B7JSX2
Gene name |
mqo |
Protein name |
Probable malate:quinone oxidoreductase |
Names |
MQO, Malate dehydrogenase [quinone] |
Species |
Bacillus cereus (strain AH820) |
KEGG Pathway |
bcu:BCAH820_2970 |
EC number |
1.1.5.4: 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 B7JSX2
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-B7JSX2-F1 | Predicted | AlphaFoldDB |
No variants for B7JSX2
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for B7JSX2 | |||||
No associated diseases with B7JSX2
No regional properties for B7JSX2
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| No domain, repeats, and functional sites for B7JSX2 | |||
Functions
| Description | ||
|---|---|---|
| EC Number | 1.1.5.4 | With a quinone or similar compound as acceptor |
| Subcellular Localization |
|
|
| PANTHER Family | ||
| PANTHER Subfamily | ||
| PANTHER Protein Class | ||
| PANTHER Pathway Category | No pathway information available | |
No GO annotations of cellular component
| Name | Definition |
|---|---|
| No GO annotations for cellular component |
2 GO annotations of molecular function
| Name | Definition |
|---|---|
| malate dehydrogenase (menaquinone) activity | Catalysis of the reaction: (S)-malate + a menaquinone = oxaloacetate + a menaquinol. |
| malate dehydrogenase (quinone) activity | Catalysis of the reaction: (S)-malate + a quinone = oxaloacetate + a quinol. |
1 GO annotations of biological process
| Name | Definition |
|---|---|
| tricarboxylic acid cycle | A nearly universal metabolic pathway in which the acetyl group of acetyl coenzyme A is effectively oxidized to two CO2 and four pairs of electrons are transferred to coenzymes. The acetyl group combines with oxaloacetate to form citrate, which undergoes successive transformations to isocitrate, 2-oxoglutarate, succinyl-CoA, succinate, fumarate, malate, and oxaloacetate again, thus completing the cycle. In eukaryotes the tricarboxylic acid is confined to the mitochondria. See also glyoxylate cycle. |
No homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| No homologous proteins | ||||
| 10 | 20 | 30 | 40 | 50 | 60 |
| MSNMQQKTDV | ILIGAGIMSA | TLGSLLKELA | PEWEIKVFEK | LASAGEESSN | EWNNAGTGHS |
| 70 | 80 | 90 | 100 | 110 | 120 |
| ALCELNYTSE | KSDGSIDISK | AVKVNEQFQL | SRQFWAYLVK | SKLIRNPQDF | IMPLPHMSLV |
| 130 | 140 | 150 | 160 | 170 | 180 |
| QGEKNVEFLK | NRFEALSKNP | LFQGMEFSDA | PETLKKWLPL | IMEGRTSNEP | MAATKIDSGT |
| 190 | 200 | 210 | 220 | 230 | 240 |
| DVNFGALTRM | LFDYLKTKDV | ELNYKHSVEN | IKRTKNGLWE | VKVHDMNSGK | IEHHTAKFVF |
| 250 | 260 | 270 | 280 | 290 | 300 |
| IGGGGGSLPL | LQKTGIPESK | HIGGFPVSGL | FMVCKNQKVV | EQHHAKVYGK | AKVGAPPMSV |
| 310 | 320 | 330 | 340 | 350 | 360 |
| PHLDTRYIDN | KKALLFGPFA | GFSPKFLKTG | SNLDLIGSVK | PNNVLTMLAA | GVKEMGLTKY |
| 370 | 380 | 390 | 400 | 410 | 420 |
| LIQQVMLSHE | KRMEELREFI | PNAKSEDWDI | VVAGQRVQVI | KDTDAGGKGT | LQFGTEVVSA |
| 430 | 440 | 450 | 460 | 470 | 480 |
| ADGSIAALLG | ASPGASTAVH | VMLEVLEKCF | PSRMVEWEGK | IKEMIPSYGI | SLTENPRLFQ |
| 490 | |||||
| DLHTSTGRTL | GLNEKETVHN |