Q7SBB6
Gene name |
NCU06207 |
Protein name |
Probable Delta(7)-sterol 5(6)-desaturase |
Names |
C-5 sterol desaturase, Ergosterol Delta(5,6) desaturase, Sterol-C5-desaturase |
Species |
Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987) |
KEGG Pathway |
ncr:NCU06207 |
EC number |
1.14.19.20: 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 Q7SBB6
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-Q7SBB6-F1 | Predicted | AlphaFoldDB |
No variants for Q7SBB6
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for Q7SBB6 | |||||
No associated diseases with Q7SBB6
1 regional properties for Q7SBB6
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| domain | Fatty acid hydroxylase | 167 - 292 | IPR006694 |
Functions
| Description | ||
|---|---|---|
| EC Number | 1.14.19.20 | 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 | |
4 GO annotations of cellular component
| Name | Definition |
|---|---|
| endoplasmic reticulum lumen | The volume enclosed by the membranes of the endoplasmic reticulum. |
| 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. |
| membrane | A lipid bilayer along with all the proteins and protein complexes embedded in it an attached to it. |
4 GO annotations of molecular function
| Name | Definition |
|---|---|
| C-5 sterol desaturase activity | Catalysis of the reaction: 5,7,24(28)-ergostatrienol + O2 + NADPH = 5,7,22,24(28)-ergostatetraenol + 2 H2O + NADP+. |
| delta7-sterol 5(6)-desaturase activity | Catalysis of the reaction: a delta(7)-sterol + 2 ferrocytochrome b5 + O2 + 2 H+ -> a delta(5,7)-sterol + 2 ferricytochrome b5 + 2 H2O. |
| iron ion binding | Binding to an iron (Fe) ion. |
| oxidoreductase activity | Catalysis of an oxidation-reduction (redox) reaction, a reversible chemical reaction in which the oxidation state of an atom or atoms within a molecule is altered. One substrate acts as a hydrogen or electron donor and becomes oxidized, while the other acts as hydrogen or electron acceptor and becomes reduced. |
2 GO annotations of biological process
| Name | Definition |
|---|---|
| ergosterol biosynthetic process | The chemical reactions and pathways resulting in the formation of ergosterol, (22E)-ergosta-5,7,22-trien-3-beta-ol, a sterol found in ergot, yeast and moulds. |
| sterol biosynthetic process | The chemical reactions and pathways resulting in the formation of sterols, steroids with one or more hydroxyl groups and a hydrocarbon side-chain in the molecule. |
No homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| No homologous proteins | ||||
| 10 | 20 | 30 | 40 | 50 | 60 |
| MDVVLEVTDQ | FMFDYMYAWL | LPARPALYDF | PDKTNGTAQA | FSSWVYEPAT | KFFSLEPSQA |
| 70 | 80 | 90 | 100 | 110 | 120 |
| AYQSIWTRDN | IYRQALSLFL | ILWLFGLVTY | YVFASLSYIF | VFDKKTMEHP | KFLKNQVWLE |
| 130 | 140 | 150 | 160 | 170 | 180 |
| IKQTNAALPV | MAFFTFPFLV | AEVRGYSLLY | DTTAEGPGRW | YDFFQFPLFI | MFTDFGIYWI |
| 190 | 200 | 210 | 220 | 230 | 240 |
| HRGLHHPLVY | KHLHKPHHKW | IMPTPYASHA | FHPIDGFAQS | IPYHIFPFIF | PLQKMAYVGL |
| 250 | 260 | 270 | 280 | 290 | 300 |
| FVFINFWTIM | IHDGEYYANN | PVINGAACHS | VHHFAFNYNY | GQFTTLWDRL | GGSYREPDGD |
| 310 | 320 | 330 | 340 | ||
| MFAKEKKMST | TTWKKQVNEM | EKIVKEVEGE | DDRLYEPTET | KKSK |