YMDB_SALTI
ID YMDB_SALTI Reviewed; 179 AA.
AC P67342; Q8Z7M1; Q8ZQ29;
DT 11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2004, sequence version 1.
DT 03-AUG-2022, entry version 94.
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};
GN OrderedLocusNames=STY1184, t1773;
OS Salmonella typhi.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=90370;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CT18;
RX PubMed=11677608; DOI=10.1038/35101607;
RA Parkhill J., Dougan G., James K.D., Thomson N.R., Pickard D., Wain J.,
RA Churcher C.M., Mungall K.L., Bentley S.D., Holden M.T.G., Sebaihia M.,
RA Baker S., Basham D., Brooks K., Chillingworth T., Connerton P., Cronin A.,
RA Davis P., Davies R.M., Dowd L., White N., Farrar J., Feltwell T.,
RA Hamlin N., Haque A., Hien T.T., Holroyd S., Jagels K., Krogh A.,
RA Larsen T.S., Leather S., Moule S., O'Gaora P., Parry C., Quail M.A.,
RA Rutherford K.M., Simmonds M., Skelton J., Stevens K., Whitehead S.,
RA Barrell B.G.;
RT "Complete genome sequence of a multiple drug resistant Salmonella enterica
RT serovar Typhi CT18.";
RL Nature 413:848-852(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700931 / Ty2;
RX PubMed=12644504; DOI=10.1128/jb.185.7.2330-2337.2003;
RA Deng W., Liou S.-R., Plunkett G. III, Mayhew G.F., Rose D.J., Burland V.,
RA Kodoyianni V., Schwartz D.C., Blattner F.R.;
RT "Comparative genomics of Salmonella enterica serovar Typhi strains Ty2 and
RT CT18.";
RL J. Bacteriol. 185:2330-2337(2003).
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=AAO69396.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=CAD08271.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AL513382; CAD08271.1; ALT_INIT; Genomic_DNA.
DR EMBL; AE014613; AAO69396.1; ALT_INIT; Genomic_DNA.
DR PIR; AD0636; AD0636.
DR RefSeq; NP_455641.1; NC_003198.1.
DR RefSeq; WP_000203944.1; NZ_WSUR01000018.1.
DR AlphaFoldDB; P67342; -.
DR SMR; P67342; -.
DR STRING; 220341.16502318; -.
DR EnsemblBacteria; AAO69396; AAO69396; t1773.
DR KEGG; stt:t1773; -.
DR KEGG; sty:STY1184; -.
DR PATRIC; fig|220341.7.peg.1185; -.
DR eggNOG; COG2110; Bacteria.
DR HOGENOM; CLU_046550_5_1_6; -.
DR OMA; HYGKGLP; -.
DR Proteomes; UP000000541; Chromosome.
DR Proteomes; UP000002670; 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_0000089207"
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; 19196 MW; 05AE468EF0CD9315 CRC64;
MTSRLQVIQG DITQLSVDAI VNAANASLMG GGGVDGAIHR AAGPALLDAC KLIRQQQGEC
QTGHAVITPA GKLSAKAVIH TVGPVWRGGE HQEAELLEEA YRNCLLLAEA NHFRSIAFPA
ISTGVYGYPR AQAAEVAVRT VSDFITRYAL PEQVYFVCYD EETARLYARL LTQQGDDPA
