ID A0A3R5VCW0_9CLOT Unreviewed; 244 AA.
AC A0A3R5VCW0;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 17.
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 {ECO:0000256|HAMAP-Rule:MF_01968};
GN ORFNames=C1I91_27295 {ECO:0000313|EMBL:QAA35420.1};
OS Clostridium manihotivorum.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=2320868 {ECO:0000313|EMBL:QAA35420.1, ECO:0000313|Proteomes:UP000286268};
RN [1] {ECO:0000313|EMBL:QAA35420.1, ECO:0000313|Proteomes:UP000286268}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CT4 {ECO:0000313|EMBL:QAA35420.1,
RC ECO:0000313|Proteomes:UP000286268};
RA Tachaapaikoon C., Sutheeworapong S., Jenjaroenpun P., Wongsurawat T.,
RA Nookeaw I., Cheawchanlertfa P., Kosugi A., Cheevadhanarak S.,
RA Ratanakhanokchai K.;
RT "Genome Sequencing and Assembly of Anaerobacter polyendosporus strain
RT CT4.";
RL Submitted (JAN-2018) 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}.
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DR EMBL; CP025746; QAA35420.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3R5VCW0; -.
DR KEGG; cmah:C1I91_27295; -.
DR OrthoDB; 9800582at2; -.
DR Proteomes; UP000286268; Chromosome.
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 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:UP000286268};
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..244
FT /note="Deacetylase sirtuin-type"
FT /evidence="ECO:0000259|PROSITE:PS50305"
FT ACT_SITE 123
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01968,
FT ECO:0000256|PROSITE-ProRule:PRU00236"
FT BINDING 24
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01968"
FT BINDING 28
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01968"
FT BINDING 35
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01968"
FT BINDING 35
FT /ligand="nicotinamide"
FT /ligand_id="ChEBI:CHEBI:17154"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01968"
FT BINDING 36
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 107
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01968"
FT BINDING 107
FT /ligand="nicotinamide"
FT /ligand_id="ChEBI:CHEBI:17154"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01968"
FT BINDING 108
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01968"
FT BINDING 108
FT /ligand="nicotinamide"
FT /ligand_id="ChEBI:CHEBI:17154"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01968"
FT BINDING 123
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01968"
FT BINDING 131
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 134
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 152
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 155
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 193
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01968"
FT BINDING 194
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01968"
FT BINDING 216
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01968"
FT BINDING 234
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01968"
SQ SEQUENCE 244 AA; 26649 MW; 4B7335B41C208A56 CRC64;
MLMSLDKLKE IIDNSDNIVF FGGAGMSTES GIPDFRSSTG LFNKKLNMTF TPEQLVSHSF
YIRYPKEFFE FYKDKLIYPE AKPNAGHLAL AKLEQMGKLK AIVTQNIDGL HQAAGSKNVF
ELHGSVLRNY CTKCHAFYDE KFILEAEEVP ICTKCGGSVK PDVVLYEEGL DEAIINGAVK
AIAAADTLII GGTSLVVYPA AGLINYFRGK NLVLINKSST SADSKANLVI HDSIGKVLSS
VVDI
//
