Q8R9N6
Gene name |
cobB1 |
Protein name |
NAD-dependent protein deacylase 1 |
Names |
Regulatory protein SIR2 homolog 1 |
Species |
Caldanaerobacter subterraneus subsp. tengcongensis (strain DSM 15242 / JCM 11007 / NBRC 100824 / MB4) (Thermoanaerobacter tengcongensis) |
KEGG Pathway |
tte:TTE1570 |
EC number |
2.3.1.286: Transferring groups other than amino-acyl groups |
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 Q8R9N6
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-Q8R9N6-F1 | Predicted | AlphaFoldDB |
No variants for Q8R9N6
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for Q8R9N6 | |||||
No associated diseases with Q8R9N6
1 regional properties for Q8R9N6
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| domain | Sirtuin family, catalytic core domain | 1 - 242 | IPR026590 |
Functions
| Description | ||
|---|---|---|
| EC Number | 2.3.1.286 | Transferring groups other than amino-acyl groups |
| Subcellular Localization |
|
|
| PANTHER Family | ||
| PANTHER Subfamily | ||
| PANTHER Protein Class | ||
| PANTHER Pathway Category | No pathway information available | |
1 GO annotations of cellular component
| Name | Definition |
|---|---|
| cytoplasm | The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures. |
6 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-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). |
1 GO annotations of biological process
| Name | Definition |
|---|---|
| protein deacetylation | The removal of an acetyl group from a protein amino acid. An acetyl group is CH3CO-, derived from acetic |
No homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| No homologous proteins | ||||
| 10 | 20 | 30 | 40 | 50 | 60 |
| MDFKILKEKL | PQSNLTVVLT | GAGISKESGI | PTFRGEDGLW | KKYNPEELAT | PWAFQRNPAL |
| 70 | 80 | 90 | 100 | 110 | 120 |
| VWEWYDYRRR | IISKAKPNKC | HLLIAEFEER | FKNVRVITQN | VDGLHEAAGS | TNVIELHGNI |
| 130 | 140 | 150 | 160 | 170 | 180 |
| WKVKCTKCDF | RGINREVPLS | KIPPECPKCG | SIVRPDVVWF | GEPLPSDKLT | EAMELSQRAD |
| 190 | 200 | 210 | 220 | 230 | 240 |
| LFIVIGTSLM | VQPAASLPFL | ALERGAFVVE | VSPEETPLSR | KAHLFFQMGA | VEFAMKFEEK |
| EG |