ID   YMDB_SALA4              Reviewed;         179 AA.
AC   B5F961;
DT   31-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT   14-OCT-2008, sequence version 1.
DT   03-AUG-2022, entry version 59.
DE   RecName: Full=O-acetyl-ADP-ribose deacetylase {ECO:0000255|HAMAP-Rule:MF_01205};
DE            EC=3.1.1.106 {ECO:0000255|HAMAP-Rule:MF_01205};
DE   AltName: Full=Regulator of RNase III activity {ECO:0000255|HAMAP-Rule:MF_01205};
GN   Name=ymdB {ECO:0000255|HAMAP-Rule:MF_01205}; OrderedLocusNames=SeAg_B2042;
OS   Salmonella agona (strain SL483).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=454166;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SL483;
RX   PubMed=21602358; DOI=10.1128/jb.00297-11;
RA   Fricke W.F., Mammel M.K., McDermott P.F., Tartera C., White D.G.,
RA   Leclerc J.E., Ravel J., Cebula T.A.;
RT   "Comparative genomics of 28 Salmonella enterica isolates: evidence for
RT   CRISPR-mediated adaptive sublineage evolution.";
RL   J. Bacteriol. 193:3556-3568(2011).
CC   -!- FUNCTION: Deacetylates O-acetyl-ADP ribose to yield ADP-ribose and free
CC       acetate. Down-regulates ribonuclease 3 (RNase III) activity. Acts by
CC       interacting directly with the region of the ribonuclease that is
CC       required for dimerization/activation. {ECO:0000255|HAMAP-
CC       Rule:MF_01205}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=3''-O-acetyl-ADP-D-ribose + H2O = acetate + ADP-D-ribose +
CC         H(+); Xref=Rhea:RHEA:59244, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:30089, ChEBI:CHEBI:57967, ChEBI:CHEBI:142723;
CC         EC=3.1.1.106; Evidence={ECO:0000255|HAMAP-Rule:MF_01205};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2''-O-acetyl-ADP-D-ribose + H2O = acetate + ADP-D-ribose +
CC         H(+); Xref=Rhea:RHEA:57060, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:30089, ChEBI:CHEBI:57967, ChEBI:CHEBI:83767;
CC         EC=3.1.1.106; Evidence={ECO:0000255|HAMAP-Rule:MF_01205};
CC   -!- SUBUNIT: Homodimer. Interacts with RNase III. {ECO:0000255|HAMAP-
CC       Rule:MF_01205}.
CC   -!- SIMILARITY: Belongs to the YmdB family. {ECO:0000255|HAMAP-
CC       Rule:MF_01205, ECO:0000305}.
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DR   EMBL; CP001138; ACH51509.1; -; Genomic_DNA.
DR   RefSeq; WP_000203946.1; NC_011149.1.
DR   AlphaFoldDB; B5F961; -.
DR   SMR; B5F961; -.
DR   EnsemblBacteria; ACH51509; ACH51509; SeAg_B2042.
DR   KEGG; sea:SeAg_B2042; -.
DR   HOGENOM; CLU_046550_5_1_6; -.
DR   OMA; HYGKGLP; -.
DR   Proteomes; UP000008819; Chromosome.
DR   GO; GO:0019213; F:deacetylase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0001883; F:purine nucleoside binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0008428; F:ribonuclease inhibitor activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0060701; P:negative regulation of ribonuclease activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0042278; P:purine nucleoside metabolic process; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.40.220.10; -; 1.
DR   HAMAP; MF_01205; YmdB; 1.
DR   InterPro; IPR002589; Macro_dom.
DR   InterPro; IPR043472; Macro_dom-like.
DR   InterPro; IPR024900; O-Ac-ADP-ribose_deAcase.
DR   Pfam; PF01661; Macro; 1.
DR   SMART; SM00506; A1pp; 1.
DR   SUPFAM; SSF52949; SSF52949; 1.
DR   PROSITE; PS51154; MACRO; 1.
PE   3: Inferred from homology;
KW   Hydrolase.
FT   CHAIN           1..179
FT                   /note="O-acetyl-ADP-ribose deacetylase"
FT                   /id="PRO_0000409483"
FT   DOMAIN          1..175
FT                   /note="Macro"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01205"
FT   ACT_SITE        35
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01205"
FT   BINDING         11..12
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01205"
FT   BINDING         25
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01205"
FT   BINDING         33..35
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01205"
FT   BINDING         122..126
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01205"
SQ   SEQUENCE   179 AA;  19164 MW;  12C5FB589B705215 CRC64;
     MTSRLQVIQG DITQLSVDAI VNAANASLMG GGGVDGAIHR AAGPALLDAC KLIRQQQGEC
     QTGHAVITPA GKLSAKAVIH TVGPVWRGGE YQEAELLEAA YRNCLLLAEA NHFRSIAFPA
     ISTGVYGYPR AQAAEVAVRT VSDFITRYAL PEQVYFVCYD EETARLYARL LTQQGDDPA