E0TW66
Gene name |
qoxB (BSUW23_18870) |
Protein name |
Quinol oxidase subunit 1 |
Names |
Oxidase aa(3)-600 subunit 1, Quinol oxidase aa3-600, subunit qoxB, Quinol oxidase polypeptide I |
Species |
Bacillus spizizenii (strain ATCC 23059 / NRRL B-14472 / W23) (Bacillus subtilis subsp. spizizenii) |
KEGG Pathway |
bss:BSUW23_18870 |
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 E0TW66
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-E0TW66-F1 | Predicted | AlphaFoldDB |
No variants for E0TW66
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for E0TW66 | |||||
No associated diseases with E0TW66
No regional properties for E0TW66
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| No domain, repeats, and functional sites for E0TW66 | |||
3 GO annotations of cellular component
| Name | Definition |
|---|---|
| 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. |
| respirasome | The protein complexes that form the electron transport system (the respiratory chain), associated with a cell membrane, usually the plasma membrane (in prokaryotes) or the inner mitochondrial membrane (on eukaryotes). The respiratory chain complexes transfer electrons from an electron donor to an electron acceptor and are associated with a proton pump to create a transmembrane electrochemical gradient. |
4 GO annotations of molecular function
| Name | Definition |
|---|---|
| copper ion binding | Binding to a copper (Cu) ion. |
| cytochrome-c oxidase activity | Catalysis of the reaction: 4 ferrocytochrome c + O2 + 4 H+ = 4 ferricytochrome c + 2 H2O. |
| heme binding | Binding to a heme, a compound composed of iron complexed in a porphyrin (tetrapyrrole) ring. |
| 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 |
|---|---|
| oxidative phosphorylation | The phosphorylation of ADP to ATP that accompanies the oxidation of a metabolite through the operation of the respiratory chain. Oxidation of compounds establishes a proton gradient across the membrane, providing the energy for ATP synthesis. |
No homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| No homologous proteins | ||||
| 10 | 20 | 30 | 40 | 50 | 60 |
| MKFKWDEFFV | TGDPLILGAQ | VSIALSTIAI | IFVLTYFKKW | KWLWSEWITT | VDHKKLGIMY |
| 70 | 80 | 90 | 100 | 110 | 120 |
| IISAVIMLFR | GGVDGLMMRA | QLALPNNSFL | DSNHYNEIFT | THGTIMIIFM | AMPFLIGLIN |
| 130 | 140 | 150 | 160 | 170 | 180 |
| VVVPLQIGAR | DVAFPYLNNL | SFWTFFVGAM | LFNISFVIGG | SPNAGWTSYM | PLASNDMSPG |
| 190 | 200 | 210 | 220 | 230 | 240 |
| PGENYYLLGL | QIAGIGTLMT | GINFMVTILK | MRTKGMTLMR | MPMFTWTTLI | TMVIIVFAFP |
| 250 | 260 | 270 | 280 | 290 | 300 |
| VLTVALALLS | FDRLFGAHFF | TLEAGGMPML | WANLFWIWGH | PEVYIVILPA | FGIFSEIISS |
| 310 | 320 | 330 | 340 | 350 | 360 |
| FARKQLFGYT | AMVGSIIAIS | VLSFLVWTHH | FFTMGNSASV | NSFFSITTMA | ISIPTGVKIF |
| 370 | 380 | 390 | 400 | 410 | 420 |
| NWLFTMYKGR | ISFTTPMLWA | LAFIPNFVIG | GVTGVMLAMA | AADYQYHNTY | FLVSHFHYVL |
| 430 | 440 | 450 | 460 | 470 | 480 |
| IAGTVFACFA | GFIFWYPKMF | GHKLNERIGK | WFFWIFMIGF | NICFFPQYFL | GLQGMPRRIY |
| 490 | 500 | 510 | 520 | 530 | 540 |
| TYGPNDGWTT | LNFISTVGAF | MMGVGFLILC | YNIYYSFRYS | TREISGDSWG | VGRSLDWATS |
| 550 | 560 | 570 | 580 | 590 | 600 |
| SAIPPHYNFA | VLPEVKSKDA | FHHMKEEKTE | LYPESKFKKI | HMPSNSGRPF | FMSVAFGIAG |
| 610 | 620 | 630 | 640 | ||
| FGLVFEWYWM | GVVGLIGVLL | CMVLRSFEYD | NGYYISVDEI | KETERKISE |