A0A1S9RD80 · A0A1S9RD80_PENBI
- ProteinNAD-dependent protein deacylase
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids322 (go to sequence)
- Protein existenceInferred from homology
- Annotation score4/5
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
- N6-glutaryl-L-lysyl-[protein] + NAD+ + H2O = 2''-O-glutaryl-ADP-D-ribose + nicotinamide + L-lysyl-[protein]
- N6-malonyl-L-lysyl-[protein] + NAD+ + H2O = 2''-O-malonyl-ADP-D-ribose + nicotinamide + L-lysyl-[protein]
- N6-succinyl-L-lysyl-[protein] + NAD+ + H2O = 2''-O-succinyl-ADP-D-ribose + nicotinamide + L-lysyl-[protein]
Cofactor
Note: Binds 1 zinc ion per subunit.
Features
Showing features for binding site, active site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 33-52 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: GAGISAASGLPTFRGAGGLW | ||||||
Binding site | 77 | substrate | ||||
Sequence: Y | ||||||
Binding site | 80 | substrate | ||||
Sequence: R | ||||||
Binding site | 111-114 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: QNVD | ||||||
Active site | 131 | Proton acceptor | ||||
Sequence: H | ||||||
Binding site | 139 | Zn2+ (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 144 | Zn2+ (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 218 | Zn2+ (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 221 | Zn2+ (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 260-262 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: GTS | ||||||
Binding site | 286-288 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: NME | ||||||
Binding site | 307 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: A |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | mitochondrion | |
Cellular Component | nucleus | |
Molecular Function | NAD+ binding | |
Molecular Function | NAD-dependent histone deacetylase activity | |
Molecular Function | protein-glutaryllysine deglutarylase activity | |
Molecular Function | protein-malonyllysine demalonylase activity | |
Molecular Function | protein-succinyllysine desuccinylase activity | |
Molecular Function | transferase activity | |
Molecular Function | zinc ion binding | |
Biological Process | protein deacetylation |
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 > Fungi > Dikarya > Ascomycota > Pezizomycotina > Eurotiomycetes > Eurotiomycetidae > Eurotiales > Aspergillaceae > Penicillium
Accessions
- Primary accessionA0A1S9RD80
Proteomes
Subcellular Location
Structure
Family & Domains
Features
Showing features for domain, region.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 8-322 | Deacetylase sirtuin-type | ||||
Sequence: VIAPSTDIQSFAEYLKGCRRILALLGAGISAASGLPTFRGAGGLWRQYDATSLATPEAFADHPGLVWQFYSYRRHMALQAQPNKAHYALAELARRNKDFITLSQNVDGLSQRAQHPSEQLNLLHGSLFDIKCTSFYCNYTRQNDFTDPIVPALDIPKQSSSPIPSETDRTGEEASKSLHDALQETIQANEVDISDASNPIPKLAPADLPRCPECKGLLRPGVIWFGEPLPTDTIKNVDDWIESAPVDLILVIGTSSSVYPAALYVDVARERGAKVVVVNMEKDMPNRGQGSCDWFFQGDASVIVPEILKSVIGDV | ||||||
Region | 162-183 | Disordered | ||||
Sequence: IPKQSSSPIPSETDRTGEEASK |
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-77 and Arg-80) that bind to malonylated and succinylated substrates and define the specificity.
Sequence similarities
Belongs to the sirtuin family. Class I subfamily.
Belongs to the sirtuin family. Class III subfamily.
Family and domain databases
Sequence
- Sequence statusComplete
- Length322
- Mass (Da)35,186
- Last updated2017-05-10 v1
- Checksum25D744DCEDFDC4D8