FolB

Dihydroneopterin aldolase
FolB
SMART accession number:SM00905
Description: Dihydroneopterin aldolase catalyses the conversion of 7,8-dihydroneopterin to 6-hydroxymethyl-7,8-dihydropterin in the biosynthetic pathway of tetrahydrofolate. In the opportunistic pathogen Pneumocystis carinii, dihydroneopterin aldolase function is expressed as the N-terminal portion of the multifunctional folic acid synthesis protein (Fas). This region encompasses two domains, FasA and FasB, which are 27% amino acid identical. FasA and FasB also share significant amino acid sequence similarity with bacterial dihydroneopterin aldolases. This region consists of two tandem sequences each homologous to folB and which form tetramers (PUBMED:9709001).
Interpro abstract (IPR006157):

Dihydroneopterin aldolase catalyses the conversion of 7,8-dihydroneopterin to 6-hydroxymethyl-7,8-dihydropterin in the biosynthetic pathway of tetrahydrofolate. In the opportunistic pathogen Pneumocystis carinii, dihydroneopterin aldolase function is expressed as the N-terminal portion of the multifunctional folic acid synthesis protein (Fas). This region encompasses two domains, FasA and FasB, which are 27% amino acid identical. FasA and FasB also share significant amino acid sequence similarity with bacterial dihydroneopterin aldolases.

This region consists of two tandem sequences each homologous to folB and which form tetramers [(PUBMED:9709001)].

GO process:folic acid-containing compound metabolic process (GO:0006760)
GO function:dihydroneopterin aldolase activity (GO:0004150)
Family alignment:
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There are 1454 FolB domains in 1423 proteins in SMART's nrdb database.

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