Q9EPL9
PR
Gene name |
Acox3 |
Protein name |
Peroxisomal acyl-coenzyme A oxidase 3 |
Names |
Branched-chain acyl-CoA oxidase, BRCACox, Pristanoyl-CoA oxidase |
Species |
Mus musculus (Mouse) |
KEGG Pathway |
mmu:80911 |
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 Q9EPL9
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-Q9EPL9-F1 | Predicted | AlphaFoldDB |
43 variants for Q9EPL9
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| rs3388757726 | 8 | K>* | No | EVA | |
| rs32626929 | 8 | K>R | No | EVA | |
| rs240348140 | 16 | T>I | No | EVA | |
| rs3395410894 | 18 | K>N | No | EVA | |
| rs3395410916 | 20 | P>S | No | EVA | |
| rs3388751265 | 42 | Q>H | No | EVA | |
| rs3388750758 | 42 | Q>P | No | EVA | |
| rs32631633 | 75 | R>* | No | EVA | |
| rs3388745533 | 76 | E>G | No | EVA | |
| rs3388758622 | 80 | L>V | No | EVA | |
| rs3388745542 | 88 | Y>* | No | EVA | |
| rs264092105 | 131 | T>S | No | EVA | |
| rs235128386 | 134 | V>I | No | EVA | |
| rs3388757729 | 153 | F>I | No | EVA | |
| rs3388762148 | 157 | A>T | No | EVA | |
| rs3388753380 | 158 | L>R | No | EVA | |
| rs3388756623 | 211 | A>T | No | EVA | |
| rs3388750759 | 238 | P>S | No | EVA | |
| rs3388742143 | 248 | G>R | No | EVA | |
| rs3388728070 | 262 | M>R | No | EVA | |
| rs3388751322 | 285 | T>S | No | EVA | |
| rs3388750743 | 311 | I>F | No | EVA | |
| rs3388753786 | 313 | S>C | No | EVA | |
| rs3388753771 | 339 | T>A | No | EVA | |
| rs256866936 | 356 | I>L | No | EVA | |
| rs232576520 | 391 | D>N | No | EVA | |
| rs3388756661 | 463 | N>I | No | EVA | |
| rs3395331494 | 465 | L>Q | No | EVA | |
| rs3395440354 | 474 | Q>R | No | EVA | |
| rs3388756012 | 475 | D>E | No | EVA | |
| rs3388762090 | 555 | C>S | No | EVA | |
| rs3388750708 | 556 | R>W | No | EVA | |
| rs217941240 | 579 | G>D | No | EVA | |
| rs32628045 | 579 | G>S | No | EVA | |
| rs3388742139 | 598 | W>R | No | EVA | |
| rs3388753822 | 605 | A>G | No | EVA | |
| rs3388757192 | 613 | I>N | No | EVA | |
| rs3388753919 | 634 | K>E | No | EVA | |
| rs3395528454 | 645 | A>T | No | EVA | |
| rs3388757152 | 648 | D>Y | No | EVA | |
| rs3388762140 | 654 | P>Q | No | EVA | |
| rs3388750694 | 691 | S>T | No | EVA | |
| rs3388728052 | 701 | L>Y | No | EVA |
No associated diseases with Q9EPL9
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 | |
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. |
5 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. |
| pristanoyl-CoA oxidase activity | Catalysis of the reaction: pristanoyl-CoA + O2 = trans-2,3-dehydropristanoyl-CoA + hydrogen peroxide. |
3 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. |
1 homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| O65201 | ACX2 | Acyl-coenzyme A oxidase 2, peroxisomal | Arabidopsis thaliana (Mouse-ear cress) | PR |
| 10 | 20 | 30 | 40 | 50 | 60 |
| MGSLPEEKDS | ALWSDTPKGP | LSAYRARASF | NSGELLLFWD | GQDVIHFKKT | IFSTLENDPL |
| 70 | 80 | 90 | 100 | 110 | 120 |
| FARSYGADLP | LEKLRELNFL | RCKRVFEYGF | FKVEELLKNP | LKILVLINCL | GMYDWSLANK |
| 130 | 140 | 150 | 160 | 170 | 180 |
| CVLHMLVFGT | TVFVSGSEKH | FKYLEKIYSL | EIFGCFALTE | LSHGSNTKAM | RTTAHYDPDT |
| 190 | 200 | 210 | 220 | 230 | 240 |
| QEFILHSPDF | EAAKFWVGNL | GKTATHAVVF | AQLYMPDGQC | HGLHSFLVQI | RDTKTLLPMT |
| 250 | 260 | 270 | 280 | 290 | 300 |
| GVMVGDIGKK | LGQNGLDNGF | AMFNKVRIPR | QNLLDRTGNI | TSEGTYNSPF | KDVRQRLGAS |
| 310 | 320 | 330 | 340 | 350 | 360 |
| LGSLSSGRIS | IISMSVVNLK | LAVSIAIRFS | ATRCQFGPTD | KEEIPVLEYP | LQQWRILPYL |
| 370 | 380 | 390 | 400 | 410 | 420 |
| AAAYALDHFS | KTIFMDLIEV | QSARLRGDHS | DQQAELGREI | HALASAGKPL | ASWTAQRGIQ |
| 430 | 440 | 450 | 460 | 470 | 480 |
| ECREACGGHG | YLAMNRFGDL | RNDNDPNCTY | EGDNNVLLQQ | TSNYLLSLLE | PPLQDGAHFT |
| 490 | 500 | 510 | 520 | 530 | 540 |
| SPLKTVDFLE | AYPGILGQKF | LGSSKADWMD | SAAPLAAYRW | LVCYLLQESH | RRYCQEKKSR |
| 550 | 560 | 570 | 580 | 590 | 600 |
| GSDFEARNNS | QVYGCRPLAL | AFMELTVMQR | FHEHIHSSGL | SPSLRTVLGR | LSTLYGLWCL |
| 610 | 620 | 630 | 640 | 650 | 660 |
| SQHMALLYRG | GYISGEQTGR | AMEDAILTLC | EQLKDDAVAL | VDVIAPSDFV | LNSPIAKADG |
| 670 | 680 | 690 | |||
| ELYKNLWAAV | LQQNGVLERA | AWWPEFSANK | SVADRLKSQL |