AC   MF_00008;
DC   Protein; auto
TR   HAMAP; MF_00008; -; 1; level=0
XX
Names: Thymidy_synth_bact
XX
ID   TYSY
DE   RecName: Full=Thymidylate synthase;
DE            Short=TS;
DE            Short=TSase;
DE            EC=2.1.1.45;
GN   Name=thyA;
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 and
CC       reductant in the reaction, yielding dihydrofolate (DHF) as a by-
CC       product. This enzymatic reaction provides an intracellular de novo
CC       source of dTMP, an essential precursor for DNA biosynthesis.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + dUMP = 7,8-
CC         dihydrofolate + dTMP; Xref=Rhea:RHEA:12104, ChEBI:CHEBI:15636,
CC         ChEBI:CHEBI:57451, ChEBI:CHEBI:63528, ChEBI:CHEBI:246422;
CC         EC=2.1.1.45;
CC   -!- PATHWAY: Pyrimidine metabolism; dTTP biosynthesis.
CC   -!- SUBUNIT: Homodimer.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- SIMILARITY: Belongs to the thymidylate synthase family. Bacterial-type
CC       ThyA subfamily.
XX
DR   PROSITE; PS00091; THYMIDYLATE_SYNTHASE; 1; trigger=no
DR   Pfam; PF00303; Thymidylat_synt; 1; trigger=no
DR   PRINTS; PR00108; THYMDSNTHASE; 1; trigger=no
DR   NCBIfam; TIGR03284; thym_sym; 1; trigger=no
XX
KW   Cytoplasm
KW   Methyltransferase
KW   Nucleotide biosynthesis
KW   Transferase
XX
GO   GO:0004799; F:thymidylate synthase activity
GO   GO:0006231; P:dTMP biosynthetic process
GO   GO:0006235; P:dTTP biosynthetic process
GO   GO:0005737; C:cytoplasm
XX
FT   From: TYSY_ECOLI (P0A884)
FT   BINDING         126..127
FT                   /ligand="dUMP"
FT                   /ligand_id="ChEBI:CHEBI:246422"
FT                   /ligand_note="ligand shared between dimeric partners"
FT   Condition: R-R
FT   BINDING         166..169
FT                   /ligand="dUMP"
FT                   /ligand_id="ChEBI:CHEBI:246422"
FT                   /ligand_note="ligand shared between dimeric partners"
FT                   /note="in other chain"
FT   Condition: R-S-x-D
FT   BINDING         207..209
FT                   /ligand="dUMP"
FT                   /ligand_id="ChEBI:CHEBI:246422"
FT                   /ligand_note="ligand shared between dimeric partners"
FT                   /note="in other chain"
FT   Condition: H-x-Y
FT   ACT_SITE        146
FT                   /note="Nucleophile"
FT   Condition: C
FT   BINDING         21
FT                   /ligand="dUMP"
FT                   /ligand_id="ChEBI:CHEBI:246422"
FT                   /ligand_note="ligand shared between dimeric partners"
FT                   /note="in other chain"
FT   Optional; Condition: R
FT   BINDING         51
FT                   /ligand="(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate"
FT                   /ligand_id="ChEBI:CHEBI:15636"
FT   Optional; Condition: [HN]
FT   BINDING         169
FT                   /ligand="(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate"
FT                   /ligand_id="ChEBI:CHEBI:15636"
FT   Condition: D
FT   BINDING         177
FT                   /ligand="dUMP"
FT                   /ligand_id="ChEBI:CHEBI:246422"
FT                   /ligand_note="ligand shared between dimeric partners"
FT                   /note="in other chain"
FT   Condition: N
FT   BINDING         263
FT                   /ligand="(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate"
FT                   /ligand_id="ChEBI:CHEBI:15636"
FT   Optional; Condition: [AS]
XX
Size: 258-323;
Related: MF_01686!;
Template: P0CI79; P0A884; P00469; P9WFR9;
Scope:
 Bacteria
 Archaea; Halobacteria
Fusion:
 Nter: None
 Cter: None
Duplicate: in BACSU, BACAM, STAEQ
Plasmid: in STAAU
Comments: Duplicates in Bacillus subtilis or Bacillus amyloliquefaciens are due to
 the presence of a phage-derived TS.
 See:
 PubMed=9648749.
 Tam N.H., Borriss R.;
 "Genes encoding thymidylate synthases A and B in the genus Bacillus
 are members of two distinct families.";
 Mol. Gen. Genet. 258:427-430(1998).
 Archaeal thyA belong to a separate family (MF_01686)
XX
# Revision 1.44 2024/01/31
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