Q6L8K7
Gene name |
PAT1 (YALI0E11099g) |
Protein name |
Acetyl-CoA acetyltransferase |
Names |
Peroxisomal acetoacetyl-CoA thiolase, Thiolase |
Species |
Yarrowia lipolytica (strain CLIB 122 / E 150) (Yeast) (Candida lipolytica) |
KEGG Pathway |
yli:YALI0E11099g |
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 Q6L8K7
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-Q6L8K7-F1 | Predicted | AlphaFoldDB |
No variants for Q6L8K7
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for Q6L8K7 | |||||
No associated diseases with Q6L8K7
4 regional properties for Q6L8K7
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 | |
2 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. |
| peroxisome | A small organelle enclosed by a single membrane, and found in most eukaryotic cells. Contains peroxidases and other enzymes involved in a variety of metabolic processes including free radical detoxification, lipid catabolism and biosynthesis, and hydrogen peroxide metabolism. |
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 |
| MRLTLPRLNA | AYIVGAARTP | VGKFNGALKS | VSAIDLGITA | AKAAVQRSKV | PADQIDEFLF |
| 70 | 80 | 90 | 100 | 110 | 120 |
| GQVLTANSGQ | APARQVVIKG | GFPESVEATT | INKVCSSGLK | TVALAAQAIK | AGDRNVIVAG |
| 130 | 140 | 150 | 160 | 170 | 180 |
| GMESMSNTPY | YSGRGLVFGN | QKLEDSIVKD | GLWDPYNNIH | MGNCCENTNK | RDGITREQQD |
| 190 | 200 | 210 | 220 | 230 | 240 |
| EYAIESYRRA | NESIKNGAFK | DEIVPVEIKT | RKGTVTVSED | EEPKGANAEK | LKGLKPVFDK |
| 250 | 260 | 270 | 280 | 290 | 300 |
| QGSVTAGNAS | PINDGASAVV | VASGTKAKEL | GTPVLAKIVS | YADAATAPID | FTIAPSLAIP |
| 310 | 320 | 330 | 340 | 350 | 360 |
| AALKKAGLTK | DDIALWEINE | AFSGVALANL | MRLGIDKSKV | NVKGGAVALG | HPIGASGNRI |
| 370 | 380 | 390 | |||
| FVTLVNALKE | GEYGVAAICN | GGGASTAIVI | KKVSSVE |