ADEC_DESRM
ID ADEC_DESRM Reviewed; 588 AA.
AC A4J872;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2007, sequence version 1.
DT 03-AUG-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=Dred_2771;
OS Desulforamulus reducens (strain ATCC BAA-1160 / DSM 100696 / MI-1)
OS (Desulfotomaculum reducens).
OC Bacteria; Firmicutes; Clostridia; Eubacteriales; Peptococcaceae;
OC Desulforamulus.
OX NCBI_TaxID=349161;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-1160 / DSM 100696 / MI-1;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Sims D., Brettin T., Bruce D., Han C., Tapia R., Schmutz J., Larimer F.,
RA Land M., Hauser L., Kyrpides N., Kim E., Tebo B.M., Richardson P.;
RT "Complete sequence of Desulfotomaculum reducens MI-1.";
RL Submitted (MAR-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; CP000612; ABO51275.1; -; Genomic_DNA.
DR RefSeq; WP_011879070.1; NC_009253.1.
DR AlphaFoldDB; A4J872; -.
DR SMR; A4J872; -.
DR STRING; 349161.Dred_2771; -.
DR EnsemblBacteria; ABO51275; ABO51275; Dred_2771.
DR KEGG; drm:Dred_2771; -.
DR eggNOG; COG1001; Bacteria.
DR HOGENOM; CLU_027935_0_0_9; -.
DR OMA; CHETTTK; -.
DR OrthoDB; 751534at2; -.
DR Proteomes; UP000001556; 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; Reference proteome.
FT CHAIN 1..588
FT /note="Adenine deaminase"
FT /id="PRO_1000073537"
SQ SEQUENCE 588 AA; 63394 MW; 80586A767D668293 CRC64;
MLGDVASLAE ELRVAAGQEP ADLYIKNIQI VDVYTETIFS GSLVIKNGKI VAVNPGWEVE
AKEVFDGKGR FAVPGFMDAH IHIEPTLLSP EALASVIVPW GTTTLFADPM EIANVAGLKG
VEALLNNTEN LPYQIYIEVP SRVPTAPGLE TTGGVLGVKE VDQLLQSNIS ASLGELDPSK
ILSIKEEYLA KIVSARANGK VANGHAIGLN WDQLNVYATA GLSDDHESVV FQELFERLRL
GIKALVREGS TERNVEALVK GAIEQNLSTE NLIFCTDDKH VNDIVREGHI SFNVQKAIAL
GLNPIKAIQM ATINTAKHFR LDHYLGALTP GKVADIVLLD DLVEIKPAYV FKNGKLVAQG
GKLTQQIEIS QYPAFLNETV KLPPNLAPTS FALPSQGNRC KVNVINLYPD QIINFASQEW
LNVAGGEVQV NTNEDILKLA VVERYGKNGS VGVGFVRGFK LKAGALASSV SHDHHNIVIV
GTNDQDMDLA AREIARHQGG LVAVENGQVI GVLPLPIGGL MSSLPAEQVM SQIDQLNKKA
EQLGCDLPAP FMTLSFISLP TVPELGLTDC GLIHVLEHRI IPTVVETE
