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