HAMAP rule MF_01968
General rule information
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Accession | MF_01968 |
Dates | 2-APR-2012 (Created) 19-NOV-2022 (Last updated, Version 11) |
Name | Sirtuin_ClassU |
Scope | Bacteria
Archaea |
Template | Q9WYW0 (NPD_THEMA) |
case <OC:Bacteria> or <OC:Archaea>
Triggered by |
end case
Propagated annotation
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Identifier, protein and gene names
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Identifier |
|
Protein name |
|
Gene name |
|
Comments
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case <OC:Archaea>
Function | NAD-dependent protein deacetylase which modulates the activities of several enzymes which are inactive in their acetylated form. Deacetylates the N-terminal lysine residue of Alba, the major archaeal chromatin protein and that, in turn, increases Alba's DNA binding affinity, thereby repressing transcription. |
else
Function | NAD-dependent protein deacetylase which modulates the activities of several enzymes which are inactive in their acetylated form. |
end case
Catalytic activity | RHEA:43636: H2O + N(6)-acetyl-L-lysyl-[protein] + NAD(+) = 2''-O-acetyl-ADP-D-ribose + L-lysyl-[protein] + nicotinamide
EC 2.3.1.286 |
case <FTGroup:1>
Cofactor | Zn(2+) Note: Binds 1 zinc ion per subunit. |
end case
Subcellular location | Cytoplasm. |
Similarity | Belongs to the sirtuin family. Class U subfamily. |
Keywords
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case <FTGroup:1>
end case
case <OC:Archaea>
end case
Gene Ontology
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GO:0005737; Cellular component: cytoplasm.
GO:0034979; Molecular function: NAD-dependent protein deacetylase activity.
GO:0070403; Molecular function: NAD+ binding.
GO:0006476; Biological process: protein deacetylation.
GO:0034979; Molecular function: NAD-dependent protein deacetylase activity.
GO:0070403; Molecular function: NAD+ binding.
GO:0006476; Biological process: protein deacetylation.
case <FTGroup:1>
GO:0008270; Molecular function: zinc ion binding.
end case
Cross-references
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Features
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From: NPD_THEMA (Q9WYW0) | ||||||||||||
Key | From | To | Description | Tag | Condition | FTGroup | ||||||
ACT_SITE | 116 | 116 | Proton acceptor | H | ||||||||
BINDING | 22 | 22 | /ligand="NAD(+)" /ligand_id="ChEBI:CHEBI:57540 | A | ||||||||
BINDING | 26 | 26 | /ligand="NAD(+)" /ligand_id="ChEBI:CHEBI:57540 | T | ||||||||
BINDING | 33 | 33 | /ligand="NAD(+)" /ligand_id="ChEBI:CHEBI:57540 | [FY] | ||||||||
BINDING | 33 | 33 | /ligand="nicotinamide" /ligand_id="ChEBI:CHEBI:17154 | [FY] | ||||||||
BINDING | 34 | 34 | /ligand="NAD(+)" /ligand_id="ChEBI:CHEBI:57540 | R | ||||||||
BINDING | 98 | 98 | /ligand="NAD(+)" /ligand_id="ChEBI:CHEBI:57540 | Q | ||||||||
BINDING | 100 | 100 | /ligand="NAD(+)" /ligand_id="ChEBI:CHEBI:57540 | [IVT] | ||||||||
BINDING | 100 | 100 | /ligand="nicotinamide" /ligand_id="ChEBI:CHEBI:17154 | [IVT] | ||||||||
BINDING | 101 | 101 | /ligand="NAD(+)" /ligand_id="ChEBI:CHEBI:57540 | D | ||||||||
BINDING | 101 | 101 | /ligand="nicotinamide" /ligand_id="ChEBI:CHEBI:17154 | D | ||||||||
BINDING | 116 | 116 | /ligand="NAD(+)" /ligand_id="ChEBI:CHEBI:57540 | H | ||||||||
BINDING | 124 | 124 | /ligand="Zn(2+)" /ligand_id="ChEBI:CHEBI:29105 | C | 1 | |||||||
BINDING | 127 | 127 | /ligand="Zn(2+)" /ligand_id="ChEBI:CHEBI:29105 | C | 1 | |||||||
BINDING | 148 | 148 | /ligand="Zn(2+)" /ligand_id="ChEBI:CHEBI:29105 | C | 1 | |||||||
BINDING | 151 | 151 | /ligand="Zn(2+)" /ligand_id="ChEBI:CHEBI:29105 | C | 1 | |||||||
BINDING | 189 | 189 | /ligand="NAD(+)" /ligand_id="ChEBI:CHEBI:57540 | [ST] | ||||||||
BINDING | 190 | 190 | /ligand="NAD(+)" /ligand_id="ChEBI:CHEBI:57540 | S | ||||||||
BINDING | 214 | 214 | /ligand="NAD(+)" /ligand_id="ChEBI:CHEBI:57540 | N | ||||||||
BINDING (Optional) | 215 | 215 | /ligand="NAD(+)" /ligand_id="ChEBI:CHEBI:57540 | [LAV] | ||||||||
BINDING (Optional) | 216 | 216 | /ligand="NAD(+)" /ligand_id="ChEBI:CHEBI:57540 | G | ||||||||
BINDING (Optional) | 231 | 231 | /ligand="NAD(+)" /ligand_id="ChEBI:CHEBI:57540 | [DE] | ||||||||
BINDING (Optional) | 232 | 232 | /ligand="NAD(+)" /ligand_id="ChEBI:CHEBI:57540 | [VGIA] |
Additional information
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Size range | 229-260 amino acids |
Related rules | MF_01121 (NPD supersedes the current rule); MF_01967 (NPD) |
Fusion | None |