B2GJ88
Gene name |
lipA |
Protein name |
Lipoyl synthase |
Names |
Lip-syn, LS, Lipoate synthase, Lipoic acid synthase, Sulfur insertion protein LipA |
Species |
Kocuria rhizophila (strain ATCC 9341 / DSM 348 / NBRC 103217 / DC2201) |
KEGG Pathway |
krh:KRH_14460 |
EC number |
2.8.1.8: Sulfurtransferases |
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 B2GJ88
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-B2GJ88-F1 | Predicted | AlphaFoldDB |
No variants for B2GJ88
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for B2GJ88 | |||||
No associated diseases with B2GJ88
Functions
| Description | ||
|---|---|---|
| EC Number | 2.8.1.8 | Sulfurtransferases |
| 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. |
3 GO annotations of molecular function
| Name | Definition |
|---|---|
| 4 iron, 4 sulfur cluster binding | Binding to a 4 iron, 4 sulfur (4Fe-4S) cluster; this cluster consists of four iron atoms, with the inorganic sulfur atoms found between the irons and acting as bridging ligands. |
| lipoate synthase activity | Catalysis of the reaction: protein N6-(octanoyl)lysine + 2 sulfur + 2 S-adenosyl-L-methionine = protein N6-(lipoyl)lysine + 2 L-methionine + 2 5'-deoxyadenosyl. |
| metal ion binding | Binding to a metal ion. |
1 GO annotations of biological process
| Name | Definition |
|---|---|
| protein lipoylation | The lipoylation of peptidyl-lysine to form peptidyl-N6-lipoyl-L-lysine. |
No homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| No homologous proteins | ||||
| 10 | 20 | 30 | 40 | 50 | 60 |
| MTIAPEGRKL | LRVEARNAEV | PIEKKPSWLK | NTAKMGPQFT | ELKSMARGRG | LHTVCEEAGC |
| 70 | 80 | 90 | 100 | 110 | 120 |
| PNIYECWEDR | EATFLIGGDT | CTRRCDFCDI | ATGKPGMVDV | AEPRKVAESV | RDLGLRYATV |
| 130 | 140 | 150 | 160 | 170 | 180 |
| TSVARDDLAD | GGAWLNAETI | RAIHAMNPST | GVEILIPDFK | GQPDAVQQVI | DAQPEVFAHN |
| 190 | 200 | 210 | 220 | 230 | 240 |
| LETVPRIFKQ | IRPAFAYERS | LDVLTQGKEH | GMIVKSNLIL | GMGETDDEVY | EALCDLHDAG |
| 250 | 260 | 270 | 280 | 290 | 300 |
| CDIITLTQYL | RPGPTFHPID | RWVKPETFVE | LSKAAEEIGF | LGVMAGPMVR | SSYRAGKLWA |
| 310 | 320 | 330 | |||
| RAMKKMGREI | PEHLSHIDDS | GSATQEASSL | LARLG |