ID   A5CPM3_CLAM3            Unreviewed;       372 AA.
AC   A5CPM3;
DT   12-JUN-2007, integrated into UniProtKB/TrEMBL.
DT   12-JUN-2007, sequence version 1.
DT   02-SEP-2026, entry version 84.
DE   RecName: Full=adenosine deaminase {ECO:0000256|ARBA:ARBA00012784};
DE            EC=3.5.4.4 {ECO:0000256|ARBA:ARBA00012784};
GN   Name=addA {ECO:0000313|EMBL:CAN01022.1};
GN   OrderedLocusNames=CMM_0983 {ECO:0000313|EMBL:CAN01022.1};
OS   Clavibacter michiganensis subsp. michiganensis (strain NCPPB 382).
OC   Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
OC   Microbacteriaceae; Clavibacter.
OX   NCBI_TaxID=443906 {ECO:0000313|EMBL:CAN01022.1, ECO:0000313|Proteomes:UP000001564};
RN   [1] {ECO:0000313|EMBL:CAN01022.1, ECO:0000313|Proteomes:UP000001564}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NCPPB 382 {ECO:0000313|EMBL:CAN01022.1,
RC   ECO:0000313|Proteomes:UP000001564};
RX   PubMed=18192381; DOI=10.1128/JB.01595-07;
RA   Gartemann K.H., Abt B., Bekel T., Burger A., Engemann J., Flugel M.,
RA   Gaigalat L., Goesmann A., Grafen I., Kalinowski J., Kaup O., Kirchner O.,
RA   Krause L., Linke B., McHardy A., Meyer F., Pohle S., Ruckert C.,
RA   Schneiker S., Zellermann E.M., Puhler A., Eichenlaub R., Kaiser O.,
RA   Bartels D.;
RT   "The genome sequence of the tomato-pathogenic actinomycete Clavibacter
RT   michiganensis subsp. michiganensis NCPPB382 reveals a large island involved
RT   in pathogenicity.";
RL   J. Bacteriol. 190:2138-2149(2008).
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; AM711867; CAN01022.1; -; Genomic_DNA.
DR   RefSeq; WP_012037669.1; NC_009480.1.
DR   AlphaFoldDB; A5CPM3; -.
DR   KEGG; cmi:CMM_0983; -.
DR   eggNOG; COG1816; Bacteria.
DR   HOGENOM; CLU_039228_0_0_11; -.
DR   OrthoDB; 9779574at2; -.
DR   Proteomes; UP000001564; Chromosome.
DR   GO; GO:0005829; C:cytosol; IEA:TreeGrafter.
DR   GO; GO:0004000; F:adenosine deaminase activity; IEA:UniProtKB-ARBA.
DR   GO; GO:0006154; P:adenosine catabolic process; IEA:TreeGrafter.
DR   GO; GO:0043103; P:hypoxanthine salvage; IEA:TreeGrafter.
DR   GO; GO:0046103; P:inosine biosynthetic process; IEA:TreeGrafter.
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; NF006847; PRK09358.1-2; 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:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:CAN01022.1};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001564};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT   DOMAIN          20..366
FT                   /note="Adenosine deaminase"
FT                   /evidence="ECO:0000259|Pfam:PF00962"
SQ   SEQUENCE   372 AA;  40103 MW;  73E111AE7140662F CRC64;
     MTIAPEDSTL PGGGSFRDLP KVSLHDHLDG GLRPGTIVEI ADEIGLELPA AGAEALGEWF
     RTSADSGSLV EYLKTFDVTI AAMQTEEHLA RVAREFVEDL ADDGVVYGEI RWAPEQHLTR
     GLSLDQTVEA VQSGIEEAVR GVEEAGGSIR VGQLVSAMRH LDRGTEIAEL AVRHRDRGVV
     GFDIAGPEAG FPPSRMQGAF DLLAREWMPR TVHAGEADGL ESIRGALLDG RALRLGHGVR
     IAEDIEVDSE EGEDVFVTLG TLAQWIKDRG IPLELSPSSN LQTGAIAAWG DAMVDHPFDL
     LYQLGFAVTV NTDNRLMSGT SISRELALLT DAFAYDLDDH EVFQLNAAAA AFLPLEEREA
     LADIISDGFA RL
//