P34956
Gene name |
qoxB (BSU38160, ipa-38d) |
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 subtilis (strain 168) |
KEGG Pathway |
bsu:BSU38160 |
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
4 structures for P34956
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| 6KOB | X-ray | 360 A | A/E | 1-649 | PDB |
| 6KOC | X-ray | 380 A | A/E | 1-649 | PDB |
| 6KOE | X-ray | 375 A | A/E | 1-649 | PDB |
| AF-P34956-F1 | Predicted | AlphaFoldDB |
No variants for P34956
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for P34956 | |||||
No associated diseases with P34956
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. |
4 GO annotations of biological process
| Name | Definition |
|---|---|
| aerobic respiration | The enzymatic release of energy from inorganic and organic compounds (especially carbohydrates and fats) which requires oxygen as the terminal electron acceptor. |
| ATP synthesis coupled electron transport | The transfer of electrons through a series of electron donors and acceptors, generating energy that is ultimately used for synthesis of ATP. |
| electron transport coupled proton transport | The transport of protons against an electrochemical gradient, using energy from electron transport. |
| respiratory 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 any of several different terminal electron acceptors 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 |
| 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 |
| FARKQLFGYK | 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 | VGRTLDWATS |
| 550 | 560 | 570 | 580 | 590 | 600 |
| SAIPPHYNFA | VLPEVKSQDA | FLHMKEEKTE | LYPESKFKKI | HMPSNSGRPF | FMSVAFGLAG |
| 610 | 620 | 630 | 640 | ||
| FGLVFEWYWM | GVVGLIGVLL | CMVLRSFEYD | NGYYISVDEI | KETERKISE |