ID   ADEC_CLOB6              Reviewed;         599 AA.
AC   C3KZB6;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   16-JUN-2009, sequence version 1.
DT   25-MAY-2022, entry version 64.
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=CLJ_B0349;
OS   Clostridium botulinum (strain 657 / Type Ba4).
OC   Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=515621;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=657 / Type Ba4;
RA   Shrivastava S., Brown J.L., Bruce D., Detter C., Munk C., Smith L.A.,
RA   Smith T.J., Sutton G., Brettin T.S.;
RT   "Genome sequence of Clostridium botulinum Ba4 strain 657.";
RL   Submitted (MAY-2008) to the EMBL/GenBank/DDBJ databases.
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CP001083; ACQ52836.1; -; Genomic_DNA.
DR   RefSeq; WP_003360406.1; NC_012658.1.
DR   AlphaFoldDB; C3KZB6; -.
DR   SMR; C3KZB6; -.
DR   EnsemblBacteria; ACQ52836; ACQ52836; CLJ_B0349.
DR   KEGG; cbi:CLJ_B0349; -.
DR   HOGENOM; CLU_027935_0_0_9; -.
DR   OMA; TDHECFT; -.
DR   Proteomes; UP000002333; 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..599
FT                   /note="Adenine deaminase"
FT                   /id="PRO_1000215358"
SQ   SEQUENCE   599 AA;  65348 MW;  245CA1460EC26D4B CRC64;
     MFNKFNTKPL WEVSKTLSSV AQGFEPADMV IINSRLINVC TREVIENTDV AISCGRIALV
     GDAKHCIGES TEVIDAKGQY IAPGFLDGHI HVESSMLSVS EYARSVVPHG TVGIYMDPHE
     ICNVLGLNGV RYMIEDGKGT PLKNMVTTPS CVPAVPGFED TGAAVGPEDV RETMKWDEIV
     GLGEMMNFPG ILYSTDHAHG VVGETLKASK TVTGHYSLPE TGKGLNGYIA SGVRCCHEST
     RAEDALAKMR LGMYAMFREG SAWHDLKEVS KAITENKVDS RFAVLISDDT HPHTLLKDGH
     LDHIIKRAIE EGIEPLTAIQ MVTINCAQCF QMDHELGSIT PGKCADIVLI EDLKDVKITK
     VIIDGNLVAK DGVLTTSIAK YDYPEDAMHS MHIKDKITPA SFNIMAQNKE KVTTRVIEII
     PERVGTYERH IELNVKDDKV QCDPSKDVLK AVVFERHHET GKAGYGFVKG FGIKRGAMAA
     TVAHDAHNLL VIGTNDEDMA LAANTLIECG GGMVAVQDGK VLGLVPLPIA GLMSNKPLEE
     MAEMVEKLDS AWKEIGCDIV SPFMTMALIP LACLPELRLT NRGLVDCNKF EFVSLFIEE