O81395
Gene name |
DRTS |
Protein name |
Bifunctional dihydrofolate reductase-thymidylate synthase |
Names |
DHFR-TS |
Species |
Zea mays (Maize) |
KEGG Pathway |
zma:541707 |
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 O81395
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-O81395-F1 | Predicted | AlphaFoldDB |
No variants for O81395
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for O81395 | |||||
No associated diseases with O81395
4 regional properties for O81395
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| domain | Dihydrofolate reductase domain | 17 - 194 | IPR001796 |
| conserved_site | Dihydrofolate reductase conserved site | 29 - 51 | IPR017925 |
| active_site | Thymidylate synthase, active site | 383 - 411 | IPR020940 |
| domain | Thymidylate synthase/dCMP hydroxymethylase domain | 240 - 521 | 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 | |
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. |
| 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. |
5 homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| O76511 | Ts | Thymidylate synthase | Drosophila melanogaster (Fruit fly) | PR |
| P04818 | TYMS | Thymidylate synthase | Homo sapiens (Human) | PR |
| P07607 | Tyms | Thymidylate synthase | Mus musculus (Mouse) | PR |
| P45352 | Tyms | Thymidylate synthase | Rattus norvegicus (Rat) | PR |
| Q05763 | THY-2 | Bifunctional dihydrofolate reductase-thymidylate synthase 2 | Arabidopsis thaliana (Mouse-ear cress) | PR |
| 10 | 20 | 30 | 40 | 50 | 60 |
| MAAVLANGDS | QGRPQRNYQV | VVAGTRDMGI | GKDGVLPWKL | PGDLKFFKEL | TLTTSDPVKK |
| 70 | 80 | 90 | 100 | 110 | 120 |
| NAVIMGRKTW | ESIPVKSRPL | PGRLNVILTR | SGSFDFATVE | NVVICGSMES | ALELLASTPY |
| 130 | 140 | 150 | 160 | 170 | 180 |
| CLSIEKVFVI | GGGQVLREYL | KGPACEAIHL | TDIQSSIECD | TFIPPVDFSV | FQPWYSSFPV |
| 190 | 200 | 210 | 220 | 230 | 240 |
| IESNIRHSFV | SFVRVRKSVA | ETHESNGKES | TEVDTKNDKF | ETENFSFLPK | MVYDRHEEYQ |
| 250 | 260 | 270 | 280 | 290 | 300 |
| YLNLVEDIIR | SGAQKNDRTG | TGTLSKFGCQ | MRFNLRKNFP | LLTTKRVFWR | GVVEELLWFI |
| 310 | 320 | 330 | 340 | 350 | 360 |
| SGSTNAKVLQ | EKGIHIWDGN | ASREYLNSVG | LAHREEGDLG | PIYGFQWRHF | GAEYTDMHAD |
| 370 | 380 | 390 | 400 | 410 | 420 |
| YTGKGFDQLM | DVIDKIKNDP | EDRRIILSAW | NPSDLKKMAL | PPCHMFAQFY | VENGELSCQM |
| 430 | 440 | 450 | 460 | 470 | 480 |
| YQRSADMGLG | VPFNIASYSL | LTYMIAQVCD | LSPGDFVHVI | GDAHVYRNHV | RALEEQIQKM |
| 490 | 500 | 510 | 520 | ||
| PKPFPILKIN | PSKKDIDSFM | ASDFKLVGYD | PHQKIEMKMA | V |