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HAMAP rule MF_01408

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General rule information [?]

Accession MF_01408
Dates 17-OCT-2002 (Created)
31-JAN-2024 (Last updated, Version 32)
Name ThyX
Scope(s) Bacteria
Archaea
Template(s) O26061 (THYX_HELPY); Q9WYT0 (THYX_THEMA); P9WG57 (THYX_MYCTU); [ Recover all ]
Triggered by HAMAP; MF_01408 (Get profile general information and statistics)

Propagated annotation [?]

Identifier, protein and gene names [?]

Identifier THYX
Protein name RecName: Full=Flavin-dependent thymidylate synthase;
                 Short=FDTS;
                 EC=2.1.1.148;
AltName: Full=FAD-dependent thymidylate synthase;
AltName: Full=Thymidylate synthase ThyX;
                 Short=TS;
                 Short=TSase;
Gene name Name=thyX;

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 NADPH and FADH(2) as the reductant.
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;
COFACTOR Name=FAD; Xref=ChEBI:CHEBI:57692; Note=Binds 4 FAD per tetramer. Each FAD binding site is formed by three monomers.;
PATHWAYPyrimidine metabolism; dTTP biosynthesis.
SUBUNITHomotetramer.
SIMILARITYBelongs to the thymidylate synthase ThyX family.

Keywords [?]


Gene Ontology [?]

GO:0050797; Molecular function:thymidylate synthase (FAD) activity
GO:0006231; Biological process:dTMP biosynthetic process
GO:0006235; Biological process:dTTP biosynthetic process

Cross-references [?]

Pfam PF02511; Thy1; 1;
NCBIfam TIGR02170; ThyX; 1;
PROSITE PS51331; THYX; 1;

Features [?]

From: THYX_THEMA (Q9WYT0)
Key From To Description Tag Condition FTGroup
BINDING 78 80 /ligand="FAD"
/ligand_id="ChEBI:CHEBI:57692"
/ligand_note="ligand shared between neighboring subunits"
R-x-R
BINDING 163 165 /ligand="FAD"
/ligand_id="ChEBI:CHEBI:57692"
/ligand_note="ligand shared between neighboring subunits"
[ND]-x-[RHN]
BINDING 75 78 /ligand="dUMP"
/ligand_id="ChEBI:CHEBI:246422"
/ligand_note="ligand shared between dimeric partners"
[QE]-x-x-R
BINDING 86 90 /ligand="dUMP"
/ligand_id="ChEBI:CHEBI:246422"
/ligand_note="ligand shared between dimeric partners"
/note="in other chain"
[EQ]-x-S-x-R
case not <FT:4>
BINDING 88 90 /ligand="dUMP"
/ligand_id="ChEBI:CHEBI:246422"
/ligand_note="ligand shared between dimeric partners"
/note="in other chain"
S-x-R
end case
ACT_SITE 174 174 /note="Involved in ionization of N3 of dUMP, leading to its activation" R
BINDING 55 55 /ligand="FAD"
/ligand_id="ChEBI:CHEBI:57692"
/ligand_note="ligand shared between neighboring subunits"
[TS]
BINDING 86 86 /ligand="FAD"
/ligand_id="ChEBI:CHEBI:57692"
/ligand_note="ligand shared between neighboring subunits"
[EQ]
BINDING 169 169 /ligand="FAD"
/ligand_id="ChEBI:CHEBI:57692"
/ligand_note="ligand shared between neighboring subunits"
[NH]
BINDING 147 147 /ligand="dUMP"
/ligand_id="ChEBI:CHEBI:246422"
/ligand_note="ligand shared between dimeric partners"
/note="in other chain"
[RKH]
BINDING 174 174 /ligand="dUMP"
/ligand_id="ChEBI:CHEBI:246422"
/ligand_note="ligand shared between dimeric partners"
R

Additional information [?]

Size range 204-305 amino acids
Related rules None
Fusion Nter: None Cter: None
Comments Divergent AQUAE and AERPE not shown in alignment and not used in size range



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