Q68FX9
PR
Gene name |
Sirt5 |
Protein name |
NAD-dependent protein deacylase sirtuin-5, mitochondrial |
Names |
Regulatory protein SIR2 homolog 5, SIR2-like protein 5 |
Species |
Rattus norvegicus (Rat) |
KEGG Pathway |
rno:306840 |
EC number |
|
Protein Class |
|
Descriptions
The autoinhibited protein was predicted that may have potential autoinhibitory elements via cis-regPred.
Autoinhibitory domains (AIDs)
Target domain |
|
Relief mechanism |
|
Assay |
cis-regPred |
Accessory elements
No accessory elements
Autoinhibited structure
Activated structure
1 structures for Q68FX9
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-Q68FX9-F1 | Predicted | AlphaFoldDB |
No variants for Q68FX9
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for Q68FX9 | |||||
No associated diseases with Q68FX9
4 regional properties for Q68FX9
Functions
6 GO annotations of cellular component
| Name | Definition |
|---|---|
| cytosol | The part of the cytoplasm that does not contain organelles but which does contain other particulate matter, such as protein complexes. |
| mitochondrial inner membrane | The inner, i.e. lumen-facing, lipid bilayer of the mitochondrial envelope. It is highly folded to form cristae. |
| mitochondrial intermembrane space | The region between the inner and outer lipid bilayers of the mitochondrial envelope. |
| mitochondrial matrix | The gel-like material, with considerable fine structure, that lies in the matrix space, or lumen, of a mitochondrion. It contains the enzymes of the tricarboxylic acid cycle and, in some organisms, the enzymes concerned with fatty acid oxidation. |
| mitochondrion | A semiautonomous, self replicating organelle that occurs in varying numbers, shapes, and sizes in the cytoplasm of virtually all eukaryotic cells. It is notably the site of tissue respiration. |
| nucleus | A membrane-bounded organelle of eukaryotic cells in which chromosomes are housed and replicated. In most cells, the nucleus contains all of the cell's chromosomes except the organellar chromosomes, and is the site of RNA synthesis and processing. In some species, or in specialized cell types, RNA metabolism or DNA replication may be absent. |
7 GO annotations of molecular function
| Name | Definition |
|---|---|
| NAD+ binding | Binding to the oxidized form, NAD, of nicotinamide adenine dinucleotide, a coenzyme involved in many redox and biosynthetic reactions. |
| NAD-dependent protein deacetylase activity | Catalysis of the removal of one or more acetyl groups from a protein, requiring NAD. |
| protein-glutaryllysine deglutarylase activity | Catalysis of the reaction: H2O + N(6)-glutaryl-L-lysyl- + NAD(+) = 2''-O-glutaryl-ADP-D-ribose + L-lysyl- |
| protein-malonyllysine demalonylase activity | Catalysis of the reaction: protein-malonyllysine + H2O => protein-lysine + malonate. This reaction is the removal of a malonyl group (CO-CH2-CO) from a malonylated lysine residue of a protein or peptide. |
| protein-succinyllysine desuccinylase activity | Catalysis of the reaction: H2O + N(6)-succinyl-L-lysyl- + NAD(+) = 2''-O-succinyl-ADP-D-ribose + L-lysyl- |
| transferase activity | Catalysis of the transfer of a group, e.g. a methyl group, glycosyl group, acyl group, phosphorus-containing, or other groups, from one compound (generally regarded as the donor) to another compound (generally regarded as the acceptor). Transferase is the systematic name for any enzyme of EC class 2. |
| zinc ion binding | Binding to a zinc ion (Zn). |
12 GO annotations of biological process
| Name | Definition |
|---|---|
| negative regulation of cardiac muscle cell apoptotic process | Any process that decreases the rate or extent of cardiac cell apoptotic process, a form of programmed cell death induced by external or internal signals that trigger the activity of proteolytic caspases whose actions dismantle a cardiac muscle cell and result in its death. |
| negative regulation of reactive oxygen species metabolic process | Any process that stops, prevents or reduces the frequency, rate or extent of reactive oxygen species metabolic process. |
| peptidyl-lysine demalonylation | The process of removing a malonyl group (CO-CH2-CO) from an malonylated lysine residue in a peptide or protein. |
| peptidyl-lysine desuccinylation | The removal of a succinyl group (CO-CH2-CH2-CO) from a succinylated lysine residue in a peptide or protein. |
| protein deacetylation | The removal of an acetyl group from a protein amino acid. An acetyl group is CH3CO-, derived from acetic |
| protein deglutarylation | The removal of a glutaryl group (CO-CH2-CH2-CH2-CO) from a residue in a peptide or protein. |
| protein demalonylation | The removal of a malonyl group (CO-CH2-CO), from an amino acid residue within a protein or peptide. |
| protein desuccinylation | The removal of a succinyl group (CO-CH2-CH2-CO) from a residue in a peptide or protein. |
| regulation of ketone biosynthetic process | Any process that modulates the frequency, rate or extent of the chemical reactions and pathways resulting in the formation of a ketone, carried out by individual cells. |
| regulation of succinate dehydrogenase activity | Any process that modulates the frequency, rate or extent of succinate dehydrogenase activity. |
| response to ischemia | Any process that results in a change in state or activity of an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a inadequate blood supply. |
| response to nutrient levels | Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a stimulus reflecting the presence, absence, or concentration of nutrients. |
3 homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| Q9VK34 | Sirt1 | NAD-dependent histone deacetylase sirtuin-1 | Drosophila melanogaster (Fruit fly) | PR |
| Q96EB6 | SIRT1 | NAD-dependent protein deacetylase sirtuin-1 | Homo sapiens (Human) | PR |
| Q923E4 | Sirt1 | NAD-dependent protein deacetylase sirtuin-1 | Mus musculus (Mouse) | PR |
| 10 | 20 | 30 | 40 | 50 | 60 |
| MRPLPVAPGR | LFSQLCCGPK | PSASPQSKIC | LTMARPSSNM | ADFRKCFANA | KHIVIISGAG |
| 70 | 80 | 90 | 100 | 110 | 120 |
| VSAESGVPTF | RGTGGYWRKW | QAQHLATPLA | FAHNPSQVWE | FYHYRREVMR | NKEPNPGHLA |
| 130 | 140 | 150 | 160 | 170 | 180 |
| IAQCEARLRD | QGRRVVVITQ | NIDELHRKAG | TKNLLEIHGT | LFKTRCTSCG | NVAENYKSPI |
| 190 | 200 | 210 | 220 | 230 | 240 |
| CPALLGKGAP | EPDTQESRIP | VHKLPRCEEA | GCGGLLRPHV | VWFGENLDPA | ILKEVDRELA |
| 250 | 260 | 270 | 280 | 290 | 300 |
| RCDLCLVVGT | SSVVYPAAMF | APQVASRGVP | VAEFNMETTP | ATNRFRFHFP | GPCGVTLPEA |
| LAPHETERIS |