ID   K7RXA2_ACIA4            Unreviewed;       355 AA.
AC   K7RXA2;
DT   06-FEB-2013, integrated into UniProtKB/TrEMBL.
DT   06-FEB-2013, sequence version 1.
DT   27-MAR-2024, entry version 52.
DE   RecName: Full=adenosine deaminase {ECO:0000256|ARBA:ARBA00012784};
DE            EC=3.5.4.4 {ECO:0000256|ARBA:ARBA00012784};
GN   OrderedLocusNames=PACID_33280 {ECO:0000313|EMBL:AFV91086.1};
OS   Acidipropionibacterium acidipropionici (strain ATCC 4875 / DSM 20272 / JCM
OS   6432 / NBRC 12425 / NCIMB 8070 / 4) (Propionibacterium acidipropionici).
OC   Bacteria; Actinomycetota; Actinomycetes; Propionibacteriales;
OC   Propionibacteriaceae; Acidipropionibacterium.
OX   NCBI_TaxID=1171373 {ECO:0000313|EMBL:AFV91086.1, ECO:0000313|Proteomes:UP000000214};
RN   [1] {ECO:0000313|EMBL:AFV91086.1, ECO:0000313|Proteomes:UP000000214}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 4875 / DSM 20272 / JCM 6432 / NBRC 12425 / NCIMB 8070
RC   {ECO:0000313|Proteomes:UP000000214};
RX   PubMed=23083487; DOI=10.1186/1471-2164-13-562;
RA   Parizzi L.P., Grassi M.C., Llerena L.A., Carazzolle M.F., Queiroz V.L.,
RA   Lunardi I., Zeidler A.F., Teixeira P.J., Mieczkowski P., Rincones J.,
RA   Pereira G.A.;
RT   "The genome sequence of Propionibacterium acidipropionici provides insights
RT   into its biotechnological and industrial potential.";
RL   BMC Genomics 13:562-562(2012).
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|ARBA:ARBA00001947};
CC   -!- SIMILARITY: Belongs to the metallo-dependent hydrolases superfamily.
CC       Adenosine and AMP deaminases family. {ECO:0000256|ARBA:ARBA00006676}.
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DR   EMBL; CP003493; AFV91086.1; -; Genomic_DNA.
DR   RefSeq; WP_015071978.1; NC_019395.1.
DR   AlphaFoldDB; K7RXA2; -.
DR   STRING; 1171373.PACID_33280; -.
DR   KEGG; pbo:PACID_33280; -.
DR   PATRIC; fig|1171373.8.peg.3273; -.
DR   eggNOG; COG1816; Bacteria.
DR   HOGENOM; CLU_039228_0_0_11; -.
DR   Proteomes; UP000000214; Chromosome.
DR   GO; GO:0046936; F:2'-deoxyadenosine deaminase activity; IEA:UniProtKB-EC.
DR   GO; GO:0004000; F:adenosine deaminase activity; IEA:UniProtKB-EC.
DR   Gene3D; 3.20.20.140; Metal-dependent hydrolases; 1.
DR   InterPro; IPR001365; A_deaminase_dom.
DR   InterPro; IPR006330; Ado/ade_deaminase.
DR   InterPro; IPR032466; Metal_Hydrolase.
DR   NCBIfam; TIGR01430; aden_deam; 1.
DR   PANTHER; PTHR11409; ADENOSINE DEAMINASE; 1.
DR   PANTHER; PTHR11409:SF43; ADENOSINE DEAMINASE; 1.
DR   Pfam; PF00962; A_deaminase; 1.
DR   SUPFAM; SSF51556; Metallo-dependent hydrolases; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000313|EMBL:AFV91086.1}.
FT   DOMAIN          12..350
FT                   /note="Adenosine deaminase"
FT                   /evidence="ECO:0000259|Pfam:PF00962"
SQ   SEQUENCE   355 AA;  37883 MW;  062F944567353576 CRC64;
     MPVSPDLVRL SPKVVLHDHL DGGLRPATVL ELSREQGVTA PGATAEEAAD WFFETADSGS
     LPKYLETFDV TVGLMQTPEA LRRVAREYVE DMASDHVVYA ETRWAPQQHT AGGLSMGEAV
     DAVQAGLDEG MAEVAELGRP VVIKQLLTAM RQLDPDPDFA ELVTHRLRRG VVGVDLAGPE
     AGFGPERFLD LFDDVADAGG HVTIHAGEGD GLESIRAALT CGAERLGHGV RLVEDITSYG
     AGVLQLGEVA AEVLQAAIAL EVCPSSNVQT GLCNDVRTHP VAVLWQAGLP VTISPDNRLM
     SRTSATREST LTADALGWEV EDLHHVAVTA ADAAFCDEKT REIVRERVDE GFAAL
//