F8QBF1 · F8QBF1_SERL3

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.

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 site74substrate
Binding site77substrate
Binding site116-119NAD+ (UniProtKB | ChEBI)
Active site141Proton acceptor
Binding site149Zn2+ (UniProtKB | ChEBI)
Binding site152Zn2+ (UniProtKB | ChEBI)
Binding site188Zn2+ (UniProtKB | ChEBI)
Binding site191Zn2+ (UniProtKB | ChEBI)
Binding site226-228NAD+ (UniProtKB | ChEBI)
Binding site252-254NAD+ (UniProtKB | ChEBI)
Binding site270NAD+ (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
      SERLA73DRAFT_114804

Organism names

Accessions

  • Primary accession
    F8QBF1

Proteomes

Subcellular Location

Keywords

Interaction

Protein-protein interaction databases

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain1-285Deacetylase 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-74 and Arg-77) 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.

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    285
  • Mass (Da)
    31,018
  • Last updated
    2011-09-21 v1
  • Checksum
    E69D278CFE534CA9
MAPLNDTELFRSILRKSTNIVAIAGAGLSAASGLSTSGIPTFRDAGGLWRSHDAMSLATPRAFFKDPSRVWQFYHYRRETALKAAPNPGHLALALLSVPEHLKIIAPEAKFTLVTQNVDGLSARASKQVSPLREPELFEMHGRLFDTICTVCNDRKANFNSPICSALAGTEDNLKNDSNIPLEDLPRCSKCAGLLRPGIVWFEEVPHHLEEIKKIVDDADLALIVGTSSTVYPAAGYAHEIAEHGGTVAVFNIQRSDNDDLAHFLFIGPCATTLPHVLLKVDVTE

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
GL945488
EMBL· GenBank· DDBJ
EGN94537.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

Disclaimer

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