YMDB_CITK8
ID YMDB_CITK8 Reviewed; 177 AA.
AC A8AI35;
DT 31-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT 23-OCT-2007, sequence version 1.
DT 03-AUG-2022, entry version 72.
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=CKO_02022;
OS Citrobacter koseri (strain ATCC BAA-895 / CDC 4225-83 / SGSC4696).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Citrobacter.
OX NCBI_TaxID=290338;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-895 / CDC 4225-83 / SGSC4696;
RG The Citrobacter koseri Genome Sequencing Project;
RA McClelland M., Sanderson E.K., Porwollik S., Spieth J., Clifton W.S.,
RA Latreille P., Courtney L., Wang C., Pepin K., Bhonagiri V., Nash W.,
RA Johnson M., Thiruvilangam P., Wilson R.;
RL Submitted (AUG-2007) to the EMBL/GenBank/DDBJ databases.
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; CP000822; ABV13148.1; -; Genomic_DNA.
DR RefSeq; WP_012132884.1; NC_009792.1.
DR AlphaFoldDB; A8AI35; -.
DR SMR; A8AI35; -.
DR STRING; 290338.CKO_02022; -.
DR EnsemblBacteria; ABV13148; ABV13148; CKO_02022.
DR GeneID; 45135986; -.
DR KEGG; cko:CKO_02022; -.
DR HOGENOM; CLU_046550_5_1_6; -.
DR OMA; HYGKGLP; -.
DR OrthoDB; 1812319at2; -.
DR Proteomes; UP000008148; 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_0000409472"
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; 18917 MW; 727AC606B88225D8 CRC64;
MKSRIHVQHG DITQLTVDVI VNAANASLLG GGGVDGAIHR AAGPTLLEAC KKVRQQQGEC
PAGHAVITLA GNLPAKAVIH TVGPVWRGGD HNESQLLEDA YFNSLQLVLA NGYRSVAFPA
ISTGAYGYPR PAAAEIAVNT VADFLARHAL PEQVYFVCYD EETARLYERL LTQQGDE
