Q6AZA0
Gene name |
acat1 |
Protein name |
Acetyl-CoA acetyltransferase, mitochondrial |
Names |
Acetoacetyl-CoA thiolase |
Species |
Danio rerio (Zebrafish) (Brachydanio rerio) |
KEGG Pathway |
dre:445290 |
EC number |
2.3.1.9: 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 Q6AZA0
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-Q6AZA0-F1 | Predicted | AlphaFoldDB |
No variants for Q6AZA0
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for Q6AZA0 | |||||
No associated diseases with Q6AZA0
5 regional properties for Q6AZA0
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| active_site | Thiolase, active site | 401 - 414 | IPR020610 |
| conserved_site | Thiolase, conserved site | 368 - 384 | IPR020613 |
| active_site | Thiolase, acyl-enzyme intermediate active site | 115 - 133 | IPR020615 |
| domain | Thiolase, N-terminal | 35 - 291 | IPR020616 |
| domain | Thiolase, C-terminal | 300 - 419 | IPR020617 |
Functions
| Description | ||
|---|---|---|
| EC Number | 2.3.1.9 | 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 |
|---|---|
| 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. |
2 GO annotations of molecular function
| Name | Definition |
|---|---|
| acetyl-CoA C-acetyltransferase activity | Catalysis of the reaction: 2 acetyl-CoA = CoA + acetoacetyl-CoA. |
| metal ion binding | Binding to a metal ion. |
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). |
No homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| No homologous proteins | ||||
| 10 | 20 | 30 | 40 | 50 | 60 |
| MTSRALYSTR | SQLCRHLAHK | YLSRSYSTRP | SLNEVVIVSA | VRTPIGSFKG | SLSTLPATKL |
| 70 | 80 | 90 | 100 | 110 | 120 |
| GSIAIKGAID | KAGIPVEEVK | EVYMGNVLQA | GEGQAPTRQA | LLGAGLPLST | PATTINKVCA |
| 130 | 140 | 150 | 160 | 170 | 180 |
| SGMKSIMLAS | QSLMCGHQDV | MVAGGMESMS | QVPYIMAREA | PPYGGVKMED | LIVKDGLTDV |
| 190 | 200 | 210 | 220 | 230 | 240 |
| YNKFHMGNCA | ENTAKNSSIS | REEQDAFAIK | SYTLSKAAWE | SGILAKEVVP | VSIPQRGKPD |
| 250 | 260 | 270 | 280 | 290 | 300 |
| VVVKEDEEYR | KVDFSKVPKL | KAVFLKENGT | VTAANASTLN | DGAAALVLMT | ADAAQRLNVT |
| 310 | 320 | 330 | 340 | 350 | 360 |
| PLAKIVAFAD | AAVAPIDFPI | APAFAVPKVL | KAAGIKKEDI | AMWEINEAFS | VVVLANIKML |
| 370 | 380 | 390 | 400 | 410 | |
| DIDPDRVNIN | GGAVSLGHPI | GMSGARIVGH | MVHNLKSGQY | GLAGICNGGG | GASSIVIQKF |