ID   ADEC_RUEPO              Reviewed;         603 AA.
AC   Q5LM18;
DT   12-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT   14-OCT-2015, sequence version 2.
DT   25-MAY-2022, entry version 92.
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=SPO3746;
OS   Ruegeria pomeroyi (strain ATCC 700808 / DSM 15171 / DSS-3) (Silicibacter
OS   pomeroyi).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC   Roseobacteraceae; Ruegeria.
OX   NCBI_TaxID=246200;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700808 / DSM 15171 / DSS-3;
RX   PubMed=15602564; DOI=10.1038/nature03170;
RA   Moran M.A., Buchan A., Gonzalez J.M., Heidelberg J.F., Whitman W.B.,
RA   Kiene R.P., Henriksen J.R., King G.M., Belas R., Fuqua C., Brinkac L.M.,
RA   Lewis M., Johri S., Weaver B., Pai G., Eisen J.A., Rahe E., Sheldon W.M.,
RA   Ye W., Miller T.R., Carlton J., Rasko D.A., Paulsen I.T., Ren Q.,
RA   Daugherty S.C., DeBoy R.T., Dodson R.J., Durkin A.S., Madupu R.,
RA   Nelson W.C., Sullivan S.A., Rosovitz M.J., Haft D.H., Selengut J., Ward N.;
RT   "Genome sequence of Silicibacter pomeroyi reveals adaptations to the marine
RT   environment.";
RL   Nature 432:910-913(2004).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=ATCC 700808 / DSM 15171 / DSS-3;
RX   PubMed=25780504; DOI=10.1186/1944-3277-9-11;
RA   Rivers A.R., Smith C.B., Moran M.A.;
RT   "An updated genome annotation for the model marine bacterium Ruegeria
RT   pomeroyi DSS-3.";
RL   Stand. Genomic Sci. 9:11-11(2014).
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CP000031; AAV96967.2; -; Genomic_DNA.
DR   RefSeq; WP_030003271.1; NC_003911.12.
DR   AlphaFoldDB; Q5LM18; -.
DR   SMR; Q5LM18; -.
DR   STRING; 246200.SPO3746; -.
DR   EnsemblBacteria; AAV96967; AAV96967; SPO3746.
DR   KEGG; sil:SPO3746; -.
DR   eggNOG; COG1001; Bacteria.
DR   HOGENOM; CLU_027935_0_0_5; -.
DR   OMA; MVTACAY; -.
DR   OrthoDB; 751534at2; -.
DR   Proteomes; UP000001023; 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..603
FT                   /note="Adenine deaminase"
FT                   /id="PRO_0000142437"
SQ   SEQUENCE   603 AA;  64109 MW;  DE5B2FDFF8106791 CRC64;
     MEPTTFPSWA DVAPRLVAVA AGREPADMII RNGTWINVHT REALPGHSIA IAEGRIAFVG
     PDASHCSGPD TRIIEANGRY MIPGLCDGHM HIESGMLTPA EFAAAVIPHG TTTMFTDPHE
     IANVLGLAGV RMMHDEALMQ PVNIFTQMPS CAPSAPGLET TGYEITPEDV AEAMTWPGII
     GLGEMMNFPG VTNADPKMLA EIAATQRAGK TVGGHYASPD LGPAFAAYVA GGPADDHEGT
     CEADAIARVR QGMRSMMRLG SAWYDVETQI TAVTEKGLDP RNFILCTDDC HSATLVNDGH
     MNRVVRHAIA CGCDPLIALQ MATINTATHF GLERELGSTA PGRRADVILT SDLRDLPIEL
     VIARGQVVAE NGKIAVDCPH YDWPDTARGT VHLGHALSAR DFEIAAPTGA NRVRANVIGV
     VENQAPTKAL KAELPVREGL VETAEHPDDV CQIALVERHR ATGGVTNAFV SGFGYQGRMA
     MASTVAHDSH HMIVVGTDRE QMALAANRLA EVGGGITIWR DGQELALVEL PIAGLMSDSP
     AAEVAAKAQA MVEAMAACGC TLNNAYMQHS LLALVVIPEL RISDLGLIDV RSFERIDLLE
     PLA