P34255
Gene name |
B0303.3 |
Protein name |
Probable 3-ketoacyl-CoA thiolase |
Names |
|
Species |
Caenorhabditis elegans |
KEGG Pathway |
cel:CELE_B0303.3 |
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 P34255
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-P34255-F1 | Predicted | AlphaFoldDB |
No variants for P34255
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for P34255 | |||||
No associated diseases with P34255
5 regional properties for P34255
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| active_site | Thiolase, active site | 427 - 440 | IPR020610 |
| conserved_site | Thiolase, conserved site | 392 - 408 | IPR020613 |
| active_site | Thiolase, acyl-enzyme intermediate active site | 106 - 124 | IPR020615 |
| domain | Thiolase, N-terminal | 26 - 298 | IPR020616 |
| domain | Thiolase, C-terminal | 305 - 444 | IPR020617 |
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. |
1 GO annotations of molecular function
| Name | Definition |
|---|---|
| acetyl-CoA C-acyltransferase activity | Catalysis of the reaction: acyl-CoA + acetyl-CoA = CoA + 3-oxoacyl-CoA. |
1 GO annotations of biological process
| Name | Definition |
|---|---|
| fatty acid beta-oxidation | A fatty acid oxidation process that results in the complete oxidation of a long-chain fatty acid. Fatty acid beta-oxidation begins with the addition of coenzyme A to a fatty acid, and occurs by successive cycles of reactions during each of which the fatty acid is shortened by a two-carbon fragment removed as acetyl coenzyme A; the cycle continues until only two or three carbons remain (as acetyl-CoA or propionyl-CoA respectively). |
| 10 | 20 | 30 | 40 | 50 | 60 |
| MLRAVSTSFG | TARAASAVAK | KNMPNIVLVD | AVRTPFVVSG | TVFKDLMAVD | LQKEAIKALV |
| 70 | 80 | 90 | 100 | 110 | 120 |
| EKTKLPYEQL | DHIICGTVIQ | ECKTSNIARE | AALLAGVPDK | IPAHTVTLAC | ISSNVAMTTG |
| 130 | 140 | 150 | 160 | 170 | 180 |
| MGMLATGNAN | AIIAGGVELL | SDVPIRYNRN | ARKAMLGMNK | AKDVPSKLKI | GGQIVKNLLS |
| 190 | 200 | 210 | 220 | 230 | 240 |
| PELPAVAEFS | TGETMGHSGD | RLAAAFNVSR | REQDEFAIRS | HTLASEAAKN | GKFTDVVPVF |
| 250 | 260 | 270 | 280 | 290 | 300 |
| LDGKKPKTIK | EDNGIRVSTL | EKLSSLKPAF | VKPHGTVTAA | NASYLTDGAS | AALIMTEEYA |
| 310 | 320 | 330 | 340 | 350 | 360 |
| LANGYKPKAY | LRDYLYVAQD | PKDQLLLSPA | YVIPKLLDKA | GLTLKDVDVF | EIHEAFAGQV |
| 370 | 380 | 390 | 400 | 410 | 420 |
| LANLNAMDSD | YFCKEQMKRS | GKFGRVPMDK | LNLWGGSLSI | GHPFGATGVR | LATHSAHRLK |
| 430 | 440 | ||||
| EEKGQYAVIA | ACAAGGHGVG | MLIEAYGK |