P94364
Gene name |
cimH (yxkJ, BSU38770) |
Protein name |
Cytochrome bd ubiquinol oxidase subunit 1 |
Names |
Cytochrome d ubiquinol oxidase subunit I |
Species |
Bacillus subtilis (strain 168) |
KEGG Pathway |
bsu:BSU38760 |
EC number |
7.1.1.7: Hydron translocation or charge separation linked to oxidoreductase reactions |
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 P94364
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-P94364-F1 | Predicted | AlphaFoldDB |
No variants for P94364
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for P94364 | |||||
No associated diseases with P94364
No regional properties for P94364
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| No domain, repeats, and functional sites for P94364 | |||
Functions
| Description | ||
|---|---|---|
| EC Number | 7.1.1.7 | Hydron translocation or charge separation linked to oxidoreductase reactions |
| Subcellular Localization |
|
|
| PANTHER Family | ||
| PANTHER Subfamily | ||
| PANTHER Protein Class | ||
| PANTHER Pathway Category | No pathway information available | |
3 GO annotations of cellular component
| Name | Definition |
|---|---|
| cytochrome complex | A protein complex in which at least one of the proteins is a cytochrome, i.e. a heme-containing protein involved in catalysis of redox reactions. |
| 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. |
| plasma membrane | The membrane surrounding a cell that separates the cell from its external environment. It consists of a phospholipid bilayer and associated proteins. |
4 GO annotations of molecular function
| Name | Definition |
|---|---|
| electron transfer activity | Any molecular entity that serves as an electron acceptor and electron donor in an electron transport chain. An electron transport chain is a process in which a series of electron carriers operate together to transfer electrons from donors to any of several different terminal electron acceptors to generate a transmembrane electrochemical gradient. |
| heme binding | Binding to a heme, a compound composed of iron complexed in a porphyrin (tetrapyrrole) ring. |
| metal ion binding | Binding to a metal ion. |
| oxidoreductase activity, acting on diphenols and related substances as donors, oxygen as acceptor | Catalysis of an oxidation-reduction (redox) reaction in which a diphenol, or related compound, acts as a hydrogen or electron donor and reduces oxygen. |
1 GO annotations of biological process
| Name | Definition |
|---|---|
| aerobic electron transport chain | A process in which a series of electron carriers operate together to transfer electrons from donors such as NADH and FADH2 to oxygen to generate a transmembrane electrochemical gradient. |
No homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| No homologous proteins | ||||
| 10 | 20 | 30 | 40 | 50 | 60 |
| MSELVLARIQ | FASTTLFHFL | FVPMSIGLVF | MVALMETLYL | VKKNELYLKM | AKFWGHLFLI |
| 70 | 80 | 90 | 100 | 110 | 120 |
| NFAVGVVTGI | LQEFQFGLNW | SDYSRFVGDV | FGAPLAIEAL | LAFFMESIFI | GLWIFGWDRL |
| 130 | 140 | 150 | 160 | 170 | 180 |
| PKKIHALCIW | LVSFGTIMSS | FWILTANSFM | QEPVGFTIKN | GRAEMNDFGA | LITNPQLWVE |
| 190 | 200 | 210 | 220 | 230 | 240 |
| FPHVIFGALA | TGAFFIAGVS | AFKLLKKKEV | PFFKQSFKLA | MIVGLCAGLG | VGLSGHMQAE |
| 250 | 260 | 270 | 280 | 290 | 300 |
| HLMESQPMKM | AASEGLWEDS | GDPAAWTAFA | TIDTKNEKSS | NEIKVPYALS | YLAYQKFSGS |
| 310 | 320 | 330 | 340 | 350 | 360 |
| VKGMKTLQAE | YEKIYGKGDY | IPPVKTTFWS | FRIMVGAGVV | MILAALGGLW | LNRRKKLENS |
| 370 | 380 | 390 | 400 | 410 | 420 |
| KWYLRIMIAL | ISFPFLANSA | GWIMTEIGRQ | PWTVMGLMTT | AQSVSPNVTA | GSLLFSIIAF |
| 430 | 440 | 450 | 460 | ||
| GVMYMILGAL | LVFLFIREIK | KGAEHDNHHD | VPVSTDPFSQ | EVYHGISS |