P41903
Gene name |
TES1 (PTE1, YJR019C, J1456) |
Protein name |
Peroxisomal acyl-coenzyme A thioester hydrolase 1 |
Names |
Peroxisomal long-chain acyl-CoA thioesterase 1 |
Species |
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
KEGG Pathway |
sce:YJR019C |
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
2 structures for P41903
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| 1TBU | X-ray | 220 A | A/B/C/D | 1-118 | PDB |
| AF-P41903-F1 | Predicted | AlphaFoldDB |
2 variants for P41903
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| s10-468186 | 30 | L>P | No | SGRP | |
| s10-467722 | 185 | Q>K | No | SGRP |
No associated diseases with P41903
2 regional properties for P41903
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| domain | Acyl-CoA thioesterase II domain | 22 - 116 | IPR025652-1 |
| domain | Acyl-CoA thioesterase II domain | 201 - 336 | IPR025652-2 |
3 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. |
| peroxisomal matrix | The volume contained within the membranes of a peroxisome; in many cells the matrix contains a crystalloid core largely composed of urate oxidase. |
| 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. |
4 GO annotations of molecular function
| Name | Definition |
|---|---|
| acyl-CoA hydrolase activity | Catalysis of the reaction: acyl-CoA + H2O = CoA + a carboxylate. |
| carboxylic ester hydrolase activity | Catalysis of the hydrolysis of a carboxylic ester bond. |
| myristoyl-CoA hydrolase activity | Catalysis of the reaction: myristoyl-CoA + H2O <=> H+ + tetradecanoate + coenzyme A. |
| palmitoyl-CoA hydrolase activity | Catalysis of the reaction: palmitoyl-CoA + H2O = CoA + palmitate. |
4 GO annotations of biological process
| Name | Definition |
|---|---|
| acyl-CoA metabolic process | The chemical reactions and pathways involving acyl-CoA, any derivative of coenzyme A in which the sulfhydryl group is in thiolester linkage with an acyl group. |
| 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). |
| fatty acid catabolic process | The chemical reactions and pathways resulting in the breakdown of a fatty acid, any of the aliphatic monocarboxylic acids that can be liberated by hydrolysis from naturally occurring fats and oils. Fatty acids are predominantly straight-chain acids of 4 to 24 carbon atoms, which may be saturated or unsaturated; branched fatty acids and hydroxy fatty acids also occur, and very long chain acids of over 30 carbons are found in waxes. |
| fatty acid oxidation | The removal of one or more electrons from a fatty acid, with or without the concomitant removal of a proton or protons, by reaction with an electron-accepting substance, by addition of oxygen or by removal of hydrogen. |
No homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| No homologous proteins | ||||
| 10 | 20 | 30 | 40 | 50 | 60 |
| MSASKMAMSN | LEKILELVPL | SPTSFVTKYL | PAAPVGSKGT | FGGTLVSQSL | LASLHTVPLN |
| 70 | 80 | 90 | 100 | 110 | 120 |
| FFPTSLHSYF | IKGGDPRTKI | TYHVQNLRNG | RNFIHKQVSA | YQHDKLIFTS | MILFAVQRSK |
| 130 | 140 | 150 | 160 | 170 | 180 |
| EHDSLQHWET | IPGLQGKQPD | PHRYEEATSL | FQKEVLDPQK | LSRYASLSDR | FQDATSMSKY |
| 190 | 200 | 210 | 220 | 230 | 240 |
| VDAFQYGVME | YQFPKDMFYS | ARHTDELDYF | VKVRPPITTV | EHAGDESSLH | KHHPYRIPKS |
| 250 | 260 | 270 | 280 | 290 | 300 |
| ITPENDARYN | YVAFAYLSDS | YLLLTIPYFH | NLPLYCHSFS | VSLDHTIYFH | QLPHVNNWIY |
| 310 | 320 | 330 | 340 | ||
| LKISNPRSHW | DKHLVQGKYF | DTQSGRIMAS | VSQEGYVVYG | SERDIRAKF |