ID   ADEC_SINFN              Reviewed;         565 AA.
AC   C3MG57;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   16-JUN-2009, sequence version 1.
DT   25-MAY-2022, entry version 83.
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=NGR_c23700;
OS   Sinorhizobium fredii (strain NBRC 101917 / NGR234).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Rhizobiaceae; Sinorhizobium/Ensifer group; Sinorhizobium.
OX   NCBI_TaxID=394;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NBRC 101917 / NGR234;
RX   PubMed=19376903; DOI=10.1128/aem.00515-09;
RA   Schmeisser C., Liesegang H., Krysciak D., Bakkou N., Le Quere A.,
RA   Wollherr A., Heinemeyer I., Morgenstern B., Pommerening-Roeser A.,
RA   Flores M., Palacios R., Brenner S., Gottschalk G., Schmitz R.A.,
RA   Broughton W.J., Perret X., Strittmatter A.W., Streit W.R.;
RT   "Rhizobium sp. strain NGR234 possesses a remarkable number of secretion
RT   systems.";
RL   Appl. Environ. Microbiol. 75:4035-4045(2009).
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; CP001389; ACP26129.1; -; Genomic_DNA.
DR   RefSeq; WP_012708887.1; NC_012587.1.
DR   RefSeq; YP_002826882.1; NC_012587.1.
DR   AlphaFoldDB; C3MG57; -.
DR   SMR; C3MG57; -.
DR   STRING; 394.NGR_c23700; -.
DR   EnsemblBacteria; ACP26129; ACP26129; NGR_c23700.
DR   KEGG; rhi:NGR_c23700; -.
DR   PATRIC; fig|394.7.peg.5189; -.
DR   eggNOG; COG1001; Bacteria.
DR   HOGENOM; CLU_027935_0_0_5; -.
DR   OMA; TDHECFT; -.
DR   OrthoDB; 751534at2; -.
DR   Proteomes; UP000001054; 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..565
FT                   /note="Adenine deaminase"
FT                   /id="PRO_1000185090"
SQ   SEQUENCE   565 AA;  60956 MW;  4EE4343BBB380DCD CRC64;
     MSEALERFID QGIGRKPADI VLKGGRFFDL VTGELVASDI AISGDRIVGT CGDYEGREEI
     DVSGRIVVPG FIDTHLHIES SLVTPHEFDR CVLPLGITTA ICDPHEIANV LGTEGIQFFL
     DSAMETIMDI RVQLSSCVPA THLETAGADL PIERLTPFRH HPKVIGLAEF MNFPGVIHKD
     PICLAKLDAF QGGHIDGHAP LLRGKELNGY LATGIRTDHE CTSAEEALEK IRKGMHILVR
     EGSVSKDLQA LMPIITERLS PHLALCTDDR NPLDIAEQGH LDHMIRTAIA AGVEPLAIYR
     AASISAARAF GLSDRGLVAP GWRADLVVLD SLENCKAEMV FSGGRRVTDA LFARRKPVEP
     VGLDSVKARE VKAADFGVPY SEVETSVIGV LPGKIITEHR RYRLPAVGNQ TGPDLGRDII
     KVAVIERHGV NGNHANGFVQ GFGLKKGAIA STVGHDSHNI CVVGVSEEDM ALAANRLGAI
     KGGFVVVEDG RVTGEIALPI AGLMSLEPYE RVRDILHHLR QAAFALGATL EEPFLQLAFL
     PLPVIPHLKI SDRGLVDVDK FALIG