Q8GPG4
Gene name |
ddhA |
Protein name |
Dimethylsulfide dehydrogenase subunit alpha |
Names |
DMS DH molybdenum subunit, DMS DH subunit alpha, Dimethyl sulfide:cytochrome c2 reductase subunit alpha, Dimethylsulfide dehydrogenase molybdenum subunit |
Species |
Rhodovulum sulfidophilum (Rhodobacter sulfidophilus) |
KEGG Pathway |
ag:AAN46632 |
EC number |
1.8.2.4: With a cytochrome as acceptor |
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 Q8GPG4
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-Q8GPG4-F1 | Predicted | AlphaFoldDB |
No variants for Q8GPG4
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for Q8GPG4 | |||||
No associated diseases with Q8GPG4
6 regional properties for Q8GPG4
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| conserved_site | Twin-arginine translocation pathway, signal sequence | 1 - 28 | IPR006311 |
| conserved_site | Molybdopterin oxidoreductase, prokaryotic, conserved site | 815 - 842 | IPR006655 |
| domain | Molybdopterin oxidoreductase | 124 - 638 | IPR006656 |
| domain | Molybdopterin dinucleotide-binding domain | 778 - 871 | IPR006657 |
| domain | Molybdopterin oxidoreductase, 4Fe-4S domain | 59 - 123 | IPR006963 |
| domain | Nitrate reductase alpha subunit-like, MopB domain | 776 - 908 | IPR037943 |
Functions
| Description | ||
|---|---|---|
| EC Number | 1.8.2.4 | With a cytochrome as acceptor |
| Subcellular Localization |
|
|
| PANTHER Family | ||
| PANTHER Subfamily | ||
| PANTHER Protein Class | ||
| PANTHER Pathway Category | No pathway information available | |
1 GO annotations of cellular component
| Name | Definition |
|---|---|
| periplasmic space | The region between the inner (cytoplasmic) and outer membrane (Gram-negative Bacteria) or cytoplasmic membrane and cell wall (Fungi and Gram-positive Bacteria). |
4 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. |
| metal ion binding | Binding to a metal ion. |
| molybdopterin cofactor binding | Binding to a molybdopterin cofactor (Moco), essential for the catalytic activity of some enzymes, e.g. sulfite oxidase, xanthine dehydrogenase, and aldehyde oxidase. The cofactor consists of a mononuclear molybdenum (Mo-molybdopterin) or tungsten ion (W-molybdopterin) coordinated by one or two molybdopterin ligands. |
| 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. |
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 |
| MLRTTRRTLM | QGASLVGAGL | FAAGRGWALN | RLEPIGDTLA | EEYPYRDWED | LYRNEFTWDY |
| 70 | 80 | 90 | 100 | 110 | 120 |
| VGKAAHCINC | LGNCAFDIYV | KDGIVIREEQ | LAKYPQISPD | IPDANPRGCQ | KGAIHSTSMY |
| 130 | 140 | 150 | 160 | 170 | 180 |
| EADRLRYPMK | RVGARGEGKW | QRISWDQATE | EIADKIIDIY | EKYGPGKLMT | HTGSGNMSMM |
| 190 | 200 | 210 | 220 | 230 | 240 |
| RMAAPYRFAS | LVGGVQLDIF | TDVGDLNTGA | HLAYGNALES | FTSDAWFGAD | YIMFLLFNPV |
| 250 | 260 | 270 | 280 | 290 | 300 |
| ATRIPDAHFL | WEAKWNGARV | VSVAPDYNPS | SIHSDLWMPI | KQGADPFLAM | SMVNVIIEGK |
| 310 | 320 | 330 | 340 | 350 | 360 |
| LYNEAFMKEQ | TDLPILVRSD | NGMLLREADL | EEGGSDQVFY | HWDSRTGAAV | KVKGSMGSEE |
| 370 | 380 | 390 | 400 | 410 | 420 |
| KTLVLGDVDP | ALEGSFEVGG | IPVTTVFEKV | RAEAAKYPPE | ETAAITGIGP | GVVRAEAETF |
| 430 | 440 | 450 | 460 | 470 | 480 |
| ARAKKALLMT | GFNIGRYSNG | IYTSWALTLM | LALTGHGGRT | GGLDTSWIAW | NQPALLELAF |
| 490 | 500 | 510 | 520 | 530 | 540 |
| FDFKKLPRLE | AGGLGEFVRG | GMMEHSRQHY | DNDKLKARTG | FDLDELQEMI | DESIDAGWMP |
| 550 | 560 | 570 | 580 | 590 | 600 |
| YYGDMKGLIS | IADNKFRRNK | NAEAYRERIL | EEVEELFVDI | NVRMDSTAQW | ADYLLPAAAH |
| 610 | 620 | 630 | 640 | 650 | 660 |
| YEAWDLRSIA | FHRFVNVFSR | PVPPIGEAKS | DWEIMEILTR | KIQERAIARG | ITGYEDGDVT |
| 670 | 680 | 690 | 700 | 710 | 720 |
| RDFATIHDDY | TMDGTLMTDH | DVVSWLVENG | PEFAGATLEE | GVERGFFVMG | EDAGPTQKLR |
| 730 | 740 | 750 | 760 | 770 | 780 |
| PSEPYHAFLQ | QTEGKEPYKT | MTGRITFFVD | HPRFVRLGAT | VPTARHHAGR | DASNYPLNFF |
| 790 | 800 | 810 | 820 | 830 | 840 |
| SPHTRWGIHS | NWRSNKFMLR | LQRGEPNIYI | SPQLAAAKGI | ADGAQVRVFN | ELSFFFAQAK |
| 850 | 860 | 870 | 880 | 890 | 900 |
| FYPSLPPDTI | MMEHGWEPHQ | FPNWRPMNVC | MATLLQPLEL | VGGWGHLNFS | LWHWNANQLA |
| HESSVDIEPA |