A1CJC4
Gene name |
ACLA_034510 |
Protein name |
Lipoyl synthase, mitochondrial |
Names |
Lipoate synthase, LS, Lip-syn, Lipoic acid synthase |
Species |
Aspergillus clavatus (strain ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 / NRRL 1 / QM 1276 / 107) |
KEGG Pathway |
act:ACLA_034510 |
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 A1CJC4
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-A1CJC4-F1 | Predicted | AlphaFoldDB |
No variants for A1CJC4
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for A1CJC4 | |||||
No associated diseases with A1CJC4
1 regional properties for A1CJC4
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| domain | Ubiquitin-conjugating enzyme E2 | 402 - 568 | IPR000608 |
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 |
|---|---|
| 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. |
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 |
| MAASTSHLRS | LCSSTRSLSR | SGVIVTPIAC | RGYATTDPSP | SATTPTPVRR | RTTFKDKLNA |
| 70 | 80 | 90 | 100 | 110 | 120 |
| GPSFSDFVSN | GNDNAPLDPS | EAYALKTALV | GPAGRKKEMT | RLPSWLKTPI | PDSKNYQRLK |
| 130 | 140 | 150 | 160 | 170 | 180 |
| KDLRGLNLHT | VCEEARCPNI | SDCWGGSDKS | SATATIMLMG | DTCTRGCRFC | SVKTSRAPPP |
| 190 | 200 | 210 | 220 | 230 | 240 |
| LDPHEPENTA | EAISRWGLGY | VVLTSVDRDD | LVDGGARHFA | ETVIKIKQKA | PSILVECLTG |
| 250 | 260 | 270 | 280 | 290 | 300 |
| DYAGDLDMVK | LVARSGLDVY | AHNVETVEAL | TPQVRDRRAN | FQQSLRVLDA | AKKAQPTLIT |
| 310 | 320 | 330 | 340 | 350 | 360 |
| KTSLMLGLGE | TDEQLWDALR | QLRAVNVDVV | TFGQYMRPTK | RHMAVHEYVT | PDRFELWRQR |
| 370 | 380 | 390 | 400 | 410 | |
| ALEMGFLYCA | SGPLVRSSYK | AGEAFIENVL | KKRRAASGGA | ETIGERPVAV | DEASR |