P97872
Gene name |
Fmo5 |
Protein name |
Flavin-containing monooxygenase 5 |
Names |
FMO 5, Dimethylaniline monooxygenase [N-oxide-forming] 5, Dimethylaniline oxidase 5, Hepatic flavin-containing monooxygenase 5, NADPH oxidase |
Species |
Mus musculus (Mouse) |
KEGG Pathway |
mmu:14263 |
EC number |
1.6.3.1: 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 P97872
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-P97872-F1 | Predicted | AlphaFoldDB |
22 variants for P97872
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| rs37557226 | 47 | A>T | No | EVA | |
| rs232178366 | 82 | Y>F | No | EVA | |
| rs3388651186 | 90 | E>* | No | EVA | |
| rs3388638395 | 98 | E>D | No | EVA | |
| rs3388654944 | 109 | T>I | No | EVA | |
| rs3388643934 | 130 | T>I | No | EVA | |
| rs1134264990 | 155 | H>L | No | EVA | |
| rs3388654075 | 170 | K>E | No | EVA | |
| rs3388647614 | 178 | K>M | No | EVA | |
| rs36298704 | 181 | V>M | No | EVA | |
| rs214803069 | 209 | K>M | No | EVA | |
| rs3388649493 | 231 | P>L | No | EVA | |
| rs237794467 | 234 | L>M | No | EVA | |
| rs3388654996 | 255 | N>S | No | EVA | |
| rs36785610 | 313 | V>I | No | EVA | |
| rs3388654119 | 326 | V>I | No | EVA | |
| rs3388644014 | 354 | K>Q | No | EVA | |
| rs3388651213 | 394 | K>Q | No | EVA | |
| rs3388649504 | 414 | E>K | No | EVA | |
| rs242145991 | 458 | R>K | No | EVA | |
| rs3388647671 | 469 | T>A | No | EVA | |
| rs3388654973 | 532 | Y>C | No | EVA |
No associated diseases with P97872
No regional properties for P97872
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| No domain, repeats, and functional sites for P97872 | |||
Functions
| Description | ||
|---|---|---|
| EC Number | 1.6.3.1 | With oxygen as acceptor |
| Subcellular Localization |
|
|
| PANTHER Family | ||
| PANTHER Subfamily | ||
| PANTHER Protein Class | ||
| PANTHER Pathway Category | No pathway information available | |
4 GO annotations of cellular component
| Name | Definition |
|---|---|
| cytosol | The part of the cytoplasm that does not contain organelles but which does contain other particulate matter, such as protein complexes. |
| endoplasmic reticulum | The irregular network of unit membranes, visible only by electron microscopy, that occurs in the cytoplasm of many eukaryotic cells. The membranes form a complex meshwork of tubular channels, which are often expanded into slitlike cavities called cisternae. The ER takes two forms, rough (or granular), with ribosomes adhering to the outer surface, and smooth (with no ribosomes attached). |
| endoplasmic reticulum membrane | The lipid bilayer surrounding the endoplasmic reticulum. |
| integral component of membrane | The component of a membrane consisting of the gene products and protein complexes having at least some part of their peptide sequence embedded in the hydrophobic region of the membrane. |
6 GO annotations of molecular function
| Name | Definition |
|---|---|
| aldehyde oxidase activity | Catalysis of the reaction: an aldehyde + H2O + O2 = a carboxylic acid + hydrogen peroxide. |
| 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. |
| monooxygenase activity | Catalysis of the incorporation of one atom from molecular oxygen into a compound and the reduction of the other atom of oxygen to water. |
| N,N-dimethylaniline monooxygenase activity | Catalysis of the reaction: N,N-dimethylaniline + NADPH + H+ + O2 = N,N-dimethylaniline N-oxide + NADP+ + H2O. |
| NADP binding | Binding to nicotinamide-adenine dinucleotide phosphate, a coenzyme involved in many redox and biosynthetic reactions; binding may be to either the oxidized form, NADP+, or the reduced form, NADPH. |
| NADPH oxidase H202-forming activity | Catalysis of the reaction: NADPH + H+ + O2 = NADP + hydrogen peroxide (H2O2). |
4 GO annotations of biological process
| Name | Definition |
|---|---|
| lipid metabolic process | The chemical reactions and pathways involving lipids, compounds soluble in an organic solvent but not, or sparingly, in an aqueous solvent. Includes fatty acids; neutral fats, other fatty-acid esters, and soaps; long-chain (fatty) alcohols and waxes; sphingoids and other long-chain bases; glycolipids, phospholipids and sphingolipids; and carotenes, polyprenols, sterols, terpenes and other isoprenoids. |
| NADPH oxidation | A metabolic process that results in the oxidation of reduced nicotinamide adenine dinucleotide, NADPH, to the oxidized form, NADP. |
| regulation of cholesterol metabolic process | Any process that modulates the rate, frequency, or extent of cholesterol metabolism, the chemical reactions and pathways involving cholesterol, cholest-5-en-3 beta-ol, the principal sterol of vertebrates and the precursor of many steroids, including bile acids and steroid hormones. |
| xenobiotic metabolic process | The chemical reactions and pathways involving a xenobiotic compound, a compound foreign to the organim exposed to it. It may be synthesized by another organism (like ampicilin) or it can be a synthetic chemical. |
12 homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| P31512 | FMO4 | Dimethylaniline monooxygenase [N-oxide-forming] 4 | Homo sapiens (Human) | PR |
| P49326 | FMO5 | Flavin-containing monooxygenase 5 | Homo sapiens (Human) | PR |
| P97501 | Fmo3 | Dimethylaniline monooxygenase [N-oxide-forming] 3 | Mus musculus (Mouse) | PR |
| Q8K2I3 | Fmo2 | Dimethylaniline monooxygenase [N-oxide-forming] 2 | Mus musculus (Mouse) | PR |
| Q8VHG0 | Fmo4 | Dimethylaniline monooxygenase [N-oxide-forming] 4 | Mus musculus (Mouse) | PR |
| Q8K4B7 | Fmo4 | Dimethylaniline monooxygenase [N-oxide-forming] 4 | Rattus norvegicus (Rat) | PR |
| Q6IRI9 | Fmo2 | Dimethylaniline monooxygenase [N-oxide-forming] 2 | Rattus norvegicus (Rat) | PR |
| Q9EQ76 | Fmo3 | Dimethylaniline monooxygenase [N-oxide-forming] 3 | Rattus norvegicus (Rat) | PR |
| Q8K4C0 | Fmo5 | Flavin-containing monooxygenase 5 | Rattus norvegicus (Rat) | PR |
| Q9SVU0 | YUC8 | Probable indole-3-pyruvate monooxygenase YUCCA8 | Arabidopsis thaliana (Mouse-ear cress) | PR |
| Q9SXD9 | At1g62580 | Flavin-containing monooxygenase FMO GS-OX-like 7 | Arabidopsis thaliana (Mouse-ear cress) | PR |
| Q9C8T8 | At1g63340 | Putative flavin-containing monooxygenase FMO GS-OX-like 10 | Arabidopsis thaliana (Mouse-ear cress) | PR |
| 10 | 20 | 30 | 40 | 50 | 60 |
| MAKKRIAVIG | AGASGLTCIK | CCLEEGLEPV | CFERSGDIGG | LWRFQEAPEE | GRASIYQSVV |
| 70 | 80 | 90 | 100 | 110 | 120 |
| INTSKEMMCF | SDYPIPDHYP | NYMHNSQVLE | YFRMYAKEFD | LLKYIQFKTT | VCSVKKQPDF |
| 130 | 140 | 150 | 160 | 170 | 180 |
| STSGQWQVVT | ECEGKQQVDV | FDGVLVCTGH | HTDAHLPLES | FPGIEKFKGK | YFHSRDYKNP |
| 190 | 200 | 210 | 220 | 230 | 240 |
| VEFTGKRVIV | IGIGNSGGDL | AVEISHTAKQ | VFLSTRRGAW | ILNRVGKHGY | PIDLLLSSRI |
| 250 | 260 | 270 | 280 | 290 | 300 |
| MYYLSRICGP | SLKNNYMEKQ | MNQRFDHEMF | GLKPKHRALS | QHPTVNDDLP | NRIIAGLVKV |
| 310 | 320 | 330 | 340 | 350 | 360 |
| KGNVKEFTET | AAVFEDGSRE | DGIDVVIFAT | GYSFAFPFLE | DSVKVVKNKV | SLYKKVFPPN |
| 370 | 380 | 390 | 400 | 410 | 420 |
| LEKPTLAIIG | LIQPLGAIMP | ISELQGRWAT | QVFKGLKKLP | SQSEMMAEIN | KAREEMAKRY |
| 430 | 440 | 450 | 460 | 470 | 480 |
| VDSQRHTIQG | DYIDTMEEIA | DLVGVRPNIL | PLVFTDPRLA | LRLLLGPCTP | VQYRLQGPGK |
| 490 | 500 | 510 | 520 | 530 | |
| WAGARKTILT | TEDRVRKPLM | TRVVERDSSG | GSLVTVRVLM | LAVAFFAVIL | AYF |