ID   YMDB_CROS8              Reviewed;         180 AA.
AC   A7MG20;
DT   31-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT   02-OCT-2007, sequence version 1.
DT   03-AUG-2022, entry version 67.
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=ESA_02300;
OS   Cronobacter sakazakii (strain ATCC BAA-894) (Enterobacter sakazakii).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Cronobacter.
OX   NCBI_TaxID=290339;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-894;
RX   PubMed=20221447; DOI=10.1371/journal.pone.0009556;
RA   Kucerova E., Clifton S.W., Xia X.Q., Long F., Porwollik S., Fulton L.,
RA   Fronick C., Minx P., Kyung K., Warren W., Fulton R., Feng D., Wollam A.,
RA   Shah N., Bhonagiri V., Nash W.E., Hallsworth-Pepin K., Wilson R.K.,
RA   McClelland M., Forsythe S.J.;
RT   "Genome sequence of Cronobacter sakazakii BAA-894 and comparative genomic
RT   hybridization analysis with other Cronobacter species.";
RL   PLoS ONE 5:E9556-E9556(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; CP000783; ABU77549.1; -; Genomic_DNA.
DR   RefSeq; WP_012125107.1; NC_009778.1.
DR   AlphaFoldDB; A7MG20; -.
DR   SMR; A7MG20; -.
DR   EnsemblBacteria; ABU77549; ABU77549; ESA_02300.
DR   KEGG; esa:ESA_02300; -.
DR   PATRIC; fig|290339.8.peg.2060; -.
DR   HOGENOM; CLU_046550_5_1_6; -.
DR   OMA; HYGKGLP; -.
DR   OrthoDB; 1812319at2; -.
DR   Proteomes; UP000000260; 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..180
FT                   /note="O-acetyl-ADP-ribose deacetylase"
FT                   /id="PRO_0000409476"
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   180 AA;  19155 MW;  B9C14779B362A22D CRC64;
     MSGRINVVQG DITLIDVDVI VNAANPSLMG GGGVDGAIHR AAGPALLAAC RQVRQQQGEC
     QPGHAVITEA GDLAAKAVVH TVGPVWRGGQ DNEPQLLADA YRNSLQLVAA NGYNSVAFPA
     ISTGIYGYPK AAAAQIAFET VSDYLTRHPQ PKQVYFVCYD EENFLLYQRL LGQYDEQPGA