADLLF ISDVREAVVT KTMVAGRTVA ENGRTVYEQS
     AGSYSPDQAL LDTVRLKAPL TESDFHIPIQ EGKKMNVIEM IPNHLETRKK EVPAPSADAF
     CPDTENDLLK IAVAERHSGE KMIGLGIVQG FGLKEGAIAT TISHDSHNII AVGTNDADLA
     KAINRLRDTG GGLTAVKNGE LLHSVPLPIA GLLSDKSAEW VNDSLGVLHE KLPLLGFTGD
     FNPFLTLSFL ALPVIPDIKM TAAGLFDVKA FQHIPLQ