DB code: S00238
| CATH domain | 3.20.20.220 : TIM Barrel | Catalytic domain |
|---|---|---|
| E.C. | 1.5.1.20 | |
| CSA | 1b5t | |
| M-CSA | 1b5t | |
| MACiE | ||
| CATH domain | Related DB codes (homologues) |
|---|
| Uniprot Enzyme Name | UniprotKB | Protein name | Synonyms | RefSeq | Pfam |
|---|---|---|---|---|
| P0AEZ1 |
5,10-methylenetetrahydrofolate reductase
|
EC
1.5.1.20
|
NP_418376.1
(Protein)
NC_000913.2 (DNA/RNA sequence) YP_491510.1 (Protein) NC_007779.1 (DNA/RNA sequence) |
PF02219
(MTHFR)
[Graphical View] |
| KEGG enzyme name |
|---|
|
methylenetetrahydrofolate 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 |
| UniprotKB: Accession Number | Entry name | Activity | Subunit | Subcellular location | Cofactor |
|---|---|---|---|---|---|
| P0AEZ1 | METF_ECOLI | 5-methyltetrahydrofolate + NAD(P)(+) = 5,10- methylenetetrahydrofolate + NAD(P)H. | Homotetramer. | FAD. |
| KEGG Pathways | Map code | Pathways | E.C. |
|---|---|---|
| MAP00670 | One carbon pool by folate | |
| MAP00680 | Methane metabolism |
| Compound table | ||||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Cofactors | Substrates | Products | Intermediates | |||||||||||
| KEGG-id | C00016 | C00703 | C00440 | C00003 | C00006 | C00143 | C00004 | C00005 | ||||||
| E.C. | ||||||||||||||
| Compound | FAD | Hg2+ | 5-Methyltetrahydrofolate | NAD+ | NADP+ | 5,10-Methylenetetrahydrofolate | NADH | NADPH | ||||||
| Type | amide group,amine group,aromatic ring (only carbon atom),aromatic ring (with nitrogen atoms),carbohydrate,nucleotide | heavy metal | amino acids,amide group,amine group,aromatic ring (only carbon atom),aromatic ring (with nitrogen atoms),carboxyl group | amide group,amine group,nucleotide | amide group,amine group,nucleotide | amino acids,amide group,amine group,aromatic ring (only carbon atom),aromatic ring (with nitrogen atoms),carboxyl group | amide group,amine group,nucleotide | amide group,amine group,nucleotide | ||||||
| ChEBI |
16238 16238 |
16793 16793 |
15641 15641 |
15846 15846 |
18009 18009 |
16908 16908 |
16474 16474 |
|||||||
| PubChem |
643975 643975 |
26623 26623 |
439234 444412 439234 444412 |
5893 5893 |
5886 5886 |
439175 439175 |
439153 439153 |
5884 5884 |
||||||
| 1b5tA |
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Bound:FAD | Bound:_HG | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | |
| 1b5tB |
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Bound:FAD | Bound:_HG | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | |
| 1b5tC |
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Bound:FAD | Bound:_HG | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | |
| Reference for Active-site residues | ||
|---|---|---|
| resource | references | E.C. |
| PDB;1b5t & literature [7] | ||
| Active-site residues | ||||||||||
|---|---|---|---|---|---|---|---|---|---|---|
| PDB | Catalytic residues | Cofactor-binding residues | Modified residues | Main-chain involved in catalysis | Comment | |||||
| 1b5tA |
|
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|
GLU 28;ASP 120 | CYS 91;ILE 92;ARG 118;MET 130(Mercury binding) | |||
| 1b5tB |
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GLU 28;ASP 120 | CYS 91;ILE 92;ARG 118;MET 130(Mercury binding) | |||
| 1b5tC |
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GLU 28;ASP 120 | CYS 91;ILE 92;ARG 118; (Mercury binding) | invisible M130 | ||
| References for Catalytic Mechanism | ||
|---|---|---|
| References | Sections | No. of steps in catalysis |
|
[3]
|
Scheme 1, Fig.1, p.6223-6225 | |
| References | |
|---|---|
| [1] | |
| Resource | |
| Comments | X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) |
| Medline ID | 99215588 |
| PubMed ID | 10201405 |
| Journal | Nat Struct Biol |
| Year | 1999 |
| Volume | 6 |
| Pages | 359-65 |
| Authors | Guenther BD, Sheppard CA, Tran P, Rozen R, Matthews RG, Ludwig ML |
| Title | The structure and properties of methylenetetrahydrofolate reductase from Escherichia coli suggest how folate ameliorates human hyperhomocysteinemia. |
| Related PDB | 1b5t |
| Related UniProtKB | P0AEZ1 |
| [2] | |
| Resource | |
| Comments | |
| Medline ID | |
| PubMed ID | 11086190 |
| Journal | J Biochem Biophys Methods |
| Year | 2000 |
| Volume | 46 |
| Pages | 11-20 |
| Authors | Sobti P, Rothenberg SP, Quadros EV |
| Title | Radioenzymatic assay for reductive catalysis of N(5)N(10)-methylenetetrahydrofolate by methylenetetrahydrofolate reductase. |
| Related PDB | |
| Related UniProtKB | |
| [3] | |
| Resource | |
| Comments | |
| Medline ID | |
| PubMed ID | 11371182 |
| Journal | Biochemistry |
| Year | 2001 |
| Volume | 40 |
| Pages | 6216-26 |
| Authors | Trimmer EE, Ballou DP, Ludwig ML, Matthews RG |
| Title | Folate activation and catalysis in methylenetetrahydrofolate reductase from Escherichia coli: roles for aspartate 120 and glutamate 28. |
| Related PDB | |
| Related UniProtKB | |
| [4] | |
| Resource | |
| Comments | |
| Medline ID | |
| PubMed ID | 11371181 |
| Journal | Biochemistry |
| Year | 2001 |
| Volume | 40 |
| Pages | 6205-15 |
| Authors | Trimmer EE, Ballou DP, Matthews RG |
| Title | Methylenetetrahydrofolate reductase from Escherichia coli: elucidation of the kinetic mechanism by steady-state and rapid-reaction studies. |
| Related PDB | |
| Related UniProtKB | |
| Comments |
|---|
|
The E.C. Although mercury is annotated as a cofactor, |
| Created | Updated |
|---|---|
| 2004-08-04 | 2009-02-26 |