P05335
Gene name |
POX4 |
Protein name |
Acyl-coenzyme A oxidase 4 |
Names |
AOX 4, Acyl-CoA oxidase 4 |
Species |
Candida maltosa (Yeast) |
KEGG Pathway |
|
EC number |
1.3.3.6: With oxygen as acceptor |
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 P05335
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-P05335-F1 | Predicted | AlphaFoldDB |
No variants for P05335
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for P05335 | |||||
No associated diseases with P05335
4 regional properties for P05335
Functions
| Description | ||
|---|---|---|
| EC Number | 1.3.3.6 | With oxygen as acceptor |
| Subcellular Localization |
|
|
| PANTHER Family | ||
| PANTHER Subfamily | ||
| PANTHER Protein Class | ||
| PANTHER Pathway Category | No pathway information available | |
1 GO annotations of cellular component
| Name | Definition |
|---|---|
| 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 |
|---|---|
| acyl-CoA oxidase activity | Catalysis of the reaction: acyl-CoA + O2 = trans-2,3-dehydroacyl-CoA + hydrogen peroxide. |
| FAD binding | Binding to the oxidized form, FAD, of flavin-adenine dinucleotide, the coenzyme or the prosthetic group of various flavoprotein oxidoreductase enzymes. |
1 GO annotations of biological process
| Name | Definition |
|---|---|
| fatty acid beta-oxidation using acyl-CoA oxidase | A fatty acid beta-oxidation pathway in which the initial step, which converts an acyl-CoA to a trans-2-enoyl-CoA, is catalyzed by acyl-CoA oxidase; the electrons removed by oxidation pass directly to oxygen and produce hydrogen peroxide, which is cleaved by peroxisomal catalases. Fatty acid beta-oxidation begins with the addition of coenzyme A to a fatty acid, and ends when 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 |
| MTFTKKNVSV | SQGPDPRTSI | QTERANSKFD | PVTMNYFLEG | SKERSELMKS | LAQQIERDPI |
| 70 | 80 | 90 | 100 | 110 | 120 |
| LFTDGSYYDL | TKDQQRELTV | LKINRLSRYR | EGDSVDTFNK | RLSIMGVVDP | QVATRIGVNL |
| 130 | 140 | 150 | 160 | 170 | 180 |
| GLFLSCISGN | GTAEQFKYWA | IDKGTHNIQG | LYGCFGMTEL | GHGSNVAGVE | TTATFDKETD |
| 190 | 200 | 210 | 220 | 230 | 240 |
| EFVINTPHIG | ATKWWIGGAA | HSATHCSVYA | RLVVDGKDYG | VKTFVVPLRD | SNHDLMPGVT |
| 250 | 260 | 270 | 280 | 290 | 300 |
| VGDIGAKMGR | DGIDNGWIQF | SNVRIPRFFM | LQKFCKVSAE | GEVVLPPLEQ | LSYSALLGGR |
| 310 | 320 | 330 | 340 | 350 | 360 |
| VMMVLDSYRM | LARVSTIALR | YAIGRRQFKG | DNVDQNDPNA | LETQLIDYPL | HQKRLFPYLA |
| 370 | 380 | 390 | 400 | 410 | 420 |
| AAYVVSTGAL | KVEHTIQSTL | ATLDAAVENN | DTTAIFKSID | DMKSLFIDSG | SLKATTTWLA |
| 430 | 440 | 450 | 460 | 470 | 480 |
| AEAIDQCRQA | CGGHGYSSYN | GFAKAFNDWV | VQCTWEGDNN | VLSLSVGKPI | IKQIIGIEDN |
| 490 | 500 | 510 | 520 | 530 | 540 |
| GKTVRGSTAF | LNQVKDFTGS | NASKVVLNNT | SDLNDINKVI | KSIEVAIIRL | AHEAAISVRK |
| 550 | 560 | 570 | 580 | 590 | 600 |
| ESLDFAGAEL | VQISKLKAHH | YLLTEFVKRV | GEFEHKELVP | FLNTIGRLYS | ATVVLDKFAG |
| 610 | 620 | 630 | 640 | 650 | 660 |
| VFLTFNVASP | QAITDLASTQ | IPKLCAEVRP | NVVAYTDSFQ | QSDMVINSAI | GKYDGDVYEN |
| 670 | 680 | 690 | 700 | ||
| YFDLVKQLNP | PKNTKAPYTA | ALEGMLNRPS | LEARERYEKS | DETAAILSK |