Q9M7B7
Gene name |
CYP79D2 |
Protein name |
Valine N-monooxygenase 2 |
Names |
Cytochrome P450 79D2 |
Species |
Manihot esculenta (Cassava) (Jatropha manihot) |
KEGG Pathway |
ag:AAV97888 |
EC number |
1.14.14.38: With reduced flavin or flavoprotein as one donor, and incorporation of one atom of oxygen |
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 Q9M7B7
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-Q9M7B7-F1 | Predicted | AlphaFoldDB |
No variants for Q9M7B7
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for Q9M7B7 | |||||
No associated diseases with Q9M7B7
1 regional properties for Q9M7B7
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| conserved_site | Cytochrome P450, conserved site | 470 - 479 | IPR017972 |
Functions
| Description | ||
|---|---|---|
| EC Number | 1.14.14.38 | With reduced flavin or flavoprotein as one donor, and incorporation of one atom of oxygen |
| Subcellular Localization |
|
|
| PANTHER Family | ||
| PANTHER Subfamily | ||
| PANTHER Protein Class | ||
| PANTHER Pathway Category | No pathway information available | |
2 GO annotations of cellular component
| Name | Definition |
|---|---|
| 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). |
| 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. |
4 GO annotations of molecular function
| Name | Definition |
|---|---|
| heme binding | Binding to a heme, a compound composed of iron complexed in a porphyrin (tetrapyrrole) ring. |
| iron ion binding | Binding to an iron (Fe) ion. |
| 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. |
| valine N-monooxygenase (oxime forming) activity | Catalysis of the reaction: L-valine + 2 O2 + 2 NADPH(4-) + 2 H+ <=> (E)-2-methylpropanal oxime + 2 NADP(3-) + carbon dioxide + 3 H2O. |
1 GO annotations of biological process
| Name | Definition |
|---|---|
| cyanogenic glycoside biosynthetic process | The chemical reactions and pathways resulting in the formation of cyanogenic glycosides, any glycoside containing a cyano group that is released as hydrocyanic acid on acid hydrolysis; such compounds occur in the kernels of various fruits. |
No homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| No homologous proteins | ||||
| 10 | 20 | 30 | 40 | 50 | 60 |
| MAMNVSTTAT | TTASFASTSS | MNNTAKILLI | TLFISIVSTV | IKLQKRASYK | KASKNFPLPP |
| 70 | 80 | 90 | 100 | 110 | 120 |
| GPTPWPLIGN | IPEMIRYRPT | FRWIHQLMKD | MNTDICLIRF | GKTNVVPISC | PVIAREILKK |
| 130 | 140 | 150 | 160 | 170 | 180 |
| HDAVFSNRPK | ILCAKTMSGG | YLTTIVVPYN | DQWKKMRKVL | TSEIISPARH | KWLHDKRAEE |
| 190 | 200 | 210 | 220 | 230 | 240 |
| ADQLVFYINN | QYKSNKNVNV | RIAARHYGGN | VIRKMMFSKR | YFGKGMPDGG | PGPEEIMHVD |
| 250 | 260 | 270 | 280 | 290 | 300 |
| AIFTALKYLY | GFCISDYLPF | LEGLDLDGQE | KIVLNANKTI | RDLQNPLIEE | RIQQWRSGER |
| 310 | 320 | 330 | 340 | 350 | 360 |
| KEMEDLLDVF | ITLQDSDGKP | LLNPDEIKNQ | IAEIMIATID | NPANAVEWAM | GELINQPELL |
| 370 | 380 | 390 | 400 | 410 | 420 |
| AKATEELDRV | VGKDRLVQES | DIPNLNYVKA | CAREAFRLHP | VAYFNVPHVA | MEDAVIGDYF |
| 430 | 440 | 450 | 460 | 470 | 480 |
| IPKGSWAILS | RYGLGRNPKT | WPDPLKYDPE | RHLNEGEVVL | TEHDLRFVTF | STGRRGCVAA |
| 490 | 500 | 510 | 520 | 530 | 540 |
| LLGTTMITMM | LARMLQCFTW | TPPPNVTRID | LSENIDELTP | ATPITGFAKP | RLAPHLYPTS |
| P |