Q9HR74
Gene name |
dmsA (VNG_0829G) |
Protein name |
Putative dimethyl sulfoxide reductase catalytic subunit A |
Names |
DMSO reductase subunit A |
Species |
Halobacterium salinarum (strain ATCC 700922 / JCM 11081 / NRC-1) (Halobacterium halobium) |
KEGG Pathway |
hal:VNG_0829G |
EC number |
1.8.5.3: With a quinone or similar compound 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 Q9HR74
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-Q9HR74-F1 | Predicted | AlphaFoldDB |
No variants for Q9HR74
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for Q9HR74 | |||||
No associated diseases with Q9HR74
Functions
| Description | ||
|---|---|---|
| EC Number | 1.8.5.3 | With a quinone or similar compound 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 |
|---|---|
| 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 |
|---|---|
| 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 |
| MSDTDLNATR | RDVLKSGAVA | AVGLSGGGLL | STLQEADDSD | TAGDAVTSFL | GEDQVVKTAC |
| 70 | 80 | 90 | 100 | 110 | 120 |
| SPNCRGKCPL | DVFVRDGQIK | KVEQQVPAAK | TFKRGCTLGM | THLQRVYNAD | RLKYPMKRTS |
| 130 | 140 | 150 | 160 | 170 | 180 |
| WSPDDPQPDQ | RGADAQFERI | AWDDALDLVA | DGIQRAKREY | GPRSLLWHSG | SGDGGITGYR |
| 190 | 200 | 210 | 220 | 230 | 240 |
| RLKELVGGLQ | DDFTYGIDTN | VGQGFNRVTG | EGGVFMPPTN | TADDWVNAET | IIIWGSDIFA |
| 250 | 260 | 270 | 280 | 290 | 300 |
| SQFQMDAEWI | LDAKRNGAKL | VVVDPVYTNT | AEKADLWLPI | KPGKDTHLAL | AMMQYIFEHD |
| 310 | 320 | 330 | 340 | 350 | 360 |
| HYDEAFLRSR | TNAPALVRAD | DGTLLDPASV | TATPPEDGIV | VFNTETGSPE | VVPAETNGPF |
| 370 | 380 | 390 | 400 | 410 | 420 |
| ALFGEWTIDG | TTVHTGLTAL | REQASSYPPQ | AVADTAGLAA | ADIETAADWL | ATRGPGGIMP |
| 430 | 440 | 450 | 460 | 470 | 480 |
| SYGVGRYLYG | HVFGQTYATL | LALTGDYGRH | GNIHAQHPSY | DGSYLETGDW | NDPDGAAGVD |
| 490 | 500 | 510 | 520 | 530 | 540 |
| TYGYNRVLDL | LANGDPVQTK | FMYGMNSNML | GNQFPERDRW | LDAMSNLDTV | VWADIYHTPT |
| 550 | 560 | 570 | 580 | 590 | 600 |
| TRQADIILPA | AHWFETEDLL | TTYTHPNLSY | RTKAHDPLWE | ARDDYYIMAG | LAQRLGHGDK |
| 610 | 620 | 630 | 640 | 650 | 660 |
| FPDDKHDVLD | RFVKNDDRLS | WDALRETGTV | ATDETPTVAY | TDEFGTESGR | ITVYDDDAPV |
| 670 | 680 | 690 | 700 | 710 | 720 |
| EEGPALPDDG | VSLEVPKPLE | ARTADDWAHA | DEYPLLFMQK | HSKWRIHSQW | ANVPWLREIN |
| 730 | 740 | 750 | 760 | 770 | 780 |
| TEPQLDIHPK | DATRRGIDDG | EYVRVHNDRG | SVVVRAKYND | GIQPGLVNTD | QGWWARDFVD |
| 790 | 800 | 810 | 820 | 830 | |
| GHLQDLISAE | TAKVGRTFAF | YDCRVEVTRA | ADEHQSNEYT | QHNPRGSSGT | ATDGDSS |