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InterPro: IPR004620 5,10-methylenetetrahydrofolate reductase

Protein matchesHelp
UniProtKB
Matches:
912 proteins
AccessionHelp IPR004620 MTHF_reductase_bac
TypeHelp Family
SignaturesHelp
InterPro RelationshipsHelp
Parent IPR003171 Methylenetetrahydrofolate reductase
GO Term annotationHelp
Process GO:0009086 methionine biosynthetic process
GO:0055114 oxidation reduction
InterPro annotation
BioMart Logo Entry Details in BioMart
AbstractHelp

The enzyme activities methylenetetrahydrofolate reductase (EC:1.5.1.20) and 5,10-methylenetetrahydrofolate reductase (FADH) (EC:1.7.99.5) differ in that the former (assigned in many eukaryotes) is defined to use NADP+ as an acceptor, while the latter (assigned in many bacteria) is flexible with respect to the acceptor. Both convert 5-methyltetrahydrofolate to 5,10-methylenetetrahydrofolate. From a larger set of proteins assigned as one or the other, this family describes the subset of proteins found in bacteria, and currently designated 5,10-methylenetetrahydrofolate reductase. This protein is an FAD-containing flavoprotein.

Structural linksHelp
SCOP: c.1.23.1
CATH: 3.20.20.220
Database linksHelp
Enzyme: EC:1.5.1.20

Taxonomic coverageHelp

Overlapping InterPro entriesHelp
IPR004620 Numbers of overlapping proteins Average numbers of overlapping amino acids

Example proteinsHelp
P0AEZ1 5,10-methylenetetrahydrofolate reductase

More proteins


Example Proteins Key


InterPro entry accession number/name and structure databases Colour code
IPR004620 5,10-methylenetetrahydrofolate reductase
IPR003171 Methylenetetrahydrofolate reductase
PDB Chain
ModBase
SCOP Domain
CATH Domain

PublicationsHelp

Additional ReadingHelp
Pejchal R, Sargeant R, Ludwig ML.
Structures of NADH and CH3-H4folate complexes of Escherichia coli methylenetetrahydrofolate reductase reveal a spartan strategy for a ping-pong reaction.
Biochemistry 44 2005 11447-57 [PubMed: 16114881]
http://dx.doi.org/10.1021/bi050533q
Guenther BD, Sheppard CA, Tran P, Rozen R, Matthews RG, Ludwig ML.
The structure and properties of methylenetetrahydrofolate reductase from Escherichia coli suggest how folate ameliorates human hyperhomocysteinemia.
Nat. Struct. Biol. 6 1999 359-65 [PubMed: 10201405]
http://dx.doi.org/10.1038/7594
Pejchal R, Campbell E, Guenther BD, Lennon BW, Matthews RG, Ludwig ML.
Structural perturbations in the Ala --> Val polymorphism of methylenetetrahydrofolate reductase: how binding of folates may protect against inactivation.
Biochemistry 45 2006 4808-18 [PubMed: 16605249]
http://dx.doi.org/10.1021/bi052294c
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InterPro 23.1