A0AAD9RCL8 · A0AAD9RCL8_9HYME
- ProteinNAD-dependent protein deacylase
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids263 (go to sequence)
- Protein existenceInferred from homology
- Annotation score3/5
Function
function
NAD-dependent lysine demalonylase, desuccinylase and deglutarylase that specifically removes malonyl, succinyl and glutaryl groups on target proteins. Has weak NAD-dependent protein deacetylase activity; however this activity may not be physiologically relevant in vivo.
Catalytic activity
- H2O + N6-glutaryl-L-lysyl-[protein] + NAD+ = 2''-O-glutaryl-ADP-D-ribose + L-lysyl-[protein] + nicotinamide
- H2O + N6-malonyl-L-lysyl-[protein] + NAD+ = 2''-O-malonyl-ADP-D-ribose + L-lysyl-[protein] + nicotinamide
- H2O + N6-succinyl-L-lysyl-[protein] + NAD+ = 2''-O-succinyl-ADP-D-ribose + L-lysyl-[protein] + nicotinamide
Cofactor
Note: Binds 1 zinc ion per subunit.
Features
Showing features for binding site, active site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 62 | substrate | ||||
Sequence: Y | ||||||
Binding site | 65 | substrate | ||||
Sequence: R | ||||||
Binding site | 100-103 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: QNID | ||||||
Active site | 118 | Proton acceptor | ||||
Sequence: H | ||||||
Binding site | 126 | Zn2+ (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 129 | Zn2+ (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 167 | Zn2+ (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 172 | Zn2+ (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 209-211 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: GTS | ||||||
Binding site | 235-237 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: NIE | ||||||
Binding site | 253 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: C |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | mitochondrion | |
Cellular Component | nucleus | |
Molecular Function | NAD+ binding | |
Molecular Function | NAD-dependent histone deacetylase activity | |
Molecular Function | protein-malonyllysine demalonylase activity | |
Molecular Function | protein-succinyllysine desuccinylase activity | |
Molecular Function | transferase activity | |
Molecular Function | zinc ion binding |
Keywords
- Molecular function
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameNAD-dependent protein deacylase
- EC number
- Alternative names
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageEukaryota > Metazoa > Ecdysozoa > Arthropoda > Hexapoda > Insecta > Pterygota > Neoptera > Endopterygota > Hymenoptera > Apocrita > Aculeata > Vespoidea > Vespidae > Eumeninae > Odynerus
Accessions
- Primary accessionA0AAD9RCL8
Proteomes
Subcellular Location
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 1-263 | Deacetylase sirtuin-type | ||||
Sequence: MSCFDQLIEDKLTKRSYKVCNESESGVPTFRGAGGYWRKYQAQSLATPEAFSANPSLVWEFYEYRRTLVSKVKPNKAHEAIAAFQKRLANDGKKVTVVTQNIDGLHQKAGTENVLELHGSLYKTRCLKCHNVSINENIPICPALHGKGIPDPSITSSTIPIEELPRCANIDCKGLLRPDIVWFGENLNESVLNKAYEIVETCDICLVIGTSSIVYPAAMFAPKVANRGVPVAEFNIETTPATRDFQYHFQGPCTITVTEALEP |
Domain
In contrast to class I sirtuins, class III sirtuins have only weak deacetylase activity. Difference in substrate specificity is probably due to a larger hydrophobic pocket with 2 residues (Tyr-62 and Arg-65) that bind to malonylated and succinylated substrates and define the specificity.
Sequence similarities
Belongs to the sirtuin family. Class III subfamily.
Family and domain databases
Sequence
- Sequence statusComplete
- Length263
- Mass (Da)29,168
- Last updated2024-05-29 v1
- ChecksumA8F5030A408C8019
Computationally mapped potential isoform sequences
There are 2 potential isoforms mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
A0AAD9VKL0 | A0AAD9VKL0_9HYME | KPH14_003368 | 238 | ||
A0AAD9RDW0 | A0AAD9RDW0_9HYME | KPH14_003368 | 246 |
Keywords
- Technical term