AC   MF_01408;
DC   Protein; auto
TR   HAMAP; MF_01408; -; 1; level=0
XX
Names: ThyX
XX
ID   THYX
DE   RecName: Full=Flavin-dependent thymidylate synthase;
DE            Short=FDTS;
DE            EC=2.1.1.148;
DE   AltName: Full=FAD-dependent thymidylate synthase;
DE   AltName: Full=Thymidylate synthase ThyX;
DE            Short=TS;
DE            Short=TSase;
GN   Name=thyX;
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;
CC       Note=Binds 4 FAD per tetramer. Each FAD binding site is formed by three
CC       monomers.;
CC   -!- PATHWAY: Pyrimidine metabolism; dTTP biosynthesis.
CC   -!- SUBUNIT: Homotetramer.
CC   -!- SIMILARITY: Belongs to the thymidylate synthase ThyX family.
XX
DR   Pfam; PF02511; Thy1; 1; trigger=no
DR   NCBIfam; TIGR02170; ThyX; 1; trigger=no
DR   PROSITE; PS51331; THYX; 1; trigger=yes
XX
KW   Transferase
KW   Methyltransferase
KW   Nucleotide biosynthesis
KW   FAD
KW   Flavoprotein
KW   NADP
XX
GO   GO:0050797; F:thymidylate synthase (FAD) activity
GO   GO:0006231; P:dTMP biosynthetic process
GO   GO:0006235; P:dTTP biosynthetic process
XX
FT   From: THYX_THEMA (Q9WYT0)
FT   BINDING         78..80
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /ligand_note="ligand shared between neighboring
FT                   subunits"
FT   Condition: R-x-R
FT   BINDING         163..165
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /ligand_note="ligand shared between neighboring
FT                   subunits"
FT   Condition: [ND]-x-[RHN]
FT   BINDING         75..78
FT                   /ligand="dUMP"
FT                   /ligand_id="ChEBI:CHEBI:246422"
FT                   /ligand_note="ligand shared between dimeric partners"
FT   Optional; Condition: [QE]-x-x-R
FT   BINDING         86..90
FT                   /ligand="dUMP"
FT                   /ligand_id="ChEBI:CHEBI:246422"
FT                   /ligand_note="ligand shared between dimeric partners"
FT                   /note="in other chain"
FT   Condition: [EQ]-x-S-x-R
case not <FT:4>
FT   BINDING         88..90
FT                   /ligand="dUMP"
FT                   /ligand_id="ChEBI:CHEBI:246422"
FT                   /ligand_note="ligand shared between dimeric partners"
FT                   /note="in other chain"
FT   Condition: S-x-R
end case
FT   ACT_SITE        174
FT                   /note="Involved in ionization of N3 of dUMP, leading to its
FT                   activation"
FT   Condition: R
FT   BINDING         55
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /ligand_note="ligand shared between neighboring
FT                   subunits"
FT   Optional; Condition: [TS]
FT   BINDING         86
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /ligand_note="ligand shared between neighboring
FT                   subunits"
FT   Optional; Condition: [EQ]
FT   BINDING         169
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /ligand_note="ligand shared between neighboring
FT                   subunits"
FT   Optional; Condition: [NH]
FT   BINDING         147
FT                   /ligand="dUMP"
FT                   /ligand_id="ChEBI:CHEBI:246422"
FT                   /ligand_note="ligand shared between dimeric partners"
FT                   /note="in other chain"
FT   Condition: [RKH]
FT   BINDING         174
FT                   /ligand="dUMP"
FT                   /ligand_id="ChEBI:CHEBI:246422"
FT                   /ligand_note="ligand shared between dimeric partners"
FT   Condition: R
XX
Size: 204-305;
Related: None;
Template: O26061; Q9WYT0; P9WG57;
Scope:
 Bacteria
 Archaea
Fusion:
 Nter: None
 Cter: None
Duplicate: None
Plasmid: in BORBU
Comments: Divergent AQUAE and AERPE not shown in alignment and not used in size range
XX
# Revision 1.32 2024/01/31
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