AC PRU00661; DC Domain; TR PROSITE; PS51331; THYX; 1; level=0 XX Names: Flavin-dependent thymidylate synthase (thyX) domain Function: The thyx domain contains FAD and methylates dUMP at position 5 of the pyrimidine ring. XX case not DE AltName: Full=Probable thymidylate synthase; DE Short=TS; DE Short=TSase; DE EC=2.1.1.148; end case XX CC -!- FUNCTION: Catalyzes the reductive methylation of 2'-deoxyuridine-5'- CC monophosphate (dUMP) to 2'-deoxythymidine-5'-monophosphate (dTMP) while CC utilizing 5,10-methylenetetrahydrofolate (mTHF) as the methyl donor, CC and NADPH and FADH(2) as the reductant. CC -!- CATALYTIC ACTIVITY: CC Reaction=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + dUMP + H(+) + CC NADPH = (6S)-5,6,7,8-tetrahydrofolate + dTMP + NADP(+); CC Xref=Rhea:RHEA:29043, ChEBI:CHEBI:15378, ChEBI:CHEBI:15636, CC ChEBI:CHEBI:57453, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, CC ChEBI:CHEBI:63528, ChEBI:CHEBI:246422; EC=2.1.1.148; CC -!- COFACTOR: CC Name=FAD; Xref=ChEBI:CHEBI:57692; synthase) domain XX GO GO:0008168; F:methyltransferase activity GO GO:0016740; F:transferase activity GO GO:0050797; F:thymidylate synthase (FAD) activity GO GO:0006231; P:dTMP biosynthetic process GO GO:0050660; F:flavin adenine dinucleotide binding XX KW FAD KW Flavoprotein KW Methyltransferase KW Nucleotide biosynthesis KW Transferase XX FT From: PS51331 FT DOMAIN from..to FT /note="ThyX #" FT MOTIF 80..90 FT /note="ThyX motif #" FT Condition: R-H-R-x(7,8)-S XX Chop: Nter=0; Cter=0; Size: 183-266; Related: None; Repeats: 1-2; Topology: Undefined; Example: O86840; Scope: Bacteria Archaea Viruses Eukaryota; Dictyostelium Comments: None; XX # Revision 1.14 2019/11/21 //