ID A0A1E8EW90_9CLOT Unreviewed; 241 AA.
AC A0A1E8EW90;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=NAD-dependent protein deacetylase {ECO:0000256|HAMAP-Rule:MF_01968};
DE EC=2.3.1.286 {ECO:0000256|HAMAP-Rule:MF_01968};
DE AltName: Full=Regulatory protein SIR2 homolog {ECO:0000256|HAMAP-Rule:MF_01968};
GN Name=cobB_2 {ECO:0000313|EMBL:OFI01522.1};
GN Synonyms=cobB {ECO:0000256|HAMAP-Rule:MF_01968};
GN ORFNames=CLOACE_20760 {ECO:0000313|EMBL:OFI01522.1};
OS Clostridium acetireducens DSM 10703.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=1121290 {ECO:0000313|EMBL:OFI01522.1, ECO:0000313|Proteomes:UP000175744};
RN [1] {ECO:0000313|EMBL:OFI01522.1, ECO:0000313|Proteomes:UP000175744}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 10703 {ECO:0000313|EMBL:OFI01522.1,
RC ECO:0000313|Proteomes:UP000175744};
RA Poehlein A., Fluechter S., Duerre P., Daniel R.;
RT "Genome sequence of Clostridium acetireducens DSM 10703.";
RL Submitted (JUN-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: NAD-dependent protein deacetylase which modulates the
CC activities of several enzymes which are inactive in their acetylated
CC form. {ECO:0000256|HAMAP-Rule:MF_01968}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + N(6)-acetyl-L-lysyl-[protein] + NAD(+) = 2''-O-acetyl-
CC ADP-D-ribose + L-lysyl-[protein] + nicotinamide;
CC Xref=Rhea:RHEA:43636, Rhea:RHEA-COMP:9752, Rhea:RHEA-COMP:10731,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:17154, ChEBI:CHEBI:29969,
CC ChEBI:CHEBI:57540, ChEBI:CHEBI:61930, ChEBI:CHEBI:83767;
CC EC=2.3.1.286; Evidence={ECO:0000256|HAMAP-Rule:MF_01968};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_01968};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|HAMAP-Rule:MF_01968};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01968}.
CC -!- SIMILARITY: Belongs to the sirtuin family. Class U subfamily.
CC {ECO:0000256|HAMAP-Rule:MF_01968}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_01968}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OFI01522.1}.
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; LZFO01000041; OFI01522.1; -; Genomic_DNA.
DR RefSeq; WP_070111098.1; NZ_LZFO01000041.1.
DR AlphaFoldDB; A0A1E8EW90; -.
DR STRING; 1121290.CLAOCE_20760; -.
DR PATRIC; fig|1121290.3.peg.2086; -.
DR OrthoDB; 9800582at2; -.
DR Proteomes; UP000175744; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0070403; F:NAD+ binding; IEA:UniProtKB-UniRule.
DR GO; GO:0034979; F:NAD-dependent protein deacetylase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR Gene3D; 3.30.1600.10; SIR2/SIRT2 'Small Domain; 1.
DR Gene3D; 3.40.50.1220; TPP-binding domain; 1.
DR HAMAP; MF_01968; Sirtuin_ClassU; 1.
DR InterPro; IPR029035; DHS-like_NAD/FAD-binding_dom.
DR InterPro; IPR003000; Sirtuin.
DR InterPro; IPR026591; Sirtuin_cat_small_dom_sf.
DR InterPro; IPR028628; Sirtuin_class_U.
DR InterPro; IPR026590; Ssirtuin_cat_dom.
DR PANTHER; PTHR11085:SF12; NAD-DEPENDENT PROTEIN DEACYLASE SIRTUIN-5, MITOCHONDRIAL; 1.
DR PANTHER; PTHR11085; NAD-DEPENDENT PROTEIN DEACYLASE SIRTUIN-5, MITOCHONDRIAL-RELATED; 1.
DR Pfam; PF02146; SIR2; 1.
DR SUPFAM; SSF52467; DHS-like NAD/FAD-binding domain; 1.
DR PROSITE; PS50305; SIRTUIN; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_01968};
KW Hydrolase {ECO:0000313|EMBL:OFI01522.1};
KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_01968, ECO:0000256|PROSITE-
KW ProRule:PRU00236};
KW NAD {ECO:0000256|ARBA:ARBA00023027, ECO:0000256|HAMAP-Rule:MF_01968};
KW Reference proteome {ECO:0000313|Proteomes:UP000175744};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_01968};
KW Zinc {ECO:0000256|HAMAP-Rule:MF_01968, ECO:0000256|PROSITE-
KW ProRule:PRU00236}.
FT DOMAIN 1..241
FT /note="Deacetylase sirtuin-type"
FT /evidence="ECO:0000259|PROSITE:PS50305"
FT ACT_SITE 121
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01968,
FT ECO:0000256|PROSITE-ProRule:PRU00236"
FT BINDING 22
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01968"
FT BINDING 26
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01968"
FT BINDING 33
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01968"
FT BINDING 33
FT /ligand="nicotinamide"
FT /ligand_id="ChEBI:CHEBI:17154"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01968"
FT BINDING 34
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01968"
FT BINDING 103
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01968"
FT BINDING 105
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01968"
FT BINDING 105
FT /ligand="nicotinamide"
FT /ligand_id="ChEBI:CHEBI:17154"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01968"
FT BINDING 106
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01968"
FT BINDING 106
FT /ligand="nicotinamide"
FT /ligand_id="ChEBI:CHEBI:17154"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01968"
FT BINDING 121
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01968"
FT BINDING 129
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01968,
FT ECO:0000256|PROSITE-ProRule:PRU00236"
FT BINDING 132
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01968,
FT ECO:0000256|PROSITE-ProRule:PRU00236"
FT BINDING 151
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01968,
FT ECO:0000256|PROSITE-ProRule:PRU00236"
FT BINDING 154
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01968,
FT ECO:0000256|PROSITE-ProRule:PRU00236"
FT BINDING 192
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01968"
FT BINDING 193
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01968"
FT BINDING 215
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01968"
FT BINDING 233
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01968"
SQ SEQUENCE 241 AA; 26855 MW; B28884EE78062002 CRC64;
MVLQKLKEII KNSSNIVFFG GAGVSTESNI PDFRSSKGLY KTKNNYEYPP EVMLSHSFFV
THPEDFFEFY RKKMIYKNAK PNDAHYALAN LEKSGKVKAV ITQNIDGLHQ IAGSKNVLEL
HGSVHKNYCT SCGKKFNLNY VLNSKDIVPK CESCGGMVRP DVVLYEEGLD MDVINKSIEY
VKNADVLIVG GTSLVVYPAA NLINYYYGDK LILINKSPTP YDNRANLAIH DSIGAVLSTV
L
//