O65201
Gene name |
ACX2 |
Protein name |
Acyl-coenzyme A oxidase 2, peroxisomal |
Names |
AOX 2, Long-chain acyl-CoA oxidase, AtCX2 |
Species |
Arabidopsis thaliana (Mouse-ear cress) |
KEGG Pathway |
ath:AT5G65110 |
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 O65201
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-O65201-F1 | Predicted | AlphaFoldDB |
19 variants for O65201
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| ENSVATH07481297 | 2 | E>K | No | 1000Genomes | |
| ENSVATH03476760 | 9 | P>L | No | 1000Genomes | |
| ENSVATH07481296 | 18 | L>I | No | 1000Genomes | |
| tmp_5_26012421_G_A | 21 | A>V | No | 1000Genomes | |
| ENSVATH12935623 | 38 | S>L | No | 1000Genomes | |
| tmp_5_26012233_A_G | 84 | S>P | No | 1000Genomes | |
| ENSVATH07481294 | 108 | I>K | No | 1000Genomes | |
| tmp_5_26012126_A_T | 119 | F>L | No | 1000Genomes | |
| tmp_5_26012127_A_T | 119 | F>Y | No | 1000Genomes | |
| ENSVATH07481289 | 167 | R>I | No | 1000Genomes | |
| ENSVATH12935619 | 204 | D>H | No | 1000Genomes | |
| ENSVATH03476758 | 253 | M>L | No | 1000Genomes | |
| tmp_5_26011200_T_C | 352 | K>R | No | 1000Genomes | |
| ENSVATH00752232 | 403 | V>L | No | 1000Genomes | |
| ENSVATH07481285 | 437 | S>C | No | 1000Genomes | |
| ENSVATH12935616 | 494 | K>N | No | 1000Genomes | |
| ENSVATH00752230 | 592 | A>T | No | 1000Genomes | |
| ENSVATH07481274 | 658 | A>V | No | 1000Genomes | |
| tmp_5_26009895_C_T | 669 | D>N | No | 1000Genomes |
No associated diseases with O65201
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. |
4 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. |
| fatty acid binding | Binding to a fatty acid, an aliphatic monocarboxylic acids liberated from naturally occurring fats and oils by hydrolysis. |
| flavin adenine dinucleotide binding | Binding to FAD, flavin-adenine dinucleotide, the coenzyme or the prosthetic group of various flavoprotein oxidoreductase enzymes, in either the oxidized form, FAD, or the reduced form, FADH2. |
4 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). |
| 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). |
| lipid homeostasis | Any process involved in the maintenance of an internal steady state of lipid within an organism or cell. |
| long-chain fatty acid metabolic process | The chemical reactions and pathways involving long-chain fatty acids, A long-chain fatty acid is a fatty acid with a chain length between C13 and C22. |
1 homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| Q9EPL9 | Acox3 | Peroxisomal acyl-coenzyme A oxidase 3 | Mus musculus (Mouse) | PR |
| 10 | 20 | 30 | 40 | 50 | 60 |
| MESRREKNPM | TEEESDGLIA | ARRIQRLSLH | LSPSLTPSPS | LPLVQTETCS | ARSKKLDVNG |
| 70 | 80 | 90 | 100 | 110 | 120 |
| EALSLYMRGK | HIDIQEKIFD | FFNSRPDLQT | PIEISKDDHR | ELCMNQLIGL | VREAGVRPFR |
| 130 | 140 | 150 | 160 | 170 | 180 |
| YVADDPEKYF | AIMEAVGSVD | MSLGIKMGVQ | YSLWGGSVIN | LGTKKHRDKY | FDGIDNLDYT |
| 190 | 200 | 210 | 220 | 230 | 240 |
| GCFAMTELHH | GSNVQGLQTT | ATFDPLKDEF | VIDTPNDGAI | KWWIGNAAVH | GKFATVFARL |
| 250 | 260 | 270 | 280 | 290 | 300 |
| ILPTHDSKGV | SDMGVHAFIV | PIRDMKTHQT | LPGVEIQDCG | HKVGLNGVDN | GALRFRSVRI |
| 310 | 320 | 330 | 340 | 350 | 360 |
| PRDNLLNRFG | DVSRDGTYTS | SLPTINKRFG | ATLGELVGGR | VGLAYASVGV | LKISATIAIR |
| 370 | 380 | 390 | 400 | 410 | 420 |
| YSLLRQQFGP | PKQPEVSILD | YQSQQHKLMP | MLASTYAYHF | ATVYLVEKYS | EMKKTHDEQL |
| 430 | 440 | 450 | 460 | 470 | 480 |
| VADVHALSAG | LKSYVTSYTA | KALSVCREAC | GGHGYAAVNR | FGSLRNDHDI | FQTFEGDNTV |
| 490 | 500 | 510 | 520 | 530 | 540 |
| LLQQVAADLL | KRYKEKFQGG | TLTVTWSYLR | ESMNTYLSQP | NPVTARWEGE | DHLRDPKFQL |
| 550 | 560 | 570 | 580 | 590 | 600 |
| DAFRYRTSRL | LQNVAARLQK | HSKTLGGFGA | WNRCLNHLLT | LAESHIETVI | LAKFIEAVKN |
| 610 | 620 | 630 | 640 | 650 | 660 |
| CPDPSAKAAL | KLACDLYALD | RIWKDIGTYR | NVDYVAPNKA | KAIHKLTEYL | SFQVRNVAKE |
| 670 | 680 | 690 | |||
| LVDAFELPDH | VTRAPIAMQS | DAYSQYTQVV | GF |