ID   YMDB_SALG2              Reviewed;         179 AA.
AC   B5RBF3;
DT   31-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT   04-NOV-2008, sequence version 1.
DT   03-AUG-2022, entry version 73.
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=SG1975;
OS   Salmonella gallinarum (strain 287/91 / NCTC 13346).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=550538;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=287/91 / NCTC 13346;
RX   PubMed=18583645; DOI=10.1101/gr.077404.108;
RA   Thomson N.R., Clayton D.J., Windhorst D., Vernikos G., Davidson S.,
RA   Churcher C., Quail M.A., Stevens M., Jones M.A., Watson M., Barron A.,
RA   Layton A., Pickard D., Kingsley R.A., Bignell A., Clark L., Harris B.,
RA   Ormond D., Abdellah Z., Brooks K., Cherevach I., Chillingworth T.,
RA   Woodward J., Norberczak H., Lord A., Arrowsmith C., Jagels K., Moule S.,
RA   Mungall K., Saunders M., Whitehead S., Chabalgoity J.A., Maskell D.,
RA   Humphreys T., Roberts M., Barrow P.A., Dougan G., Parkhill J.;
RT   "Comparative genome analysis of Salmonella enteritidis PT4 and Salmonella
RT   gallinarum 287/91 provides insights into evolutionary and host adaptation
RT   pathways.";
RL   Genome Res. 18:1624-1637(2008).
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; AM933173; CAR37825.1; -; Genomic_DNA.
DR   RefSeq; WP_000203945.1; NC_011274.1.
DR   AlphaFoldDB; B5RBF3; -.
DR   SMR; B5RBF3; -.
DR   EnsemblBacteria; CAR37825; CAR37825; SG1975.
DR   KEGG; seg:SG1975; -.
DR   HOGENOM; CLU_046550_5_1_6; -.
DR   OMA; HYGKGLP; -.
DR   Proteomes; UP000008321; 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_0000409484"
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;  19169 MW;  2A44768EEAFEBA0F CRC64;
     MTSRLQVIQG DITQLSVDAI VNAANASLMG GGGVDGAIHR AAGPALLDAC KLIRQQQGEC
     QTGHAVITPA GKLSAKAVIH TVGPVWRGGE HQEAELLEEA YRSCLLLAEA NHFRSIAFPA
     ISTGVYGYPR AQAAEVAVRT VSDFITRYAL PEQVYFVCYD EETARLYARL LTQQGDDPA