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9CAUD:A0A0K2D0F3
Contents
| Species (Taxon ID) | Bacillus phage TsarBomba. (1690456) | |
| Gene Name(s) | No Information Provided. | |
| Protein Name(s) | ThyX (ECO:0000313 with EMBL:ALA13147.1) | |
| External Links | ||
| UniProt | A0A0K2D0F3 | |
| EMBL | KT224359 | |
| RefSeq | YP_009206866.1 | |
| GeneID | 26633357 | |
| GO | GO:0004799 GO:0006231 | |
| Gene3D | 3.30.572.10 | |
| HAMAP | MF_00008 | |
| InterPro | IPR023451 IPR000398 IPR020940 | |
| Pfam | PF00303 | |
| PRINTS | PR00108 | |
| SUPFAM | SSF55831 | |
| TIGRFAMs | TIGR03284 | |
| PROSITE | PS00091 | |
Annotations
| Qualifier | GO ID | GO term name | Reference | ECO ID | ECO term name | with/from | Aspect | Extension | Notes | Status |
|---|---|---|---|---|---|---|---|---|---|---|
| GO:0004799 |
thymidylate synthase activity |
ECO:0000250 |
|
F |
"The R166Q mutant was crystallized in the presence of dUMP and a structure determined to 2.9 A resolution, but neither the ligand nor the sulfate from the crystallization buffer was found in the active site." meaning that this protein has a TS sight and if this site was mutated from a R to a Q at the 166 peptide, the site was inactive. This has a similar sequence from the TS in E.coli. |
complete | ||||
| GO:0032259 |
methylation |
ECO:0000315 |
P |
Figure 1 showed that ThyX proteins also act as NADPH oxidase by reacting directly with O2. |
complete | |||||
| GO:0006231 |
dTMP biosynthetic process |
ECO:0000314 |
P |
Thymidylate synthase catalyzes the reductive methylation of dUMP to dTMP with concomitant conversion of 5,10-methylenetetrahydrofolate to dihydrofolate: 5,10-methylenetetrahydrofolate + dUMP = dihydrofolate + dTMP This provides the sole de novo pathway for production of dTMP and is the only enzyme in folate metabolism in which the 5,10-methylenetetrahydrofolate is oxidised during one-carbon transfer. |
complete | |||||
|
involved_in |
GO:0032259 |
methylation |
ECO:0000366 |
evidence based on logical inference from automatic annotation used in automatic assertion |
GO:0004799 |
P |
Seeded From UniProt |
complete | ||
|
enables |
GO:0004799 |
thymidylate synthase activity |
ECO:0000256 |
match to sequence model evidence used in automatic assertion |
F |
Seeded From UniProt |
complete | |||
|
involved_in |
GO:0006231 |
dTMP biosynthetic process |
ECO:0000256 |
match to sequence model evidence used in automatic assertion |
P |
Seeded From UniProt |
complete | |||
Notes
References
See Help:References for how to manage references in GONUTS.
- ↑ Sotelo-Mundo, RR et al. (2006) Crystal structures of thymidylate synthase mutant R166Q: structural basis for the nearly complete loss of catalytic activity. J. Biochem. Mol. Toxicol. 20 88-92 PubMed GONUTS page
- ↑ Becker, HF et al. (2014) Substrate interaction dynamics and oxygen control in the active site of thymidylate synthase ThyX. Biochem. J. 459 37-45 PubMed GONUTS page
- ↑ Benkovic, SJ (1980) On the mechanism of action of folate- and biopterin-requiring enzymes. Annu. Rev. Biochem. 49 227-51 PubMed GONUTS page
