Q3A825
Gene name |
nuoBCD (nuoB, nuoC, nuoD, Pcar_0206) |
Protein name |
NADH-quinone oxidoreductase subunit B/C/D |
Names |
NADH dehydrogenase I subunit B/C/D, NDH-1 subunit B/C/D |
Species |
Syntrophotalea carbinolica (strain DSM 2380 / NBRC 103641 / GraBd1) (Pelobacter carbinolicus) |
KEGG Pathway |
pca:Pcar_0206 |
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 Q3A825
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-Q3A825-F1 | Predicted | AlphaFoldDB |
No variants for Q3A825
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for Q3A825 | |||||
No associated diseases with Q3A825
3 regional properties for Q3A825
1 GO annotations of cellular component
| Name | Definition |
|---|---|
| plasma membrane | The membrane surrounding a cell that separates the cell from its external environment. It consists of a phospholipid bilayer and associated proteins. |
5 GO annotations of molecular function
| Name | Definition |
|---|---|
| 4 iron, 4 sulfur cluster binding | Binding to a 4 iron, 4 sulfur (4Fe-4S) cluster; this cluster consists of four iron atoms, with the inorganic sulfur atoms found between the irons and acting as bridging ligands. |
| iron ion binding | Binding to an iron (Fe) ion. |
| NAD binding | Binding to nicotinamide adenine dinucleotide, a coenzyme involved in many redox and biosynthetic reactions; binding may be to either the oxidized form, NAD+, or the reduced form, NADH. |
| NADH dehydrogenase (ubiquinone) activity | Catalysis of the reaction: NADH + ubiquinone + 5 H(+)(in) <=> NAD(+) + ubiquinol + 4 H(+)(out). |
| quinone binding | Binding to a quinone, any member of a class of diketones derivable from aromatic compounds by conversion of two CH groups into CO groups with any necessary rearrangement of double bonds. |
No GO annotations of biological process
| Name | Definition |
|---|---|
| No GO annotations for biological process |
No homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| No homologous proteins | ||||
| 10 | 20 | 30 | 40 | 50 | 60 |
| MSESIPKNII | LTTLDDAINW | GRKNSMWPMF | FGLSCCFVEM | MGSMTPRFDL | ARFGAEVLRG |
| 70 | 80 | 90 | 100 | 110 | 120 |
| TPREADLMVI | AGTPFKKMAA | SMLRVYEEMA | NPKWVIAMGS | CANSGGMYDV | YSVMQGVNQV |
| 130 | 140 | 150 | 160 | 170 | 180 |
| LPVDVYIPGC | PPRPEAFMQG | LMTLQEKIAR | KESPARPVLN | LRGGNEGTTV | PILIDGSSKT |
| 190 | 200 | 210 | 220 | 230 | 240 |
| RDTRGPGYGH | CPIRGTAQQH | PDFKGHRAAG | MWGPPQPKIA | FSASTAPLLE | QLRERFGDDV |
| 250 | 260 | 270 | 280 | 290 | 300 |
| RQEEGADMPT | LVADPAQVPE | LLRFLKQDID | QPYERLEDLT | AIDETARSQR | PAHDLTMVYH |
| 310 | 320 | 330 | 340 | 350 | 360 |
| LLSFERAGYL | RVKAPLRNDR | AEVPSITGLW | PAANWYEREA | FDMFGVRFAG | HPDLRRILMP |
| 370 | 380 | 390 | 400 | 410 | 420 |
| EGWQGHPLRK | SHPSRATDMP | PFTRDTATTM | VPPEGSHFFS | NRAPVDNQSL | SILNLGPQHP |
| 430 | 440 | 450 | 460 | 470 | 480 |
| GTHGILRVIL | QLAGEEIVDL | DSEIGYHHRG | AEKIAERQHW | NQYIPYTDRI | DYLAGSLNNL |
| 490 | 500 | 510 | 520 | 530 | 540 |
| AYLYSVETLC | GVEVPPRARY | IRVLLSELFR | IASHLVWLGT | FAHDVGAMTP | VFYAFDSREK |
| 550 | 560 | 570 | 580 | 590 | 600 |
| IFDIIELITG | GRMHPAWFRI | GGVPDDLPDG | WLAAVEAFTR | DFEARIDEFD | RLLTGGPIFR |
| 610 | 620 | 630 | 640 | 650 | 660 |
| ARTEGIGTVS | RQQAVELGFS | GPNLRATGLA | WDLRKSMPYG | GYDEFDFDVV | TAGGGDCFAR |
| 670 | 680 | 690 | 700 | 710 | 720 |
| YLVRLGELRQ | SLRIVRQAAE | GMPQGRWISD | QYRYAYPKRE | DGLQDIESLI | HHFLHVSRGP |
| 730 | 740 | 750 | 760 | 770 | 780 |
| AAPRGECYRA | IESSKGECGY | YAVSDGGTGA | YRLRIRTPSF | PHLQALPQLS | RGRLVADVIT |
| 790 | |||||
| ILGSLDYVLA | DLDR |