YMDB_ESCF3
ID YMDB_ESCF3 Reviewed; 177 AA.
AC B7LT90;
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=EFER_1884;
OS Escherichia fergusonii (strain ATCC 35469 / DSM 13698 / CCUG 18766 / IAM
OS 14443 / JCM 21226 / LMG 7866 / NBRC 102419 / NCTC 12128 / CDC 0568-73).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=585054;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35469 / DSM 13698 / BCRC 15582 / CCUG 18766 / IAM 14443 / JCM
RC 21226 / LMG 7866 / NBRC 102419 / NCTC 12128 / CDC 0568-73;
RX PubMed=19165319; DOI=10.1371/journal.pgen.1000344;
RA Touchon M., Hoede C., Tenaillon O., Barbe V., Baeriswyl S., Bidet P.,
RA Bingen E., Bonacorsi S., Bouchier C., Bouvet O., Calteau A., Chiapello H.,
RA Clermont O., Cruveiller S., Danchin A., Diard M., Dossat C., Karoui M.E.,
RA Frapy E., Garry L., Ghigo J.M., Gilles A.M., Johnson J., Le Bouguenec C.,
RA Lescat M., Mangenot S., Martinez-Jehanne V., Matic I., Nassif X., Oztas S.,
RA Petit M.A., Pichon C., Rouy Z., Ruf C.S., Schneider D., Tourret J.,
RA Vacherie B., Vallenet D., Medigue C., Rocha E.P.C., Denamur E.;
RT "Organised genome dynamics in the Escherichia coli species results in
RT highly diverse adaptive paths.";
RL PLoS Genet. 5:E1000344-E1000344(2009).
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=CAQ89394.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; CU928158; CAQ89394.1; ALT_INIT; Genomic_DNA.
DR RefSeq; WP_000842232.1; NC_011740.1.
DR AlphaFoldDB; B7LT90; -.
DR SMR; B7LT90; -.
DR EnsemblBacteria; CAQ89394; CAQ89394; EFER_1884.
DR KEGG; efe:EFER_1884; -.
DR HOGENOM; CLU_046550_5_1_6; -.
DR OrthoDB; 1812319at2; -.
DR BioCyc; EFER585054:EFER_RS09455-MON; -.
DR Proteomes; UP000000745; 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..177
FT /note="O-acetyl-ADP-ribose deacetylase"
FT /id="PRO_0000409478"
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; 19133 MW; 882A2B0CF75417D3 CRC64;
MKSRIHVLQG DITQLAVDVI VNAANSSLMG GGGVDGAIHR AAGPELLEAC QKVRRQQGEC
PTGHAVITIA GNLPARAVIH TVGPVWRDGE HNEDQLLHDA YLNSLKLAQA NGYKSIAFPA
ISTGVYGFPR AAAAEIAVKT VSDFITRHAL PEQIYFVCYD EENSRLYNRL LTQQGDE
