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UniProt functional annotation for Q9WYT0 | ||
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| UniProt code: Q9WYT0. |
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| Organism: | |
Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8). |
| Taxonomy: | |
Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. |
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| Function: | |
Catalyzes the reductive methylation of 2'-deoxyuridine-5'- monophosphate (dUMP) to 2'-deoxythymidine-5'-monophosphate (dTMP) while utilizing 5,10-methylenetetrahydrofolate (mTHF) as the methyl donor, and NAD(P)H and FADH(2) as the reductant. {ECO:0000269|PubMed:12791256, ECO:0000269|PubMed:19370033}. |
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| Catalytic activity: | |
Reaction=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + dUMP + H(+) + NADPH = (6S)-5,6,7,8-tetrahydrofolate + dTMP + NADP(+); Xref=Rhea:RHEA:29043, ChEBI:CHEBI:15378, ChEBI:CHEBI:15636, ChEBI:CHEBI:57453, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:63528, ChEBI:CHEBI:246422; EC=2.1.1.148; Evidence={ECO:0000269|PubMed:12791256, ECO:0000269|PubMed:19370033}; |
| Cofactor: | |
Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000269|PubMed:12791256, ECO:0000305|PubMed:12211025}; Note=Binds 4 FAD per tetramer. Each FAD binding site is formed by three monomers. {ECO:0000269|PubMed:12211025, ECO:0000269|PubMed:12791256}; |
| Biophysicochemical properties: | |
Kinetic parameters: KM=30 uM for dUMP (at 65 degrees Celsius) {ECO:0000269|PubMed:19370033}; Note=kcat is 1.2 sec(-1) (at 65 degrees Celsius). {ECO:0000269|PubMed:19370033}; |
| Pathway: | |
Pyrimidine metabolism; dTTP biosynthesis. {ECO:0000255|HAMAP- Rule:MF_01408}. |
| Subunit: | |
Homotetramer. {ECO:0000269|PubMed:12211025, ECO:0000269|PubMed:12791256, ECO:0000269|PubMed:24563811}. |
| Miscellaneous: | |
Reaction mechanism involved a direct methylene transfer from mTHF to dUMP (PubMed:23019356). FDTS ionizes N3 of dUMP using the active-site Arg-174, providing a new mechanism for dUMP activation. The phosphate of dUMP is crucial for flavin oxidation, suggesting that it acts as the base that deprotonates C5 of the dUMP-methylene adduct (PubMed:27214228). {ECO:0000269|PubMed:23019356, ECO:0000269|PubMed:27214228}. |
| Similarity: | |
Belongs to the thymidylate synthase ThyX family. {ECO:0000255|HAMAP-Rule:MF_01408}. |
Annotations taken from UniProtKB at the EBI.