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InterPro: IPR003171 Methylenetetrahydrofolate reductase

Protein matches Help

UniProtKB

Matches:

1711 proteins

Overview:	sorted by AC,	sorted by name,	of known structure,	proteins with splice variants
Detailed:	sorted by AC,	sorted by name,	of known structure	proteins with splice variants
Table:	For all matching proteins,	of known structure
Architectures
Accession List
Matches in BioMart

Accession

IPR003171 Mehydrof_redctse

Type

Family

Signatures Help

Database	ID	Name	Proteins
Pfam	PF02219	MTHFR	1711
Signatures in BioMart

InterPro Relationships Help

Children

IPR004620 5,10-methylenetetrahydrofolate reductase
IPR004621 Eukaryotic-type methylenetetrahydrofolate reductase

GO Term annotation Help

Process

GO:0006555 methionine metabolic process
GO:0055114 oxidation reduction

Function

GO:0004489 methylenetetrahydrofolate reductase (NADPH) activity

InterPro annotation

Entry Details in BioMart

Abstract

This family includes the 5,10-methylenetetrahydrofolate reductase EC:1.7.99.5 from bacteria and methylenetetrahydrofolate reductase EC:1.5.1.20 from eukaryotes. The structure for this domain is known [1] to be a TIM barrel.

Structural links Help

PDB - click here

SCOP: c.1.23.1

CATH: 3.20.20.220

Database links Help

Enzyme: EC:1.5.1.20

PANDIT: PF02219

Blocks: IPB003171

Pfam Clan: CL0086.8

Taxonomic coverage Help

Overlapping InterPro entries Help

IPR003171

Numbers of overlapping proteins

Average numbers of overlapping amino acids

Example proteins Help

O80585 Methylenetetrahydrofolate reductase 2

P42898 Methylenetetrahydrofolate reductase

P46151 Methylenetetrahydrofolate reductase 1

Q17693 Probable methylenetetrahydrofolate reductase

Q9WU20 Methylenetetrahydrofolate reductase

More proteins

Example Proteins Key

InterPro entry accession number/name and structure databases		Colour code
IPR004621	Eukaryotic-type methylenetetrahydrofolate reductase
IPR003171	Methylenetetrahydrofolate reductase
	SWISS-MODEL
	ModBase

Publications Open in usermanual
1.	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. 6 359-65 1999 [PubMed: 10201405] http://dx.doi.org/10.1038/7594

Additional Reading Open in usermanual
	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
	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

InterPro 23.1