A0A0L0NQP0 · A0A0L0NQP0_CANAR

  • Protein
    NAD-dependent protein deacylase
  • Status
    UniProtKB unreviewed (TrEMBL)
  • Amino acids
  • Protein existence
    Inferred from homology
  • Annotation score
    4/5

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.

Caution

Lacks conserved residue(s) required for the propagation of feature annotation.
The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data.

Catalytic activity

Cofactor

Zn2+ (UniProtKB | Rhea| CHEBI:29105 )

Note: Binds 1 zinc ion per subunit.

Features

Showing features for binding site, active site.

Type
IDPosition(s)Description
Binding site67substrate
Binding site70substrate
Binding site102-105NAD+ (UniProtKB | ChEBI)
Active site122Proton acceptor
Binding site130Zn2+ (UniProtKB | ChEBI)
Binding site135Zn2+ (UniProtKB | ChEBI)
Binding site187Zn2+ (UniProtKB | ChEBI)
Binding site190Zn2+ (UniProtKB | ChEBI)
Binding site229-231NAD+ (UniProtKB | ChEBI)
Binding site277NAD+ (UniProtKB | ChEBI)

GO annotations

AspectTerm
Cellular Componentmitochondrion
Cellular Componentnucleus
Molecular FunctionNAD+ binding
Molecular FunctionNAD-dependent histone deacetylase activity
Molecular Functionprotein-glutaryllysine deglutarylase activity
Molecular Functionprotein-malonyllysine demalonylase activity
Molecular Functionprotein-succinyllysine desuccinylase activity
Molecular Functiontransferase activity
Molecular Functionzinc ion binding
Biological Processprotein deacetylation

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    NAD-dependent protein deacylase
  • EC number
  • Alternative names
    • Regulatory protein SIR2 homolog 5

Gene names

    • ORF names
      QG37_07269

Organism names

  • Taxonomic identifier
  • Organism
  • Strain
    • 6684
  • Taxonomic lineage
    Eukaryota > Fungi > Dikarya > Ascomycota > Saccharomycotina > Saccharomycetes > Saccharomycetales > Metschnikowiaceae > Metschnikowiaceae incertae sedis > Candida/Metschnikowiaceae

Accessions

  • Primary accession
    A0A0L0NQP0

Proteomes

Organism-specific databases

Subcellular Location

Keywords

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain1-293Deacetylase sirtuin-type

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-67 and Arg-70) 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 status
    Complete
  • Length
    293
  • Mass (Da)
    32,406
  • Last updated
    2015-11-11 v1
  • MD5 Checksum
    A7D5D1C4E1557C98CB28DEC9B37648E1
MLKQASEFKEYLRNLKRIVALVGAGLSASSGLPVFRGSQGLWKNFNMIDLATPDAFYIDPGLVWQFYAWRRHMALAAQPNAGHRALAALSQDPSKEFLTITQNVDGLLTRAGHNKRHLYEIHGSLFELRCTSFTCTHREENYDDPLTETLRCDDEYERNTNDESIDTDTLPQFSPIKELAVKDLPPCPVCGSLMRPGVVWFGESLPLRALDGIDTFLESGPVDLILVIGTSGTVYPANGYVERVRQLGGKVAIFNTDIEEDVVAGRVADTWGFQGDAAKLLPELIGTQSSSQV

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
LGST01000056
EMBL· GenBank· DDBJ
KND96383.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

Disclaimer

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