P06598
Gene name |
POX4 (AOX) |
Protein name |
Acyl-coenzyme A oxidase 4 |
Names |
Acyl-CoA oxidase 4, PXP-4, Peroxisomal fatty acyl-CoA oxidase |
Species |
Candida tropicalis (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 P06598
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-P06598-F1 | Predicted | AlphaFoldDB |
No variants for P06598
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for P06598 | |||||
No associated diseases with P06598
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 | SQGPDPRSSI | QKERDSSKWN | PQQMNYFLEG | SVERSELMKA | LAQQMERDPI |
| 70 | 80 | 90 | 100 | 110 | 120 |
| LFTDGSYYDL | TKDQQRELTA | VKINRIARYR | EQESIDTFNK | RLSLIGIFDP | QVGTRIGVNL |
| 130 | 140 | 150 | 160 | 170 | 180 |
| GLFLSCIRGN | GTTSQLNYWA | NEKETADVKG | IYGCFGMTEL | AHGSNVAGLE | TTATFDKESD |
| 190 | 200 | 210 | 220 | 230 | 240 |
| EFVINTPHIG | ATKWWIGGAA | HSATHCSVYA | RLIVDGQDYG | VKTFVVPLRD | SNHDLMPGVT |
| 250 | 260 | 270 | 280 | 290 | 300 |
| VGDIGPKMGR | DGIDNGWIQF | SNVRIPRFFM | LQKFCKVSAE | GEVTLPPLEQ | LSYSALLGGR |
| 310 | 320 | 330 | 340 | 350 | 360 |
| VMMVLDSYRM | LARMSTIALR | YAIGRRQFKG | DNVDPNDPNA | LETQLIDYPL | HQKRLFPYFV |
| 370 | 380 | 390 | 400 | 410 | 420 |
| PPMSSPSVPS | RLNTPSRPPW | SNWTSPLKRT | TPRLIFKSID | DMKSLFVDSG | SLKSTATWLG |
| 430 | 440 | 450 | 460 | 470 | 480 |
| AEAIDQCRQA | CGGHGHSSYN | GFGKAYNDWV | VQCTWEGDNN | VLGMSVGKPI | VKQVISIEDA |
| 490 | 500 | 510 | 520 | 530 | 540 |
| GKTVRGSTAF | LNQLKEYTGS | NSSKVVLNTV | ADLDDIKTVI | KAIEVAIIRL | SQEAASIVKK |
| 550 | 560 | 570 | 580 | 590 | 600 |
| ESFDYVGAEL | VQLSKLKAHH | YLLTEYIRRI | DTFDQKELAP | YLITLGKLYA | ATIVLDRFAG |
| 610 | 620 | 630 | 640 | 650 | 660 |
| VFLTFNVAST | EAITALASVQ | IPKLCAEVRP | NVVAYTDSFQ | QSDMIVNSAI | GRYDGDIYEN |
| 670 | 680 | 690 | 700 | ||
| YFDLVKLQNP | PSKTKAPYSD | ALEAMLNRPT | LDERERFQKS | DETAAILSK |