ID   ADEC_PARDP              Reviewed;         597 AA.
AC   A1B5X6;
DT   26-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 1.
DT   25-MAY-2022, entry version 79.
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=Pden_2836;
OS   Paracoccus denitrificans (strain Pd 1222).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC   Rhodobacteraceae; Paracoccus.
OX   NCBI_TaxID=318586;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Pd 1222;
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   Munk A.C., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Lykidis A., Spiro S.,
RA   Richardson D.J., Moir J.W.B., Ferguson S.J., van Spanning R.J.M.,
RA   Richardson P.;
RT   "Complete sequence of chromosome 2 of Paracoccus denitrificans PD1222.";
RL   Submitted (DEC-2006) 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; CP000490; ABL70920.1; -; Genomic_DNA.
DR   RefSeq; WP_011749111.1; NC_008687.1.
DR   AlphaFoldDB; A1B5X6; -.
DR   SMR; A1B5X6; -.
DR   STRING; 318586.Pden_2836; -.
DR   PRIDE; A1B5X6; -.
DR   EnsemblBacteria; ABL70920; ABL70920; Pden_2836.
DR   KEGG; pde:Pden_2836; -.
DR   eggNOG; COG1001; Bacteria.
DR   HOGENOM; CLU_027935_0_0_5; -.
DR   OMA; MVTACAY; -.
DR   Proteomes; UP000000361; Chromosome 2.
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..597
FT                   /note="Adenine deaminase"
FT                   /id="PRO_0000292391"
SQ   SEQUENCE   597 AA;  62923 MW;  B2A9C858E78F1AF5 CRC64;
     MNKETGMLKP WIEAQARLVE VAAGRAPADL VIRGGQWVNV HTREVIPGMD VAVADGRVAY
     VGPDAGPSVG PGTQVIEADG RFMVPGLIDA HMHVESGMLT PAGFAAAVIP HGTTTIFHDP
     HEIANVLGLE GVRLMRDESL LQPISMFTQM PSCAPSAPGL ETTGQPITEG EVAQAMGWDG
     IVGLGEMMNF PGVASGDRQM LTEIAATRAA GKTVGGHYAS PDLGRPFHAY VAGGANDDHE
     TTTEAQGIAR VRQGMGCMMR LGSAWYDVES QITAITEKGL DPRFFILCTD DSHSGTLVND
     GHMNRVVRHA VDCGCDPLVA IQMATINAAS HFGLERELGS ITPGRRADVI LTSDLRSLPI
     ETVIAQGVVV AETGKLLVDC PRIAWPEAAR DSVHLGRSLT GADFAVRATG DSARVRVIGV
     VENQAPTRAL TAQLPIRDGV VEPQGETCHI ALVERHRGTG GVVNGFVSGF GYQGRMAVAS
     TVAHDSHHMI VVGTDRDSMA AAANHLGRIG GGVTVFRDGE ELATVALPIA GLMSDRPAAE
     VAEAAQGIVK AMQDCGCTLN NAYMQHSLLA LVVIPELRIS DLGIVDVTRF ELVDLMV