B5UAQ8
Gene name |
CYP719A5 |
Protein name |
Cheilanthifoline synthase |
Names |
CHS, Cytochrome P450 719A5 |
Species |
Eschscholzia californica (California poppy) |
KEGG Pathway |
|
EC number |
1.14.19.65: With oxidation of a pair of donors resulting in the reduction of molecular oxygen to two molecules of water |
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 B5UAQ8
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-B5UAQ8-F1 | Predicted | AlphaFoldDB |
No variants for B5UAQ8
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for B5UAQ8 | |||||
No associated diseases with B5UAQ8
1 regional properties for B5UAQ8
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| conserved_site | Cytochrome P450, conserved site | 425 - 434 | IPR017972 |
Functions
| Description | ||
|---|---|---|
| EC Number | 1.14.19.65 | With oxidation of a pair of donors resulting in the reduction of molecular oxygen to two molecules of water |
| 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 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. |
4 GO annotations of molecular function
| Name | Definition |
|---|---|
| (S)-cheilanthifoline synthase activity | Catalysis of the reaction: (S)-scoulerine + + O2 -> (S)-cheilanthifoline |
| 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. |
1 GO annotations of biological process
| Name | Definition |
|---|---|
| isoquinoline alkaloid biosynthetic process | The chemical reactions and pathways resulting in the formation of isoquinoline alkaloids, alkaloid compounds that contain bicyclic N-containing aromatic rings and are derived from a 3,4-dihydroxytyramine (dopamine) precursor that undergoes a Schiff base addition with aldehydes of different origin. |
No homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| No homologous proteins | ||||
| 10 | 20 | 30 | 40 | 50 | 60 |
| MEESLWVVTA | TVVVVFAIAK | LLKKSSSIST | MEWPKGPKKL | PIIGNLHQLG | GEAFHVVLAN |
| 70 | 80 | 90 | 100 | 110 | 120 |
| LAKIHGTVMT | IWVGAWRPMI | VISDIDKAWE | VLVNKSSDYA | GRDFPEITKI | ISANWKNISC |
| 130 | 140 | 150 | 160 | 170 | 180 |
| SDSGPFWQNL | RKGLQGGALA | PLNVISQYQL | QERDMKNLIT | SMQEKASKNN | GILKPLDYLK |
| 190 | 200 | 210 | 220 | 230 | 240 |
| EETIRLLSRL | IFGQSFNDEN | FVKGVHLALD | DLVRISGYAS | LADAFKFCEN | LPSHKKSIRE |
| 250 | 260 | 270 | 280 | 290 | 300 |
| VHEVNERVVN | LVKPYLVKNP | PTNTYLYFLN | SQKFSDEVII | SAVLEVYDLG | VDSTASTAVW |
| 310 | 320 | 330 | 340 | 350 | 360 |
| ALTFLVREPR | VQEKLYKEII | DLTGGERSVK | VEDVSKLPYL | QAVMKETMRM | KPIAPMAIPH |
| 370 | 380 | 390 | 400 | 410 | 420 |
| KTSRDTSLMG | KKVNKGTSIM | VNLYAIHHNP | KVFPEPYKFI | PERFLQGQES | KYGDIKEMEQ |
| 430 | 440 | 450 | 460 | 470 | 480 |
| SLLPFSAGMR | ICAGMELGKL | QYGFSLASLV | EAFKWTCAVD | GKLPDLSEDH | CFILLMKNPL |
| EARITPRTQL |