ID   YMDB2_PANVC             Reviewed;         171 AA.
AC   E1PL40;
DT   31-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT   30-NOV-2010, sequence version 1.
DT   03-AUG-2022, entry version 52.
DE   RecName: Full=O-acetyl-ADP-ribose deacetylase 2 {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 2 {ECO:0000255|HAMAP-Rule:MF_01205};
GN   Name=ymdB2 {ECO:0000255|HAMAP-Rule:MF_01205};
GN   OrderedLocusNames=Pvag_pPag20013;
OS   Pantoea vagans (strain C9-1) (Pantoea agglomerans (strain C9-1)).
OG   Plasmid pPag2.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Erwiniaceae; Pantoea.
OX   NCBI_TaxID=712898;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C9-1;
RX   PubMed=20952567; DOI=10.1128/jb.01122-10;
RA   Smits T.H., Rezzonico F., Kamber T., Goesmann A., Ishimaru C.A.,
RA   Stockwell V.O., Frey J.E., Duffy B.;
RT   "The genome sequence of the biocontrol agent Pantoea vagans strain C9-1.";
RL   J. Bacteriol. 192:6486-6487(2010).
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; CP001894; ADO08003.1; -; Genomic_DNA.
DR   RefSeq; WP_013360008.1; NC_014563.1.
DR   AlphaFoldDB; E1PL40; -.
DR   SMR; E1PL40; -.
DR   EnsemblBacteria; ADO08003; ADO08003; Pvag_pPag20013.
DR   KEGG; pva:Pvag_pPag20013; -.
DR   HOGENOM; CLU_046550_5_1_6; -.
DR   OMA; AQRFSND; -.
DR   OrthoDB; 1812319at2; -.
DR   Proteomes; UP000006631; Plasmid pPag2.
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; Plasmid; Reference proteome.
FT   CHAIN           1..171
FT                   /note="O-acetyl-ADP-ribose deacetylase 2"
FT                   /id="PRO_0000409482"
FT   DOMAIN          1..171
FT                   /note="Macro"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01205"
FT   ACT_SITE        34
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01205"
FT   BINDING         10..11
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01205"
FT   BINDING         24
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01205"
FT   BINDING         32..34
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01205"
FT   BINDING         121..125
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01205"
SQ   SEQUENCE   171 AA;  18228 MW;  67474C9DCEFEF42B CRC64;
     MNKITVIQGD ITNIASEAII NVANSSLLGG GGVDGAIHRA GGPVILAECQ AIRSRQGGCK
     VGEAVITGAG TLPADYVIHT VGPRWSDGRH NEDTQLKSVY LSCFKLVGHH GIKTVSFPNI
     STGIYGFPKK RAAAIALDVI KHCIAENRTI EKVNLVCFDA ENYDLYLKLL N