P9WQG3
Gene name |
fadE12 (Rv0972c, MTCY10D7.02) |
Protein name |
Acyl-CoA dehydrogenase FadE12 |
Names |
Medium chain acyl-CoA dehydrogenase, MCADH |
Species |
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) |
KEGG Pathway |
mtu:Rv0972c |
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 P9WQG3
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-P9WQG3-F1 | Predicted | AlphaFoldDB |
No variants for P9WQG3
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for P9WQG3 | |||||
No associated diseases with P9WQG3
2 GO annotations of cellular component
| Name | Definition |
|---|---|
| cytoplasm | The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures. |
| plasma membrane | The membrane surrounding a cell that separates the cell from its external environment. It consists of a phospholipid bilayer and associated proteins. |
2 GO annotations of molecular function
| Name | Definition |
|---|---|
| acyl-CoA dehydrogenase activity | Catalysis of the reaction: acyl-CoA + oxidized |
| flavin adenine dinucleotide binding | Binding to FAD, flavin-adenine dinucleotide, the coenzyme or the prosthetic group of various flavoprotein oxidoreductase enzymes, in either the oxidized form, FAD, or the reduced form, FADH2. |
1 GO annotations of biological process
| Name | Definition |
|---|---|
| fatty acid beta-oxidation using acyl-CoA dehydrogenase | A fatty acid beta-oxidation pathway in which the initial step of each oxidation cycle, which converts an acyl-CoA to a trans-2-enoyl-CoA, is catalyzed by acyl-CoA dehydrogenase; the electrons removed by oxidation pass through the respiratory chain to oxygen and leave H2O as the product. Fatty acid beta-oxidation begins with the addition of coenzyme A to a fatty acid, and ends when only two or three carbons remain (as acetyl-CoA or propionyl-CoA respectively). |
No homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| No homologous proteins | ||||
| 10 | 20 | 30 | 40 | 50 | 60 |
| MTDTSFIESE | ERQALRKAVA | SWVANYGHEY | YLDKARKHEH | TSELWAEAGK | LGFLGVNLPE |
| 70 | 80 | 90 | 100 | 110 | 120 |
| EYGGGGAGMY | ELSLVMEEMA | AAGSALLLMV | VSPAINGTII | AKFGTDDQKK | RWLPGIADGS |
| 130 | 140 | 150 | 160 | 170 | 180 |
| LTMAFAITEP | DAGSNSHKIT | TTARRDGSDW | IIKGQKVFIS | GIDQAQAVLV | VGRSEEAKTG |
| 190 | 200 | 210 | 220 | 230 | 240 |
| KLRPALFVVP | TDAPGFSYTP | IEMELVSPER | QFQVFLDDVR | LPADALVGAE | DAAIAQLFAG |
| 250 | 260 | 270 | 280 | 290 | 300 |
| LNPERIMGAA | SAVGMGRFAL | GRAVDYVKTR | KVWSTPIGAH | QGLAHPLAQC | HIEVELAKLM |
| 310 | 320 | 330 | 340 | 350 | 360 |
| TQKAATLYDH | GDDFGAAEAA | NMAKYAAAEA | SSRAVDQAVQ | SMGGNGLTKE | YGVAAMMTSA |
| 370 | 380 | ||||
| RLARIAPISR | EMVLNFVAQT | SLGLPRSY |