HAMAP rule MF_01121
General rule information
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Accession | MF_01121 |
Dates | 28-OCT-2003 (Created)
3-SEP-2024 (Last updated, Version 39) |
Name | Sirtuin_ClassIII |
Scope(s) |
Bacteria Archaea |
Template(s) | O28597 (NPD1_ARCFU); Q9NXA8 (SIR5_HUMAN); [ Recover all ] |
Triggered by |
case c? <OC:Bacteria> or <OC:Archaea>
HAMAP; MF_01121 (Get profile general information and statistics) end case
|
Propagated annotation
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Identifier, protein and gene names
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Identifier | NPD |
Protein name | RecName: Full=NAD-dependent protein deacylase; EC=2.3.1.286; AltName: Full=Regulatory protein SIR2 homolog; |
Gene name | Name=cobB; |
Comments
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case <OC:Enterobacterales> and <FTGroup:3> | |
FUNCTION | NAD-dependent lysine deacetylase that specifically removes acetyl groups on target proteins. Also acts as a protein-lysine deacylase by mediating protein desuccinylation and de-2- hydroxyisobutyrylation. Modulates the activities of several proteins which are inactive in their acylated form. |
else case <OC:Bacteria> and <FTGroup:3> and not <OC:Enterobacterales> | |
FUNCTION | NAD-dependent lysine deacetylase and desuccinylase that specifically removes acetyl and succinyl groups on target proteins. Modulates the activities of several proteins which are inactive in their acylated form. |
else case <OC:Archaea> and <FTGroup:3> | |
FUNCTION | NAD-dependent lysine deacetylase and desuccinylase that specifically removes acetyl and succinyl groups on target proteins. Modulates the activities of several proteins which are inactive in their acylated 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 case <OC:Bacteria> and not <FTGroup:3> | |
FUNCTION | NAD-dependent protein deacetylase which modulates the activities of several proteins which are inactive in their acetylated form. |
else case <OC:Archaea> and not <FTGroup:3> | |
FUNCTION | NAD-dependent protein deacetylase which modulates the activities of several proteins 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. |
end case | |
CATALYTIC ACTIVITY | Reaction=N(6)-acetyl-L-lysyl-[protein] + NAD(+) + H2O = 2''-O-acetyl- ADP-D-ribose + nicotinamide + L-lysyl-[protein]; Xref=Rhea:RHEA:43636, Rhea:RHEA-COMP:9752, Rhea:RHEA-COMP:10731, ChEBI:CHEBI:15377, ChEBI:CHEBI:17154, ChEBI:CHEBI:29969, ChEBI:CHEBI:57540, ChEBI:CHEBI:61930, ChEBI:CHEBI:83767; EC=2.3.1.286; |
case <FTGroup:3> | |
CATALYTIC ACTIVITY | Reaction=N(6)-succinyl-L-lysyl-[protein] + NAD(+) + H2O = 2''-O- succinyl-ADP-D-ribose + nicotinamide + L-lysyl-[protein]; Xref=Rhea:RHEA:47668, Rhea:RHEA-COMP:9752, Rhea:RHEA-COMP:11877, ChEBI:CHEBI:15377, ChEBI:CHEBI:17154, ChEBI:CHEBI:29969, ChEBI:CHEBI:57540, ChEBI:CHEBI:87830, ChEBI:CHEBI:87832; |
end case | |
case <OC:Enterobacterales> and <FTGroup:3> | |
CATALYTIC ACTIVITY | Reaction=N(6)-(2-hydroxyisobutanoyl)-L-lysyl-[protein] + NAD(+) + H2O = 2''-O-(2-hydroxyisobutanoyl)-ADP-D-ribose + nicotinamide + L-lysyl- [protein]; Xref=Rhea:RHEA:24364, Rhea:RHEA-COMP:9752, Rhea:RHEA- COMP:15921, ChEBI:CHEBI:15377, ChEBI:CHEBI:17154, ChEBI:CHEBI:29969, ChEBI:CHEBI:57540, ChEBI:CHEBI:144968, ChEBI:CHEBI:144969; |
end case | |
case <FTGroup:1> | |
COFACTOR | Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Note=Binds 1 zinc ion per subunit.; |
end case | |
SUBCELLULAR LOCATION | Cytoplasm. |
case <FTGroup:3> | |
DOMAIN | 2 residues (#{Tyr-64} and #{Arg-67}) present in a large hydrophobic pocket are probably involved in substrate specificity. They are important for desuccinylation activity, but dispensable for deacetylation activity. |
end case | |
SIMILARITY | Belongs to the sirtuin family. Class III subfamily. |
Keywords
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Cytoplasm | |
NAD | |
case <FTGroup:1> | |
Metal-binding | |
Zinc | |
end case | |
case <OC:Archaea> | |
Transcription | |
Transcription regulation | |
Transferase | |
end case |
Gene Ontology
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GO:0005737; Cellular component:cytoplasm | |
GO:0034979; Molecular function:NAD-dependent protein lysine deacetylase activity | |
GO:0070403; Molecular function:NAD+ binding | |
GO:0006476; Biological process:protein deacetylation | |
case <FTGroup:3> | |
GO:0036055; Molecular function:protein-succinyllysine desuccinylase activity | |
GO:0036048; Biological process:protein desuccinylation | |
end case | |
case <FTGroup:1> | |
GO:0008270; Molecular function:zinc ion binding | |
end case |
Cross-references
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Features
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From: NPD1_ARCFU (O28597) | ||||||||||||
Key | From | To | Description | Tag | Condition | FTGroup | ||||||
BINDING | 20 | 39 | /ligand="NAD(+)" /ligand_id="ChEBI:CHEBI:57540" |
G-A-G-x-S-[AK]-x-S-G-[ILV]-x-T-x(7,8)-W | ||||||||
BINDING | 98 | 101 | /ligand="NAD(+)" /ligand_id="ChEBI:CHEBI:57540" |
Q-N-[IV]-[DE] | ||||||||
BINDING | 185 | 187 | /ligand="NAD(+)" /ligand_id="ChEBI:CHEBI:57540" |
G-[TS]-S | ||||||||
BINDING | 211 | 213 | /ligand="NAD(+)" /ligand_id="ChEBI:CHEBI:57540" |
N-x(2) | ||||||||
ACT_SITE | 116 | 116 | /note="Proton acceptor" | 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 | 2 | |||||||
BINDING | 145 | 145 | /ligand="Zn(2+)" /ligand_id="ChEBI:CHEBI:29105" |
C | 1 | |||||||
BINDING | 148 | 148 | /ligand="Zn(2+)" /ligand_id="ChEBI:CHEBI:29105" |
C | 2 | |||||||
BINDING | 64 | 64 | /ligand="substrate" | Y | 3 | |||||||
BINDING | 67 | 67 | /ligand="substrate" | R | 3 | |||||||
BINDING | 229 | 229 | /ligand="NAD(+)" /ligand_id="ChEBI:CHEBI:57540" |
Additional information
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Size range | 208-262 amino acids |
Related rules |
MF_01967 MF_01968 |
Fusion | Nter: None Cter: None |
Comments | The gene name sir2 is used in a few prokaryotes. The gene is subject to alternative promoter usage in Salty, giving rise to 2 proteins with different N-termini. The longer protein is used in the seed alignment. Other Enterobacteriaceae probably do that too, maybe other bacteria as well. |