B9KNB3
Gene name |
sucC |
Protein name |
Succinate--CoA ligase [ADP-forming] subunit beta |
Names |
Succinyl-CoA synthetase subunit beta, SCS-beta |
Species |
Cereibacter sphaeroides (strain KD131 / KCTC 12085) (Rhodobacter sphaeroides) |
KEGG Pathway |
rsk:RSKD131_2359 |
EC number |
6.2.1.5: Acid--thiol ligases |
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 B9KNB3
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-B9KNB3-F1 | Predicted | AlphaFoldDB |
No variants for B9KNB3
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for B9KNB3 | |||||
No associated diseases with B9KNB3
6 regional properties for B9KNB3
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| domain | TGS | 288 - 363 | IPR004095 |
| domain | Small GTP-binding protein domain | 62 - 213 | IPR005225 |
| domain | GTP binding domain | 64 - 166 | IPR006073 |
| conserved_site | GTP1/OBG, conserved site | 115 - 128 | IPR006074 |
| domain | OBG-type guanine nucleotide-binding (G) domain | 63 - 288 | IPR031167 |
| domain | GTP binding protein, second domain | 185 - 289 | IPR031662 |
Functions
| Description | ||
|---|---|---|
| EC Number | 6.2.1.5 | Acid--thiol ligases |
| Subcellular Localization |
|
|
| PANTHER Family | ||
| PANTHER Subfamily | ||
| PANTHER Protein Class | ||
| PANTHER Pathway Category | No pathway information available | |
1 GO annotations of cellular component
| Name | Definition |
|---|---|
| cytoplasm | The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures. |
3 GO annotations of molecular function
| Name | Definition |
|---|---|
| ATP binding | Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator. |
| magnesium ion binding | Binding to a magnesium (Mg) ion. |
| succinate-CoA ligase (ADP-forming) activity | Catalysis of the reaction: ATP + succinate + CoA = ADP + succinyl-CoA + phosphate. |
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 |
| MNIHEYQAKA | LLRSYGAPVS | DGRVVLKADE | AKSAAGELGG | PLWVVKAQIH | AGGRGKGKFK |
| 70 | 80 | 90 | 100 | 110 | 120 |
| EPEAGEKGGV | RLAKSVGEAA | ELAKQMLGRT | LVTHQTGPAG | KQVNRIYIEE | GSDIARELYL |
| 130 | 140 | 150 | 160 | 170 | 180 |
| ALLVDRGTSR | ISFVVSTEGG | MDIEEVAAST | PEKIVSFSVD | PASGLSDFHG | RRVAFALGLE |
| 190 | 200 | 210 | 220 | 230 | 240 |
| GAQVKQCVQL | VKNLYRAFVE | KDMEMLEINP | LIVMTDGNLK | VLDAKVGFDN | NALYRQSDVM |
| 250 | 260 | 270 | 280 | 290 | 300 |
| ALRDETEEDP | KELAASKFDL | NYIALDGEIG | CMVNGAGLAM | ATMDIIKLYG | AEPANFLDVG |
| 310 | 320 | 330 | 340 | 350 | 360 |
| GGATKEKVTE | AFKIITSDPN | VKGILVNIFG | GIMRCDIIAE | GIIAAVKEVG | LQVPLVVRLE |
| 370 | 380 | 390 | |||
| GTNVEKGKEI | IANSGLNVIA | GDNLSDAAQK | IVKAVKG |