ID   ADEC2_RHIEC             Reviewed;         595 AA.
AC   Q2K4Q9;
DT   26-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT   07-MAR-2006, sequence version 1.
DT   25-MAY-2022, entry version 94.
DE   RecName: Full=Adenine deaminase 2 {ECO:0000255|HAMAP-Rule:MF_01518};
DE            Short=Adenase 2 {ECO:0000255|HAMAP-Rule:MF_01518};
DE            Short=Adenine aminase 2 {ECO:0000255|HAMAP-Rule:MF_01518};
DE            EC=3.5.4.2 {ECO:0000255|HAMAP-Rule:MF_01518};
GN   Name=ade2 {ECO:0000255|HAMAP-Rule:MF_01518}; Synonyms=adeC2;
GN   OrderedLocusNames=RHE_CH03420;
OS   Rhizobium etli (strain CFN 42 / ATCC 51251).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Rhizobiaceae; Rhizobium/Agrobacterium group; Rhizobium.
OX   NCBI_TaxID=347834;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CFN 42 / ATCC 51251;
RX   PubMed=16505379; DOI=10.1073/pnas.0508502103;
RA   Gonzalez V., Santamaria R.I., Bustos P., Hernandez-Gonzalez I.,
RA   Medrano-Soto A., Moreno-Hagelsieb G., Janga S.C., Ramirez M.A.,
RA   Jimenez-Jacinto V., Collado-Vides J., Davila G.;
RT   "The partitioned Rhizobium etli genome: genetic and metabolic redundancy in
RT   seven interacting replicons.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:3834-3839(2006).
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; CP000133; ABC92177.1; -; Genomic_DNA.
DR   RefSeq; WP_011426646.1; NC_007761.1.
DR   AlphaFoldDB; Q2K4Q9; -.
DR   SMR; Q2K4Q9; -.
DR   STRING; 347834.RHE_CH03420; -.
DR   EnsemblBacteria; ABC92177; ABC92177; RHE_CH03420.
DR   KEGG; ret:RHE_CH03420; -.
DR   eggNOG; COG1001; Bacteria.
DR   HOGENOM; CLU_027935_0_0_5; -.
DR   OMA; IEGHFPG; -.
DR   Proteomes; UP000001936; Chromosome.
DR   GO; GO:0000034; F:adenine deaminase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006146; P:adenine catabolic process; IEA:InterPro.
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.
PE   3: Inferred from homology;
KW   Hydrolase; Manganese; Reference proteome.
FT   CHAIN           1..595
FT                   /note="Adenine deaminase 2"
FT                   /id="PRO_0000292393"
SQ   SEQUENCE   595 AA;  62579 MW;  E94689C9F6409813 CRC64;
     MNAIARQEPF DLNDPALRAR AVAAARGDAP FDMLITGGRL LDAVTGLIRE ADIGLVGALI
     ASVHAPASRT DAVEIIDATG GILTPGLIDM HMHVESSMVT PAEYASAVLP HGVTTVVWDP
     HEFGNVQGLD GVRWAIEAAR TLPLRMILLA PSCVPSAPGL ELAGADFDAA VIAEMLRSPA
     VGGVAEVMNM RGVIDGDPRM SAIVNSGLAS GKLVCGHARG LTGADLNAFM AAGVTSDHEL
     TSGADLAAKL SAGLTIELRG SHDHLLQEFV EVLNGLGHLP ATVTLCTDDV FPDELYQSGG
     LDEVARRLVR YGMKPEWALR AATFNAAQRL KRSDLGLVAS GRRADLVLFE DLTELRARLV
     ISDGRIVARN GSMEAAVQPL DTAPLINSTK LPPLTESDFR VPAKGARVRI ATIDRPRFTQ
     WGEAETEIRD GFVVPPAGSA MIAVAHRHGK AGGTPRIGFL TGWGEWRGAF CTTVSHDSHN
     LTVFGGDARD MALAANAVIK AGGGLAVAKD GAIQAILPLP LSGLVTDASL KDTASAFSDI
     RKAMDKIVDW KPPYRVFKAC FGATLACNAG PHQTDRGIAD VTTGKVLESP VLEIF