ID A0A1C4Y6T8_9ACTN Unreviewed; 281 AA.
AC A0A1C4Y6T8;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2016, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE RecName: Full=NAD-dependent protein deacetylase {ECO:0000256|HAMAP-Rule:MF_01967};
DE EC=2.3.1.286 {ECO:0000256|HAMAP-Rule:MF_01967};
DE AltName: Full=Regulatory protein SIR2 homolog {ECO:0000256|HAMAP-Rule:MF_01967};
GN Name=cobB {ECO:0000256|HAMAP-Rule:MF_01967};
GN ORFNames=GA0070612_4324 {ECO:0000313|EMBL:SCF16091.1};
OS Micromonospora chokoriensis.
OC Bacteria; Actinomycetota; Actinomycetes; Micromonosporales;
OC Micromonosporaceae; Micromonospora.
OX NCBI_TaxID=356851 {ECO:0000313|EMBL:SCF16091.1, ECO:0000313|Proteomes:UP000198224};
RN [1] {ECO:0000313|EMBL:SCF16091.1, ECO:0000313|Proteomes:UP000198224}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 45160 {ECO:0000313|EMBL:SCF16091.1,
RC ECO:0000313|Proteomes:UP000198224};
RA Kjaerup R.B., Dalgaard T.S., Juul-Madsen H.R.;
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_01967}.
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_01967};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_01967};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|HAMAP-Rule:MF_01967};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01967}.
CC -!- SIMILARITY: Belongs to the sirtuin family. Class II subfamily.
CC {ECO:0000256|HAMAP-Rule:MF_01967}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_01967,
CC ECO:0000256|PROSITE-ProRule:PRU00236}.
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DR EMBL; LT607409; SCF16091.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1C4Y6T8; -.
DR eggNOG; COG0846; Bacteria.
DR Proteomes; UP000198224; Chromosome i.
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_01967; Sirtuin_ClassII; 1.
DR InterPro; IPR029035; DHS-like_NAD/FAD-binding_dom.
DR InterPro; IPR003000; Sirtuin.
DR InterPro; IPR026591; Sirtuin_cat_small_dom_sf.
DR InterPro; IPR026587; Sirtuin_class_II.
DR InterPro; IPR026590; Ssirtuin_cat_dom.
DR PANTHER; PTHR11085; NAD-DEPENDENT PROTEIN DEACYLASE SIRTUIN-5, MITOCHONDRIAL-RELATED; 1.
DR PANTHER; PTHR11085:SF2; NAD-DEPENDENT PROTEIN LIPOAMIDASE SIRTUIN-4, MITOCHONDRIAL; 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|HAMAP-Rule:MF_01967};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW Rule:MF_01967};
KW NAD {ECO:0000256|ARBA:ARBA00023027, ECO:0000256|HAMAP-Rule:MF_01967};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_01967};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|HAMAP-Rule:MF_01967}.
FT DOMAIN 1..281
FT /note="Deacetylase sirtuin-type"
FT /evidence="ECO:0000259|PROSITE:PS50305"
FT ACT_SITE 117
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01967"
FT BINDING 99..102
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01967"
FT BINDING 125
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01967"
FT BINDING 128
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01967"
FT BINDING 176
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01967"
FT BINDING 179
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01967"
FT BINDING 217..219
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01967"
FT BINDING 243..245
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01967"
FT BINDING 261
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01967"
SQ SEQUENCE 281 AA; 29391 MW; 4DC127A0B6C23FFA CRC64;
MESLDALTSL VAGGGVVVLS GAGLSTESGI PDYRGPSGVA RRHTPMTYQV FTRDPVARRR
YWARSHLGWR LIAGAAPNDG HRAVAGLQRA GLVDAVITQN VDGLHGAAGS TSVIELHGRL
DEVICLDCGN LTSREELDRR LREANPDFTA RVAAVNPDGD VDLPEEQVAA FRTVDCGICG
TGMLKPDVVF FGETVPAQRV ARCFAAVQRA RSLLVLGSSL TVMSGRRFVI RAAKQGIPVA
IVNQGPTRGD GHASVCVDAP LGAVLPELAA RVSGSAAPVG V
//
