P07382
Gene name |
LmjF06.0860 (LmjF_06_0860) |
Protein name |
Bifunctional dihydrofolate reductase-thymidylate synthase |
Names |
DHFR-TS |
Species |
Leishmania major |
KEGG Pathway |
lma:LMJF_06_0860 |
EC number |
1.5.1.3: With NAD(+) or NADP(+) 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 P07382
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-P07382-F1 | Predicted | AlphaFoldDB |
No variants for P07382
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for P07382 | |||||
No associated diseases with P07382
4 regional properties for P07382
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| domain | Dihydrofolate reductase domain | 26 - 229 | IPR001796 |
| conserved_site | Dihydrofolate reductase conserved site | 38 - 60 | IPR017925 |
| active_site | Thymidylate synthase, active site | 380 - 408 | IPR020940 |
| domain | Thymidylate synthase/dCMP hydroxymethylase domain | 236 - 520 | IPR023451 |
Functions
| Description | ||
|---|---|---|
| EC Number | 1.5.1.3 | With NAD(+) or NADP(+) as acceptor |
| Subcellular Localization |
|
|
| PANTHER Family | ||
| PANTHER Subfamily | ||
| PANTHER Protein Class | ||
| PANTHER Pathway Category | No pathway information available | |
3 GO annotations of cellular component
| Name | Definition |
|---|---|
| cytoplasm | The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures. |
| cytosol | The part of the cytoplasm that does not contain organelles but which does contain other particulate matter, such as protein complexes. |
| mitochondrion | A semiautonomous, self replicating organelle that occurs in varying numbers, shapes, and sizes in the cytoplasm of virtually all eukaryotic cells. It is notably the site of tissue respiration. |
2 GO annotations of molecular function
| Name | Definition |
|---|---|
| dihydrofolate reductase activity | Catalysis of the reaction: 5,6,7,8-tetrahydrofolate + NADP+ = 7,8-dihydrofolate + NADPH + H+. |
| thymidylate synthase activity | Catalysis of the reaction: 5,10-methylenetetrahydrofolate + dUMP = 7,8-dihydrofolate + thymidylate. |
4 GO annotations of biological process
| Name | Definition |
|---|---|
| dTMP biosynthetic process | The chemical reactions and pathways resulting in the formation of dTMP, deoxyribosylthymine monophosphate (2'-deoxyribosylthymine 5'-phosphate). |
| methylation | The process in which a methyl group is covalently attached to a molecule. |
| one-carbon metabolic process | The chemical reactions and pathways involving the transfer of one-carbon units in various oxidation states. |
| tetrahydrofolate biosynthetic process | The chemical reactions and pathways resulting in the formation of tetrahydrofolate, 5,6,7,8-tetrahydrofolic acid, a folate derivative bearing additional hydrogens on the pterin group. |
No homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| No homologous proteins | ||||
| 10 | 20 | 30 | 40 | 50 | 60 |
| MSRAAARFKI | PMPETKADFA | FPSLRAFSIV | VALDMQHGIG | DGESIPWRVP | EDMTFFKNQT |
| 70 | 80 | 90 | 100 | 110 | 120 |
| TLLRNKKPPT | EKKRNAVVMG | RKTWESVPVK | FRPLKGRLNI | VLSSKATVEE | LLAPLPEGQR |
| 130 | 140 | 150 | 160 | 170 | 180 |
| AAAAQDVVVV | NGGLAEALRL | LARPLYCSSI | ETAYCVGGAQ | VYADAMLSPC | IEKLQEVYLT |
| 190 | 200 | 210 | 220 | 230 | 240 |
| RIYATAPACT | RFFPFPPENA | ATAWDLASSQ | GRRKSEAEGL | EFEICKYVPR | NHEERQYLEL |
| 250 | 260 | 270 | 280 | 290 | 300 |
| IDRIMKTGIV | KEDRTGVGTI | SLFGAQMRFS | LRDNRLPLLT | TKRVFWRGVC | EELLWFLRGE |
| 310 | 320 | 330 | 340 | 350 | 360 |
| TSAQLLADKD | IHIWDGNGSR | EFLDSRGLTE | NKEMDLGPVY | GFQWRHFGAD | YKGFEANYDG |
| 370 | 380 | 390 | 400 | 410 | 420 |
| EGVDQIKLIV | ETIKTNPNDR | RLLVTAWNPC | ALQKMALPPC | HLLAQFYVNT | DTSELSCMLY |
| 430 | 440 | 450 | 460 | 470 | 480 |
| QRSCDMGLGV | PFNIASYALL | TILIAKATGL | RPGELVHTLG | DAHVYRNHVD | ALKAQLERVP |
| 490 | 500 | 510 | |||
| HAFPTLIFKE | ERQYLEDYEL | TDMEVIDYVP | HPAIKMEMAV |