ID A0A2X3EFG4_KLUCR Unreviewed; 185 AA.
AC A0A2X3EFG4;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=O-acetyl-ADP-ribose deacetylase {ECO:0000256|HAMAP-Rule:MF_01205};
DE EC=3.1.1.106 {ECO:0000256|HAMAP-Rule:MF_01205};
DE AltName: Full=Regulator of RNase III activity {ECO:0000256|HAMAP-Rule:MF_01205};
GN Name=ymdB {ECO:0000256|HAMAP-Rule:MF_01205,
GN ECO:0000313|EMBL:HAT1569553.1};
GN ORFNames=I8Y10_000875 {ECO:0000313|EMBL:HAT1569553.1}, NCTC12993_06213
GN {ECO:0000313|EMBL:VFS82494.1};
OS Kluyvera cryocrescens (Kluyvera citrophila).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Kluyvera.
OX NCBI_TaxID=580 {ECO:0000313|EMBL:HAT1569553.1};
RN [1] {ECO:0000313|EMBL:HAT1569553.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=88CZ1 {ECO:0000313|EMBL:HAT1569553.1};
RX PubMed=30286803;
RA Souvorov A., Agarwala R., Lipman D.J.;
RT "SKESA: strategic k-mer extension for scrupulous assemblies.";
RL Genome Biol. 19:153-153(2018).
RN [2] {ECO:0000313|EMBL:VFS82494.1, ECO:0000313|Proteomes:UP000401081}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCTC12993 {ECO:0000313|EMBL:VFS82494.1,
RC ECO:0000313|Proteomes:UP000401081};
RG Pathogen Informatics;
RL Submitted (MAR-2019) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:HAT1569553.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=88CZ1 {ECO:0000313|EMBL:HAT1569553.1};
RG NCBI Pathogen Detection Project;
RL Submitted (NOV-2020) 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:0000256|HAMAP-
CC 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:0000256|HAMAP-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:0000256|HAMAP-Rule:MF_01205};
CC -!- SUBUNIT: Homodimer. Interacts with RNase III. {ECO:0000256|HAMAP-
CC Rule:MF_01205}.
CC -!- SIMILARITY: Belongs to the YmdB family. {ECO:0000256|ARBA:ARBA00010580,
CC ECO:0000256|HAMAP-Rule:MF_01205}.
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DR EMBL; DACSDP010000003; HAT1569553.1; -; Genomic_DNA.
DR EMBL; CAADJD010000025; VFS82494.1; -; Genomic_DNA.
DR RefSeq; WP_061280086.1; NZ_VKGH01000003.1.
DR AlphaFoldDB; A0A2X3EFG4; -.
DR STRING; 580.GCA_001266615_03709; -.
DR OrthoDB; 6194521at2; -.
DR Proteomes; UP000401081; Unassembled WGS sequence.
DR Proteomes; UP000863970; Unassembled WGS sequence.
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:0042278; P:purine nucleoside metabolic process; IEA:UniProtKB-UniRule.
DR CDD; cd02908; Macro_OAADPr_deacetylase; 1.
DR Gene3D; 3.40.220.10; Leucine Aminopeptidase, subunit E, domain 1; 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 PANTHER; PTHR11106:SF27; ADP-RIBOSE GLYCOHYDROLASE MACROD2; 1.
DR PANTHER; PTHR11106; GANGLIOSIDE INDUCED DIFFERENTIATION ASSOCIATED PROTEIN 2-RELATED; 1.
DR Pfam; PF01661; Macro; 1.
DR SMART; SM00506; A1pp; 1.
DR SUPFAM; SSF52949; Macro domain-like; 1.
DR PROSITE; PS51154; MACRO; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|HAMAP-Rule:MF_01205, ECO:0000313|EMBL:HAT1569553.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000401081}.
FT DOMAIN 1..175
FT /note="Macro"
FT /evidence="ECO:0000259|PROSITE:PS51154"
FT ACT_SITE 35
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01205"
FT BINDING 11..12
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01205"
FT BINDING 25
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01205"
FT BINDING 33..35
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01205"
FT BINDING 122..126
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01205"
SQ SEQUENCE 185 AA; 19679 MW; 75FD00CE191A0653 CRC64;
MTERIQLLQG DITRLEVDVI VNAANPSLLG GGGVDGAIHR AAGPSLQEAC AVVRQQQGTC
PPGHAVITHA GELKAKAVIH TVGPVWQGGG EHEASLLEQA YRNSLQLALD NGYHTLAFPA
ISTGAYGYPH AAAAEIAVRT VAAFLTRRSL PEIVYFVCFD DETLRLYQQQ LGQTRIPSLA
NDANT
//
