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ADEC_PETMO
ID   ADEC_PETMO              Reviewed;         570 AA.
AC   A9BIU9;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   15-JAN-2008, sequence version 1.
DT   25-MAY-2022, entry version 81.
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=Pmob_1744;
OS   Petrotoga mobilis (strain DSM 10674 / SJ95).
OC   Bacteria; Thermotogae; Petrotogales; Petrotogaceae; Petrotoga.
OX   NCBI_TaxID=403833;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 10674 / SJ95;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA   Tice H., Pitluck S., Meincke L., Brettin T., Bruce D., Detter J.C., Han C.,
RA   Kuske C.R., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Mikhailova N., Noll K., Richardson P.;
RT   "Complete sequence of Petroga mobilis SJ95.";
RL   Submitted (NOV-2007) 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}.
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DR   EMBL; CP000879; ABX32437.1; -; Genomic_DNA.
DR   RefSeq; WP_012209534.1; NC_010003.1.
DR   AlphaFoldDB; A9BIU9; -.
DR   SMR; A9BIU9; -.
DR   STRING; 403833.Pmob_1744; -.
DR   EnsemblBacteria; ABX32437; ABX32437; Pmob_1744.
DR   KEGG; pmo:Pmob_1744; -.
DR   eggNOG; COG1001; Bacteria.
DR   HOGENOM; CLU_027935_0_0_0; -.
DR   OMA; TDHECFT; -.
DR   OrthoDB; 751534at2; -.
DR   Proteomes; UP000000789; 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..570
FT                   /note="Adenine deaminase"
FT                   /id="PRO_1000146245"
SQ   SEQUENCE   570 AA;  63017 MW;  E67688FB62EE2F46 CRC64;
     MSNKDLLPIA LGKEKADLVF KNGKIIDVFN EKVIEEDLAI SNGVIIGFGK YEGKEEVDLE
     GKFISPGFID AHLHLESAMV TIEEFAKTVI PLGTLTLVAD PHEIANVAGK VGIKYFLTIG
     NNIPWNFNLM VPSCVPVTTF DKSGSVLNAE KIKELITEEN FFGLGEVMDY EGVITGQDYI
     WDKIELMKDY FIDGHAPKLQ GKILNAYLLA GIMADHETTS PNEALEKISK GMYIMVREGS
     VTRDLQSLLP AINDKNNCNF LFATDDKHPE DLISEGHINF MIKKAIKLGM EPFRAIKLAT
     LNAARSLGLH RLGGIAPGYK ADLLIIDNLD ELGIFQVYKD GKKVAENGKA LFQVNSNNFE
     RPPTIFHSVN IAPIREEDFK IPKGKTYRVI NMIQDQIITG EDFFSFPDSF EEERFIRYNI
     NKIAVVERHK STGKIGLGLI RGFGLESGAI ASSIAHDSHN IIVLGTNSCD MKIAVEKIAE
     IQGGIVIANN QKIVDFIELP IGGLISTDPI GKVSEKLQEL RKIVHNLGVK TNSPFMTLAF
     MGLPVVPKLK ITCDGLYDVE NHIFVSLVVN
 
 
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