EzCatDB: S00238

DB codeS00238
CATH domainDomain 13.20.20.220Catalytic domain
E.C.1.5.1.20
CSA1b5t


Enzyme Name
Swiss-protKEGG

P0AEZ1
Protein name5,10-methylenetetrahydrofolate reductasemethylenetetrahydrofolate reductase [NAD(P)H]
methylenetetrahydrofolate (reduced nicotinamide adenine dinucleotidephosphate) reductase
5,10-methylenetetrahydrofolate reductase (NADPH)
5,10-methylenetetrahydrofolic acid reductase
5,10-CH2-H4folate reductase
methylenetetrahydrofolate reductase (NADPH2)
5-methyltetrahydrofolate:NAD+ oxidoreductase
5-methyltetrahydrofolate:NAD+ oxidoreductase
methylenetetrahydrofolate (reduced riboflavin adenine dinucleotide)reductase
5,10-methylenetetrahydrofolate reductase
methylenetetrahydrofolate reductase
N5,10-methylenetetrahydrofolate reductase
5,10-methylenetetrahydropteroylglutamate reductase
N5,N10-methylenetetrahydrofolate reductase
methylenetetrahydrofolic acid reductase
5-methyltetrahydrofolate:(acceptor) oxidoreductase (incorrect)
5,10-methylenetetrahydrofolate reductase (FADH2)
MetF
methylenetetrahydrofolate reductase (NADPH)
5-methyltetrahydrofolate:NADP+ oxidoreductase
SynonymsEC 1.5.1.20

KEGG pathways
MAP codePathways
MAP00670One carbon pool by folate
MAP00680Methane metabolism

Swiss-prot:Accession NumberP0AEZ1
Entry nameMETF_ECOLI
Activity5-methyltetrahydrofolate + NAD(P)(+) = 5,10- methylenetetrahydrofolate + NAD(P)H.
SubunitHomotetramer.
Subcellular location
CofactorFAD.


CofactorsSubstratesProducts
KEGG-idC00016C00703C00440C00003C00006C00143C00004C00005
CompoundFADHg2+5-MethyltetrahydrofolateNAD+NADP+5,10-MethylenetetrahydrofolateNADHNADPH
Typeamide group,amine group,aromatic ring (only carbon atom),aromatic ring (with nitrogen atoms),carbohydrate,nucleotideheavy metalamino acids,amide group,amine group,aromatic ring (only carbon atom),aromatic ring (with nitrogen atoms),carboxyl groupamide group,amine group,nucleotideamide group,amine group,nucleotideamino acids,amide group,amine group,aromatic ring (only carbon atom),aromatic ring (with nitrogen atoms),carboxyl groupamide group,amine group,nucleotideamide group,amine group,nucleotide
1b5tABound:FADBound:_HGUnboundUnboundUnboundUnboundUnboundUnbound
1b5tBBound:FADBound:_HGUnboundUnboundUnboundUnboundUnboundUnbound
1b5tCBound:FADBound:_HGUnboundUnboundUnboundUnboundUnboundUnbound

Active-site residues
resource
PDB;1b5t & literature [7]
pdbCatalytic residuesCofactor-binding residuescomment
1b5tAGLU 28;ASP 120
CYS 91;ILE 92;ARG 118;MET 130(Mercury binding)

1b5tBGLU 28;ASP 120
CYS 91;ILE 92;ARG 118;MET 130(Mercury binding)

1b5tCGLU 28;ASP 120
CYS 91;ILE 92;ARG 118;       (Mercury binding)
invisible M130

References for Catalytic Mechanism
ReferencesSectionsNo. of steps in catalysis
[3]Scheme 1, Fig.1, p.6223-6225

references
[1]
CommentsX-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS)
Medline ID99215588
PubMed ID10201405
JournalNat Struct Biol
Year1999
Volume6
Pages359-65
AuthorsGuenther BD, Sheppard CA, Tran P, Rozen R, Matthews RG, Ludwig ML
TitleThe structure and properties of methylenetetrahydrofolate reductase from Escherichia coli suggest how folate ameliorates human hyperhomocysteinemia.
Related PDB1b5t
Related Swiss-protP0AEZ1
[2]
PubMed ID11086190
JournalJ Biochem Biophys Methods
Year2000
Volume46
Pages11-20
AuthorsSobti P, Rothenberg SP, Quadros EV
TitleRadioenzymatic assay for reductive catalysis of N(5)N(10)-methylenetetrahydrofolate by methylenetetrahydrofolate reductase.
[3]
PubMed ID11371182
JournalBiochemistry
Year2001
Volume40
Pages6216-26
AuthorsTrimmer EE, Ballou DP, Ludwig ML, Matthews RG
TitleFolate activation and catalysis in methylenetetrahydrofolate reductase from Escherichia coli: roles for aspartate 120 and glutamate 28.
[4]
PubMed ID11371181
JournalBiochemistry
Year2001
Volume40
Pages6205-15
AuthorsTrimmer EE, Ballou DP, Matthews RG
TitleMethylenetetrahydrofolate reductase from Escherichia coli: elucidation of the kinetic mechanism by steady-state and rapid-reaction studies.

comments
The E.C. was transferred from 1.7.99.5 to 1.5.1.20.
Although mercury is annotated as a cofactor, it is not clear how it functions in the active site.

createdupdated
2004-08-042009-02-26


Copyright: Nozomi Nagano, JST & CBRC-AIST
Funded by PRESTO/Japan Science and Technology Corporation (JST) (December 2001 - November 2004)
Funded by Grant-in-Aid for Publication of Scientific Research Results/Japan Society for the Promotion of Science (JSPS) (April 2005 - March 2006)
Funded by Grant-in-Aid for Scientific Research (B)/Japan Society for the Promotion of Science (JSPS) (April 2005 - March 2008)
Funded by BIRD/Japan Science and Technology Corporation (JST) (September 2005 - September 2010)
Funded by BIRD/Japan Science and Technology Corporation (JST) (October 2007 - September 2010)
Funded by Grant-in-Aid for Publication of Scientific Research Results/Japan Society for the Promotion of Science (JSPS) (April 2011 - March 2012)

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