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HAMAP rule MF_01967
General rule information
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| Accession | MF_01967 |
| Dates | 2-APR-2012 (Created)
25-APR-2024 (Last updated, Version 12) |
| Name | Sirtuin_ClassII |
| Scope(s) |
Bacteria |
| Template(s) | Q9Y6E7 (SIR4_HUMAN); [ Recover all ] |
| Triggered by |
case c? <OC:Bacteria>
HAMAP; MF_01967 (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 deacetylase; EC=2.3.1.286; AltName: Full=Regulatory protein SIR2 homolog; |
| Gene name | Name=cobB; |
Comments
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| FUNCTION | NAD-dependent protein deacetylase which modulates the activities of several enzymes which are inactive in their acetylated form. |
| CATALYTIC ACTIVITY | Reaction=H2O + N(6)-acetyl-L-lysyl-[protein] + NAD(+) = 2''-O-acetyl- ADP-D-ribose + L-lysyl-[protein] + nicotinamide; 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:1> | |
| COFACTOR | Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Note=Binds 1 zinc ion per subunit.; |
| end case | |
| SUBCELLULAR LOCATION | Cytoplasm. |
| SIMILARITY | Belongs to the sirtuin family. Class II subfamily. |
Keywords
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| Cytoplasm | |
| NAD | |
| case <FTGroup:1> | |
| Metal-binding | |
| Zinc | |
| end case | |
| Transferase | |
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:1> | |
| GO:0008270; Molecular function:zinc ion binding | |
| end case | |
Cross-references
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Features
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| From: SIR4_HUMAN (Q9Y6E7) | ||||||||||||
| Key | From | To | Description | Tag | Condition | FTGroup | ||||||
| BINDING | 62 | 82 | /ligand="NAD(+)" /ligand_id="ChEBI:CHEBI:57540" |
G-A-G-x-S-T-x-x-G-[IV]-P-D-Y-R-x(7) | ||||||||
| BINDING | 143 | 146 | /ligand="NAD(+)" /ligand_id="ChEBI:CHEBI:57540" |
Q-N-V-D | ||||||||
| BINDING | 260 | 262 | /ligand="NAD(+)" /ligand_id="ChEBI:CHEBI:57540" |
G-[ST]-S | ||||||||
| BINDING | 286 | 288 | /ligand="NAD(+)" /ligand_id="ChEBI:CHEBI:57540" |
N-x-G | ||||||||
| ACT_SITE | 161 | 161 | /note="Proton acceptor" | H | ||||||||
| BINDING | 169 | 169 | /ligand="Zn(2+)" /ligand_id="ChEBI:CHEBI:29105" |
C | 1 | |||||||
| BINDING | 172 | 172 | /ligand="Zn(2+)" /ligand_id="ChEBI:CHEBI:29105" |
C | 1 | |||||||
| BINDING | 220 | 220 | /ligand="Zn(2+)" /ligand_id="ChEBI:CHEBI:29105" |
C | 1 | |||||||
| BINDING | 223 | 223 | /ligand="Zn(2+)" /ligand_id="ChEBI:CHEBI:29105" |
C | 1 | |||||||
| BINDING | 304 | 304 | /ligand="NAD(+)" /ligand_id="ChEBI:CHEBI:57540" |
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Additional information
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| Size range | 273-373 amino acids |
| Related rules |
MF_01121 MF_01968 |
| Fusion | Nter: None Cter: None |