YMDB_SALTY
ID YMDB_SALTY Reviewed; 179 AA.
AC P67341; Q8Z7M1; Q8ZQ29;
DT 11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2004, sequence version 1.
DT 03-AUG-2022, entry version 84.
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=STM1147;
OS Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=99287;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX PubMed=11677609; DOI=10.1038/35101614;
RA McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P.,
RA Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D.,
RA Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E.,
RA Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R.,
RA Wilson R.K.;
RT "Complete genome sequence of Salmonella enterica serovar Typhimurium LT2.";
RL Nature 413:852-856(2001).
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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AE006468; AAL20077.1; -; Genomic_DNA.
DR RefSeq; NP_460118.1; NC_003197.2.
DR RefSeq; WP_000203944.1; NC_003197.2.
DR AlphaFoldDB; P67341; -.
DR SMR; P67341; -.
DR STRING; 99287.STM1147; -.
DR PaxDb; P67341; -.
DR EnsemblBacteria; AAL20077; AAL20077; STM1147.
DR GeneID; 1252665; -.
DR KEGG; stm:STM1147; -.
DR PATRIC; fig|99287.12.peg.1214; -.
DR HOGENOM; CLU_046550_5_1_6; -.
DR OMA; HYGKGLP; -.
DR PhylomeDB; P67341; -.
DR BioCyc; SENT99287:STM1147-MON; -.
DR Proteomes; UP000001014; Chromosome.
DR GO; GO:0019213; F:deacetylase activity; IBA:GO_Central.
DR GO; GO:0061463; F:O-acetyl-ADP-ribose deacetylase activity; IBA:GO_Central.
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:0060702; P:negative regulation of endoribonuclease activity; IBA:GO_Central.
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..179
FT /note="O-acetyl-ADP-ribose deacetylase"
FT /id="PRO_0000089206"
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
