A0A7J7FBI7 · A0A7J7FBI7_DICBM

Function

function

NAD-dependent lysine demalonylase, desuccinylase and deglutarylase that specifically removes malonyl, succinyl and glutaryl groups on target proteins. Activates CPS1 and contributes to the regulation of blood ammonia levels during prolonged fasting: acts by mediating desuccinylation and deglutarylation of CPS1, thereby increasing CPS1 activity in response to elevated NAD levels during fasting. Activates SOD1 by mediating its desuccinylation, leading to reduced reactive oxygen species. Modulates ketogenesis through the desuccinylation and activation of HMGCS2. Has weak NAD-dependent protein deacetylase activity; however this activity may not be physiologically relevant in vivo. Can deacetylate cytochrome c (CYCS) and a number of other proteins in vitro such as Uox.

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 site40-59NAD+ (UniProtKB | ChEBI)
Binding site98substrate
Binding site101substrate
Binding site136-139NAD+ (UniProtKB | ChEBI)
Active site154Proton acceptor
Binding site162Zn2+ (UniProtKB | ChEBI)
Binding site165Zn2+ (UniProtKB | ChEBI)
Binding site177Zn2+ (UniProtKB | ChEBI)
Binding site190Zn2+ (UniProtKB | ChEBI)
Binding site227-229NAD+ (UniProtKB | ChEBI)
Binding site253-255NAD+ (UniProtKB | ChEBI)
Binding site270NAD+ (UniProtKB | ChEBI)

GO annotations

AspectTerm
Cellular Componentcytosol
Cellular Componentmitochondrion
Cellular Componentnucleus
Molecular FunctionNAD+ binding
Molecular FunctionNAD-dependent histone deacetylase 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 sirtuin-5, mitochondrial
  • EC number
  • Alternative names
    • Regulatory protein SIR2 homolog 5
    • SIR2-like protein 5

Gene names

    • Name
      SIRT5
    • ORF names
      HPG69_008743

Organism names

Accessions

  • Primary accession
    A0A7J7FBI7

Proteomes

Subcellular Location

Mitochondrion
Cytoplasm, cytosol
Nucleus
Note: Mainly mitochondrial. Also present extramitochondrially, with a fraction present in the cytosol and very small amounts also detected in the nucleus.

Keywords

Interaction

Subunit

Monomer. Homodimer. Interacts with CPS1.

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain15-273Deacetylase 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-98 and Arg-101) that bind to malonylated and succinylated substrates and define the specificity.

Sequence similarities

Belongs to the sirtuin family. Class III subfamily.

Keywords

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    273
  • Mass (Da)
    30,146
  • Last updated
    2021-04-07 v1
  • Checksum
    AD8E45E37C63BA1C
MWDVNAQVVRCIDEDFILSLDMADFRKCFAKAKHIVVISGAGVSAESGVPTFRGAGGYWRKWQAQARPGDVDVGIVILEDLATPQAFARNPSRVWEFYHYRREVMQSKEPNPGHLAIAECEARLHKQGRQVMVITQNIDELHRKAGTKNLLEIHGSLFKTRCTSCGVVAANYKSPICPALSGKGCEEAGCGGLLRPHVVWFGENLDLAILEQVDRELALCDLCLVVGTSSVVYPAAMFAPQVSARGVPVAEFNMETTPATNRFSCFYGKTKYY

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
JACDTQ010000823
EMBL· GenBank· DDBJ
KAF5925066.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

Disclaimer

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