P38866
Gene name |
FMO1 (YHR176W) |
Protein name |
Thiol-specific monooxygenase |
Names |
Flavin-dependent monooxygenase |
Species |
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
KEGG Pathway |
sce:YHR176W |
EC number |
|
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 P38866
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-P38866-F1 | Predicted | AlphaFoldDB |
13 variants for P38866
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| s08-454385 | 53 | K>E | No | SGRP | |
| s08-454436 | 70 | K>E | No | SGRP | |
| s08-454572 | 115 | S>N | No | SGRP | |
| s08-454605 | 126 | S>F | No | SGRP | |
| s08-454653 | 142 | D>G | No | SGRP | |
| s08-454715 | 163 | A>T | No | SGRP | |
| s08-454745 | 173 | G>S | No | SGRP | |
| s08-454748 | 174 | A>T | No | SGRP | |
| s08-454905 | 226 | L>P | No | SGRP | |
| s08-454986 | 253 | R>K | No | SGRP | |
| s08-455012 | 262 | I>V | No | SGRP | |
| s08-455463 | 412 | A>V | No | SGRP | |
| s08-455477 | 417 | A>T | No | SGRP |
No associated diseases with P38866
No regional properties for P38866
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| No domain, repeats, and functional sites for P38866 | |||
2 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 membrane | The lipid bilayer surrounding the endoplasmic reticulum. |
4 GO annotations of molecular function
| Name | Definition |
|---|---|
| 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. |
1 GO annotations of biological process
| Name | Definition |
|---|---|
| protein folding | The process of assisting in the covalent and noncovalent assembly of single chain polypeptides or multisubunit complexes into the correct tertiary structure. |
1 homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| Q9SVU0 | YUC8 | Probable indole-3-pyruvate monooxygenase YUCCA8 | Arabidopsis thaliana (Mouse-ear cress) | PR |
| 10 | 20 | 30 | 40 | 50 | 60 |
| MTVNDKKRLA | IIGGGPGGLA | AARVFSQSLP | NFEIEIFVKD | YDIGGVWHYP | EQKSDGRVMY |
| 70 | 80 | 90 | 100 | 110 | 120 |
| DHLETNISKK | LMQFSGFPFE | ENVPLYPSRR | NIWEYLKAYY | KTFIANKDAI | SIHFSTEVTY |
| 130 | 140 | 150 | 160 | 170 | 180 |
| LKKKNSQWEI | TSKDELRTTK | SDFDFVIVAS | GHYSVPKLPT | NIAGLDLWFD | NKGAFHSKDF |
| 190 | 200 | 210 | 220 | 230 | 240 |
| KNCEFAREKV | VIVVGNGSSG | QDIANQLTTV | AKKVYNSIKE | PASNQLKAKL | IETVQTIDSA |
| 250 | 260 | 270 | 280 | 290 | 300 |
| DWKNRSVTLS | DGRVLQNIDY | IIFATGYYYS | FPFIEPSVRL | EVLGEGVTGD | KHSSVNLHNL |
| 310 | 320 | 330 | 340 | 350 | 360 |
| WEHMIYVKDP | TLSFILTPQL | VIPFPLSELQ | AAIMVEVFCK | SLPITTTFDS | NACGTHNFPK |
| 370 | 380 | 390 | 400 | 410 | 420 |
| GKDLEYYAEL | QELLNSIPRR | VGHFEPVVWD | DRLIDLRNSS | YTDKEERNVL | LAEHAQALKK |
| 430 | |||||
| KKAPYFLPAP | HT |