ID   ADEC2_OENOB             Reviewed;         567 AA.
AC   Q04DZ9;
DT   26-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT   14-NOV-2006, sequence version 1.
DT   25-MAY-2022, entry version 80.
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}; OrderedLocusNames=OEOE_1462;
OS   Oenococcus oeni (strain ATCC BAA-331 / PSU-1).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Oenococcus.
OX   NCBI_TaxID=203123;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-331 / PSU-1;
RX   PubMed=17030793; DOI=10.1073/pnas.0607117103;
RA   Makarova K.S., Slesarev A., Wolf Y.I., Sorokin A., Mirkin B., Koonin E.V.,
RA   Pavlov A., Pavlova N., Karamychev V., Polouchine N., Shakhova V.,
RA   Grigoriev I., Lou Y., Rohksar D., Lucas S., Huang K., Goodstein D.M.,
RA   Hawkins T., Plengvidhya V., Welker D., Hughes J., Goh Y., Benson A.,
RA   Baldwin K., Lee J.-H., Diaz-Muniz I., Dosti B., Smeianov V., Wechter W.,
RA   Barabote R., Lorca G., Altermann E., Barrangou R., Ganesan B., Xie Y.,
RA   Rawsthorne H., Tamir D., Parker C., Breidt F., Broadbent J.R., Hutkins R.,
RA   O'Sullivan D., Steele J., Unlu G., Saier M.H. Jr., Klaenhammer T.,
RA   Richardson P., Kozyavkin S., Weimer B.C., Mills D.A.;
RT   "Comparative genomics of the lactic acid bacteria.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:15611-15616(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}.
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; CP000411; ABJ57323.1; -; Genomic_DNA.
DR   RefSeq; WP_011677717.1; NC_008528.1.
DR   AlphaFoldDB; Q04DZ9; -.
DR   SMR; Q04DZ9; -.
DR   STRING; 203123.OEOE_1462; -.
DR   EnsemblBacteria; ABJ57323; ABJ57323; OEOE_1462.
DR   KEGG; ooe:OEOE_1462; -.
DR   PATRIC; fig|203123.7.peg.1482; -.
DR   eggNOG; COG1001; Bacteria.
DR   HOGENOM; CLU_027935_0_0_9; -.
DR   OMA; MVTACAY; -.
DR   OrthoDB; 751534at2; -.
DR   Proteomes; UP000000774; 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..567
FT                   /note="Adenine deaminase 2"
FT                   /id="PRO_0000292390"
SQ   SEQUENCE   567 AA;  62656 MW;  A544B8689616BC2E CRC64;
     MIKADLKIIN GQIYNTFTRQ FTAKEVAIVD GKFFQIADKL SDDFKFEDIL DLKGSYVIPG
     LIDSHMHIES SMATPTNFSE TAIRFGTTTV IADAHEIANT SGIKGLKRFM DQPSLIDTFF
     AIPSSVPSTN PELETTGGII DLEEVKELLA DPRIICLGEA MNFKGITSEP NSLIRKIIAL
     CQKKRPRMPL EGHVPNISKE DLAKFIFAGI LSDHTQQTPA LIKEKIENGM FIQLQKKSLN
     KENIETIVKN HFYDYSALVT DDTMADDLIN GHLNSIIKLA VKCGLPLEWA IYMTTYTPAQ
     HMHFQDRGVI APGKIADFVV LNNLDGFSIK NVYKRGVPID KLSIDDEKPF ASEEYHSIYV
     PNRSAKDFTL RVSKDLKKIT ANVIEIAAKG TFTKAVKKEL LVKDGIVDWQ KAGLALLAVQ
     ERYGKTGQLT LALVSKSINK SGAIATTWAH DHHNLMVLGT NPDSMAIAYD KVASQQGGYL
     VVKDKEIVAN VQLPIAGIIS DEPIDIIGHK LKKVRLAMKD LGYVNTNEIM SLSTLSLLVS
     PSIKVSDKGI FDVKTQTKIP LLLAGEE