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Protein Domain : IPR020628

Name  Formate-tetrahydrofolate ligase, FTHFS, conserved site Short Name  Formate_THF_ligase_CS
Type  Conserved_site Description  Formate--tetrahydrofolate ligase () (formyltetrahydrofolate synthetase) (FTHFS) is one of the enzymesparticipating in the transfer of one-carbon units, an essential element of various biosynthetic pathways. In many of these processes the transfers of one-carbon units are mediated by the coenzyme tetrahydrofolate (THF). In eukaryotes the FTHFS activity is expressed by a multifunctional enzyme, C-1-tetrahydrofolate synthase (C1-THF synthase), which also catalyses the dehydrogenase and cyclohydrolase activities. Two forms of C1-THF synthases are known [], one is located in the mitochondrial matrix, while the second one is cytoplasmic. In both forms the FTHFS domainconsists of about 600 amino acid residues and is located in the C-terminal section of C1-THF synthase. In prokaryotes FTHFS activity is expressed by a monofunctional homotetrameric enzyme of about 560 amino acid residues [].The crystal structure of N(10)-formyltetrahydrofolate synthetase from Moorella thermoaceticashows that the subunit is composed of three domains organised around three mixed beta-sheets. There are two cavities between adjacent domains. One of them was identified as the nucleotide binding site by homology modelling. The large domain contains a seven-stranded beta-sheet surrounded by helices on both sides. The second domain contains a five-stranded beta-sheet with two alpha-helices packed on one side while the other two are a wall of the active site cavity. The third domain contains a four-stranded beta-sheet forming a half-barrel. The concave side is covered bytwo helices while the convex side is another wall of the large cavity. Arg 97 is likely involved in formyl phosphate binding. The tetrameric molecule is relatively flat with the shape of the letter X, and the active sites are located at the end of the subunits far from the subunit interface [].These signature patterns cover two regions that are almost perfectly conserved. The first one is a glycine-rich segment located in the N-terminal part of FTHFS and which could be part of an ATP-binding domain []. The second pattern is located in the central section of FTHFS.

Publication Counts Displayer

0 Child Features

0 Contains

2 Cross References

Identifier
Source . Name

Subject . Primary Identifier
PS00721 PROSITE IPR020628
PS00722 PROSITE IPR020628

3 Data Sets

Name URL
TrEMBL data set http://www.ebi.ac.uk/trembl/
InterPro data set  
InterPro GO Annotation data set  

1 Found In

DB identifier Name Short Name Type
IPR000559 Formate-tetrahydrofolate ligase, FTHFS Formate_THF_ligase Family

3 GO Annotation


Subject . Secondary Identifier

Subject . Name

Subject . Symbol

Ontology Term . Identifier

Ontology Term . Name
Formate-tetrahydrofolate ligase, FTHFS, conserved site   GO:0004329 formate-tetrahydrofolate ligase activity
Formate-tetrahydrofolate ligase, FTHFS, conserved site   GO:0005524 ATP binding
Formate-tetrahydrofolate ligase, FTHFS, conserved site   GO:0009396 folic acid-containing compound biosynthetic process

3 Ontology Annotations


Subject . Secondary Identifier

Subject . Name

Subject . Symbol

Ontology Term . Identifier

Ontology Term . Name
Formate-tetrahydrofolate ligase, FTHFS, conserved site   GO:0004329 formate-tetrahydrofolate ligase activity
Formate-tetrahydrofolate ligase, FTHFS, conserved site   GO:0005524 ATP binding
Formate-tetrahydrofolate ligase, FTHFS, conserved site   GO:0009396 folic acid-containing compound biosynthetic process

0 Parent Features

11 Proteins

DB identifier Primary Accession
Organism . Name
FBpp0099494 O96553 Drosophila melanogaster
FBpp0281021 Q293Q3 Drosophila pseudoobscura
FBpp0172911 B4KD13 Drosophila mojavensis
FBpp0237670 B4LZJ8 Drosophila virilis
FBpp0271053 B4PKR2 Drosophila yakuba
B6IKC9_CAEBR B6IKC9 Caenorhabditis briggsae
H2WJ24_CAEJA H2WJ24 Caenorhabditis japonica
G0MW71_CAEBE G0MW71 Caenorhabditis brenneri
Q21284_CAEEL Q21284 Caenorhabditis elegans
C1TC_DROME-2 O96553-2 Drosophila melanogaster
E3MVI0_CAERE E3MVI0 Caenorhabditis remanei