ID   YMDB_CITRI              Reviewed;         177 AA.
AC   D2TT52;
DT   31-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT   31-MAY-2011, sequence version 2.
DT   03-AUG-2022, entry version 56.
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=ROD_11041;
OS   Citrobacter rodentium (strain ICC168) (Citrobacter freundii biotype 4280).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Citrobacter.
OX   NCBI_TaxID=637910;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ICC168;
RX   PubMed=19897651; DOI=10.1128/jb.01144-09;
RA   Petty N.K., Bulgin R., Crepin V.F., Cerdeno-Tarraga A.M., Schroeder G.N.,
RA   Quail M.A., Lennard N., Corton C., Barron A., Clark L., Toribio A.L.,
RA   Parkhill J., Dougan G., Frankel G., Thomson N.R.;
RT   "The Citrobacter rodentium genome sequence reveals convergent evolution
RT   with human pathogenic Escherichia coli.";
RL   J. Bacteriol. 192:525-538(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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CBG87876.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; FN543502; CBG87876.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; WP_024132603.1; NC_013716.1.
DR   AlphaFoldDB; D2TT52; -.
DR   SMR; D2TT52; -.
DR   STRING; 637910.ROD_11041; -.
DR   KEGG; cro:ROD_11041; -.
DR   eggNOG; COG2110; Bacteria.
DR   HOGENOM; CLU_046550_5_1_6; -.
DR   OrthoDB; 1812319at2; -.
DR   Proteomes; UP000001889; 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; Reference proteome.
FT   CHAIN           1..177
FT                   /note="O-acetyl-ADP-ribose deacetylase"
FT                   /id="PRO_0000409473"
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   177 AA;  18932 MW;  18D114EEC9773871 CRC64;
     MNSRIHVIHG DITTVAVDAI VNAANPSLMG GGGVDGAIHR AAGPELLEAC MTVRRQQGEC
     PPGHAVITAA GRLPAKAVIH TVGPIWRGGE HNEAQLLHDA YLNSLNLALA NGYQSIAFPA
     ISTGVYGYPR AAAAEIAVNT ISEFITRRAS PEQIYFVCYD EETTRLYQRL LTQQGDQ