P16263
Gene name |
odhB (citM, BSU19360) |
Protein name |
Dihydrolipoyllysine-residue succinyltransferase component of 2-oxoglutarate dehydrogenase complex |
Names |
2-oxoglutarate dehydrogenase complex component E2, OGDC-E2, Dihydrolipoamide succinyltransferase component of 2-oxoglutarate dehydrogenase complex |
Species |
Bacillus subtilis (strain 168) |
KEGG Pathway |
bsu:BSU19360 |
EC number |
2.3.1.61: Transferring groups other than amino-acyl groups |
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 P16263
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-P16263-F1 | Predicted | AlphaFoldDB |
No variants for P16263
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for P16263 | |||||
No associated diseases with P16263
4 regional properties for P16263
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| domain | Biotin/lipoyl attachment | 1 - 76 | IPR000089 |
| domain | 2-oxoacid dehydrogenase acyltransferase, catalytic domain | 187 - 415 | IPR001078 |
| binding_site | 2-oxo acid dehydrogenase, lipoyl-binding site | 26 - 55 | IPR003016 |
| domain | Peripheral subunit-binding domain | 123 - 160 | IPR004167 |
Functions
| Description | ||
|---|---|---|
| EC Number | 2.3.1.61 | Transferring groups other than amino-acyl groups |
| Subcellular Localization |
|
|
| PANTHER Family | ||
| PANTHER Subfamily | ||
| PANTHER Protein Class | ||
| PANTHER Pathway Category | No pathway information available | |
2 GO annotations of cellular component
| Name | Definition |
|---|---|
| cytosol | The part of the cytoplasm that does not contain organelles but which does contain other particulate matter, such as protein complexes. |
| oxoglutarate dehydrogenase complex | A complex of multiple copies of three enzymatic components: oxoglutarate dehydrogenase (lipoamide) (E1), dihydrolipoamide S-succinyltransferase (E2) and dihydrolipoamide dehydrogenase (E3); catalyzes the overall conversion of 2-oxoglutarate to succinyl-CoA and carbon dioxide (CO2). |
1 GO annotations of molecular function
| Name | Definition |
|---|---|
| dihydrolipoyllysine-residue succinyltransferase activity | Catalysis of the reaction: succinyl-CoA + dihydrolipoamide = CoA + S-succinyldihydrolipoamide. |
2 GO annotations of biological process
| Name | Definition |
|---|---|
| L-lysine catabolic process to acetyl-CoA via saccharopine | The chemical reactions and pathways resulting in the breakdown of L-lysine into other compounds, including acetyl-CoA, via the intermediate saccharopine. |
| 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 |
| MAEIKVPELA | ESISEGTIAQ | WLKQPGDYVE | QGEYLLELET | DKVNVELTAE | ESGVLQEVLK |
| 70 | 80 | 90 | 100 | 110 | 120 |
| DSGDTVQVGE | IIGTISEGAG | ESSAPAPTEK | TESKESVKEE | KQAEPAAQEV | SEEAQSEAKS |
| 130 | 140 | 150 | 160 | 170 | 180 |
| RTIASPSARK | LAREKGIDLS | QVPTGDPLGR | VRKQDVEAYE | KPASKPAPQQ | KQQPQAQKAQ |
| 190 | 200 | 210 | 220 | 230 | 240 |
| QSFDKPVEVQ | KMSRRRQTIA | KRLVEVQQTS | AMLTTFNEVD | MTAVMNLRKR | RKDQFFEQNE |
| 250 | 260 | 270 | 280 | 290 | 300 |
| VKLGFMSFFT | KAVVAALKKY | PLLNAEIQGD | ELIVKKFYDI | GIAVAADEGL | VVPVVRDADR |
| 310 | 320 | 330 | 340 | 350 | 360 |
| LTFAGIEKEI | GELAKKARNN | KLTLSELQGG | SFTITNGGTF | GSLMSTPILN | SPQVGILGMH |
| 370 | 380 | 390 | 400 | 410 | |
| KIQLRPVAID | EERFENRPMM | YIALSYDHRI | VDGKEAVGFL | VTIKNLLEDP | EQLLLEG |