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HAMAP rule MF_00008

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General rule information [?]

Accession MF_00008
Dates 1-JUN-2001 (Created)
31-JAN-2024 (Last updated, Version 44)
Name Thymidy_synth_bact
Scope(s) Bacteria
Archaea
Halobacteria
Template(s) P0CI79 (TYSY1_BACSU); P0A884 (TYSY_ECOLI); P00469 (TYSY_LACCA); P9WFR9 (TYSY_MYCTU); [ Recover all ]
Triggered by HAMAP; MF_00008 (Get profile general information and statistics)

Propagated annotation [?]

Identifier, protein and gene names [?]

Identifier TYSY
Protein name RecName: Full=Thymidylate synthase;
                 Short=TS;
                 Short=TSase;
                 EC=2.1.1.45;
Gene name Name=thyA;

Comments [?]

FUNCTIONCatalyzes 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 reductant in the reaction, yielding dihydrofolate (DHF) as a by- product. This enzymatic reaction provides an intracellular de novo source of dTMP, an essential precursor for DNA biosynthesis.
CATALYTIC ACTIVITY Reaction=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + dUMP = 7,8- dihydrofolate + dTMP; Xref=Rhea:RHEA:12104, ChEBI:CHEBI:15636, ChEBI:CHEBI:57451, ChEBI:CHEBI:63528, ChEBI:CHEBI:246422; EC=2.1.1.45;
PATHWAYPyrimidine metabolism; dTTP biosynthesis.
SUBUNITHomodimer.
SUBCELLULAR LOCATIONCytoplasm.
SIMILARITYBelongs to the thymidylate synthase family. Bacterial-type ThyA subfamily.

Keywords [?]


Gene Ontology [?]

GO:0004799; Molecular function:thymidylate synthase activity
GO:0006231; Biological process:dTMP biosynthetic process
GO:0006235; Biological process:dTTP biosynthetic process
GO:0005737; Cellular component:cytoplasm

Cross-references [?]

PROSITE PS00091; THYMIDYLATE_SYNTHASE; 1;
Pfam PF00303; Thymidylat_synt; 1;
PRINTS PR00108; THYMDSNTHASE; 1;
NCBIfam TIGR03284; thym_sym; 1;

Features [?]

From: TYSY_ECOLI (P0A884)
Key From To Description Tag Condition FTGroup
BINDING 126 127 /ligand="dUMP"
/ligand_id="ChEBI:CHEBI:246422"
/ligand_note="ligand shared between dimeric partners"
R-R
BINDING 166 169 /ligand="dUMP"
/ligand_id="ChEBI:CHEBI:246422"
/ligand_note="ligand shared between dimeric partners"
/note="in other chain"
R-S-x-D
BINDING 207 209 /ligand="dUMP"
/ligand_id="ChEBI:CHEBI:246422"
/ligand_note="ligand shared between dimeric partners"
/note="in other chain"
H-x-Y
ACT_SITE 146 146 /note="Nucleophile" C
BINDING 21 21 /ligand="dUMP"
/ligand_id="ChEBI:CHEBI:246422"
/ligand_note="ligand shared between dimeric partners"
/note="in other chain"
R
BINDING 51 51 /ligand="(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate"
/ligand_id="ChEBI:CHEBI:15636"
[HN]
BINDING 169 169 /ligand="(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate"
/ligand_id="ChEBI:CHEBI:15636"
D
BINDING 177 177 /ligand="dUMP"
/ligand_id="ChEBI:CHEBI:246422"
/ligand_note="ligand shared between dimeric partners"
/note="in other chain"
N
BINDING 263 263 /ligand="(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate"
/ligand_id="ChEBI:CHEBI:15636"
[AS]

Additional information [?]

Size range 258-323 amino acids
Related rules MF_01686
Fusion Nter: None Cter: None
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)



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