P75863
Gene name |
ycbX (b0947, JW5126) |
Protein name |
Uncharacterized protein YcbX |
Names |
|
Species |
Escherichia coli (strain K12) |
KEGG Pathway |
eco:b0947 |
EC number |
|
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 P75863
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-P75863-F1 | Predicted | AlphaFoldDB |
No variants for P75863
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for P75863 | |||||
No associated diseases with P75863
4 regional properties for P75863
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| domain | 2Fe-2S ferredoxin-type iron-sulfur binding domain | 289 - 369 | IPR001041 |
| domain | Molybdenum cofactor sulfurase, C-terminal | 115 - 264 | IPR005302 |
| domain | Molybdenum cofactor sulfurase, middle domain | 1 - 116 | IPR005303 |
| binding_site | 2Fe-2S ferredoxin, iron-sulphur binding site | 323 - 331 | IPR006058 |
No GO annotations of cellular component
| Name | Definition |
|---|---|
| No GO annotations for cellular component |
4 GO annotations of molecular function
| Name | Definition |
|---|---|
| 2 iron, 2 sulfur cluster binding | Binding to a 2 iron, 2 sulfur (2Fe-2S) cluster; this cluster consists of two iron atoms, with two inorganic sulfur atoms found between the irons and acting as bridging ligands. |
| catalytic activity | Catalysis of a biochemical reaction at physiological temperatures. In biologically catalyzed reactions, the reactants are known as substrates, and the catalysts are naturally occurring macromolecular substances known as enzymes. Enzymes possess specific binding sites for substrates, and are usually composed wholly or largely of protein, but RNA that has catalytic activity (ribozyme) is often also regarded as enzymatic. |
| molybdenum ion binding | Binding to a molybdenum ion (Mo). |
| pyridoxal phosphate binding | Binding to pyridoxal 5' phosphate, 3-hydroxy-5-(hydroxymethyl)-2-methyl4-pyridine carboxaldehyde 5' phosphate, the biologically active form of vitamin B6. |
2 GO annotations of biological process
| Name | Definition |
|---|---|
| response to toxic substance | Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a toxic stimulus. |
| toxin catabolic process | The chemical reactions and pathways resulting in the breakdown of toxin, a poisonous compound (typically a protein) that is produced by cells or organisms and that can cause disease when introduced into the body or tissues of an organism. |
No homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| No homologous proteins | ||||
| 10 | 20 | 30 | 40 | 50 | 60 |
| MATLIRLFIH | PVKSMRGIGL | THALADVSGL | AFDRIFMITE | PDGTFITARQ | FPQMVRFTPS |
| 70 | 80 | 90 | 100 | 110 | 120 |
| PVHDGLHLTA | PDGSSAYVRF | ADFATQDAPT | EVWGTHFTAR | IAPDAINKWL | SGFFSREVQL |
| 130 | 140 | 150 | 160 | 170 | 180 |
| RWVGPQMTRR | VKRHNTVPLS | FADGYPYLLA | NEASLRDLQQ | RCPASVKMEQ | FRPNLVVSGA |
| 190 | 200 | 210 | 220 | 230 | 240 |
| SAWEEDRWKV | IRIGDVVFDV | VKPCSRCIFT | TVSPEKGQKH | PAGEPLKTLQ | SFRTAQDNGD |
| 250 | 260 | 270 | 280 | 290 | 300 |
| VDFGQNLIAR | NSGVIRVGDE | VEILATAPAK | IYGAAAADDT | ANITQQPDAN | VDIDWQGQAF |
| 310 | 320 | 330 | 340 | 350 | 360 |
| RGNNQQVLLE | QLENQGIRIP | YSCRAGICGS | CRVQLLEGEV | TPLKKSAMGD | DGTILCCSCV |
| PKTALKLAR |