O64894
Gene name |
Acx |
Protein name |
Acyl-coenzyme A oxidase, peroxisomal |
Names |
AOX, Long-chain acyl-CoA oxidase |
Species |
Cucurbita maxima (Pumpkin) (Winter squash) |
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 O64894
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-O64894-F1 | Predicted | AlphaFoldDB |
No variants for O64894
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for O64894 | |||||
No associated diseases with O64894
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 |
|---|---|
| glyoxysome | A specialized form of peroxisome that contains the enzymes of the glyoxylate pathway. The glyoxysome is found in some plant cells, notably the cells of germinating seeds. |
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 | 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). |
No homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| No homologous proteins | ||||
| 10 | 20 | 30 | 40 | 50 | 60 |
| MASPGEPNRT | AEDESQAAAR | RIERLSLHLT | PIPLDDSQGV | EMETCAAGKA | KAKIEVDMGS |
| 70 | 80 | 90 | 100 | 110 | 120 |
| LSLYMRGKHR | EIQERVFEYF | NSRPELQTPV | GISMADHREL | CMKQLVGLVR | EAGIRPFRFV |
| 130 | 140 | 150 | 160 | 170 | 180 |
| NEDPAKYFAI | MEAVGSVDVS | LAIKMGVQFS | LWGGSVINLG | TKKHRDRFFD | GIDNVDYPGC |
| 190 | 200 | 210 | 220 | 230 | 240 |
| FAMTELHHGS | NVQGLQTTAT | FDPITDEFII | NTPNDGAIKW | WIGNAAVHGK | FATVFAKLVL |
| 250 | 260 | 270 | 280 | 290 | 300 |
| PTHDSRKTAD | MGVHAFIVPI | RDLKSHKTLP | GIEIHDCGHK | VGLNGVDNGA | LRFRSVRIPR |
| 310 | 320 | 330 | 340 | 350 | 360 |
| DNLLNRFGEV | SRDGKYKSSL | PSINKRFAAT | LGELVGGRVG | LAYSSASVLK | IASTIAIRYS |
| 370 | 380 | 390 | 400 | 410 | 420 |
| LLRQQFGPPK | QPEVSILDYQ | SQQHKLMPML | ASTYAFHFST | MQLVEKYAQM | KKTHDEELVG |
| 430 | 440 | 450 | 460 | 470 | 480 |
| DVHALSAGLK | AYVTSYTAKS | LSTCREACGG | HGYAVVNRFG | TLRNDHDIFQ | TFEGDNTVLL |
| 490 | 500 | 510 | 520 | 530 | 540 |
| QQVAAYLLKQ | YQEKFQGGTL | AVTWNYLRES | MNTYLSQPNP | VTARWESADH | LRDPKFQLDA |
| 550 | 560 | 570 | 580 | 590 | 600 |
| FQYRTSRLLQ | SVAVRLRKHT | KNLGSFGAWN | RCLNHLLTLA | ESHIESVILA | QFIESVQRCP |
| 610 | 620 | 630 | 640 | 650 | 660 |
| NANTQATLKL | VCDLYALDRI | WNDIGTYRNV | DYVAPNKAKA | IHKLTEYLCF | QVRNIAQELV |
| 670 | 680 | ||||
| DAFDLPDHVT | RAPIAMKSNA | YSQYTQYIGF |