A0AAJ1TSS4 · A0AAJ1TSS4_9HYPH
- ProteinNAD-dependent protein deacylase
- GenecobB
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids236 (go to sequence)
- Protein existenceInferred from homology
- Annotation score2/5
Function
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.
Catalytic activity
- H2O + N6-acetyl-L-lysyl-[protein] + NAD+ = 2''-O-acetyl-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 | 12-31 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: GAGVSAESGLGTFRDRGGIW | ||||||
Binding site | 56 | substrate | ||||
Sequence: Y | ||||||
Binding site | 59 | substrate | ||||
Sequence: R | ||||||
Binding site | 94-97 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: QNVD | ||||||
Active site | 112 | Proton acceptor | ||||
Sequence: H | ||||||
Binding site | 120 | Zn2+ (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 123 | Zn2+ (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 139 | Zn2+ (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 142 | Zn2+ (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 179-181 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: GTS | ||||||
Binding site | 205-207 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: NLE | ||||||
Binding site | 223 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: A |
GO annotations
Aspect | Term | |
---|---|---|
Molecular Function | hydrolase activity |
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 lineageBacteria > Pseudomonadota > Alphaproteobacteria > Hyphomicrobiales > Methylobacteriaceae > Methylobacterium
Accessions
- Primary accessionA0AAJ1TSS4
Proteomes
Subcellular Location
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 1-236 | Deacetylase sirtuin-type | ||||
Sequence: MGDPNNIFVLTGAGVSAESGLGTFRDRGGIWARFDPMKLATPEAYAADPDTVLDFYDHRRRGVIAAEPNAAHVALARAEARLAARGGRLFLCTQNVDDLHERAGSRAVVHMHGELLKARCTACGTVTPWRDDLDRASICPACGGVGRMRPDVVWFGEMPMHLDAIEDALAAADLFVAVGTSGAVYPAAGYVREARARNIPTCEINLEPSDNADAFDDARYGPASMALPRFLADLGL |
Domain
2 residues (Tyr-56 and Arg-59) present in a large hydrophobic pocket are probably involved in substrate specificity. They are important for desuccinylation activity, but dispensable for deacetylation activity.
Sequence similarities
Belongs to the sirtuin family. Class III subfamily.
Family and domain databases
Sequence
- Sequence statusComplete
- Length236
- Mass (Da)25,254
- Last updated2024-07-24 v1
- Checksum35C5E7ECB681C86E