ID   ADEC3_RHIL3             Reviewed;         600 AA.
AC   Q1M901;
DT   26-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT   30-MAY-2006, sequence version 1.
DT   25-MAY-2022, entry version 84.
DE   RecName: Full=Adenine deaminase 3 {ECO:0000255|HAMAP-Rule:MF_01518};
DE            Short=Adenase 3 {ECO:0000255|HAMAP-Rule:MF_01518};
DE            Short=Adenine aminase 3 {ECO:0000255|HAMAP-Rule:MF_01518};
DE            EC=3.5.4.2 {ECO:0000255|HAMAP-Rule:MF_01518};
GN   Name=ade3 {ECO:0000255|HAMAP-Rule:MF_01518}; OrderedLocusNames=RL4472;
GN   and
GN   Name=ade4 {ECO:0000255|HAMAP-Rule:MF_01518}; OrderedLocusNames=pRL90169;
OS   Rhizobium leguminosarum bv. viciae (strain 3841).
OG   Plasmid pRL9.
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Rhizobiaceae; Rhizobium/Agrobacterium group; Rhizobium.
OX   NCBI_TaxID=216596;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=3841;
RX   PubMed=16640791; DOI=10.1186/gb-2006-7-4-r34;
RA   Young J.P.W., Crossman L.C., Johnston A.W.B., Thomson N.R., Ghazoui Z.F.,
RA   Hull K.H., Wexler M., Curson A.R.J., Todd J.D., Poole P.S., Mauchline T.H.,
RA   East A.K., Quail M.A., Churcher C., Arrowsmith C., Cherevach I.,
RA   Chillingworth T., Clarke K., Cronin A., Davis P., Fraser A., Hance Z.,
RA   Hauser H., Jagels K., Moule S., Mungall K., Norbertczak H.,
RA   Rabbinowitsch E., Sanders M., Simmonds M., Whitehead S., Parkhill J.;
RT   "The genome of Rhizobium leguminosarum has recognizable core and accessory
RT   components.";
RL   Genome Biol. 7:R34.1-R34.20(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; AM236083; CAK03886.1; -; Genomic_DNA.
DR   EMBL; AM236080; CAK09957.1; -; Genomic_DNA.
DR   RefSeq; WP_011649691.1; NC_008380.1.
DR   AlphaFoldDB; Q1M901; -.
DR   SMR; Q1M901; -.
DR   STRING; 216596.RL4472; -.
DR   EnsemblBacteria; CAK03886; CAK03886; pRL90169.
DR   EnsemblBacteria; CAK09957; CAK09957; RL4472.
DR   KEGG; rle:pRL90169; -.
DR   KEGG; rle:RL4472; -.
DR   eggNOG; COG1001; Bacteria.
DR   HOGENOM; CLU_027935_0_0_5; -.
DR   OMA; MVTACAY; -.
DR   OrthoDB; 751534at2; -.
DR   Proteomes; UP000006575; Chromosome.
DR   Proteomes; UP000006575; Plasmid pRL9.
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; Plasmid.
FT   CHAIN           1..600
FT                   /note="Adenine deaminase 3"
FT                   /id="PRO_0000292396"
SQ   SEQUENCE   600 AA;  64116 MW;  878205C5D6AB9CD9 CRC64;
     MSTLTRFSVQ PLSTMTRRLA DVASARREPD LVIQGARVLS TYSERFLDGR EVWISGGRIA
     AVKPAGSYRG GSAKLYDARG GIIAPGLVDP HIHIESSMVT ACAYAEAALL NGTTTIFCDS
     HEIGNVMDVA GVEAMLEDAR QAPLSIFLTV PSTVPATTPD LETAGGDLTP DKIAALFDKW
     PEAVALGEKM DFVPVAMGDE RSHAILAAAL GRGRPVSGHV YGREFVAAYA ASGVTDTHEA
     IDRGIADDLL EAGVWIFLRG GPPTTPWHSL PQAIKTITEL GASHKRVAVC TDDRDAEDLL
     AFGLDWVTRE AVKYGMRPEE AWAMGSLHGA TRFGMEGEIG GLGGGRRADL VLLSDDLTPV
     STWYGGKLVV DSKKITPILD EALSKPYRYP DAAYHTVKLP KNLKLTPDLP TETVVAHTIK
     TELPGITLGH VTVTLEPAND WQAHFDKHDL CFVTVVERHG KSAGNVAHGL LNGFGLRQGA
     VASSVGHDSH NIIVAGTNAA DMQVALDAIE EKQGGVCVVM DGKVTAMVPL PIAGLLSDKR
     VHQVADEVKA LKLEWEKAGC TIAYMGFNLI PLSVIPEIRI TDKGLVLVPE MVISPLFEKA