Accession | TIGR00676 |
Name | fadh2 |
Function | methylenetetrahydrofolate reductase [NAD(P)H] |
Gene Symbol | metF |
Trusted Cutoff | 293.70 |
Domain Trusted Cutoff | 293.70 |
Noise Cutoff | 289.85 |
Domain Noise Cutoff | 289.85 |
Isology Type | equivalog |
EC Number | 1.5.1.20 |
HMM Length | 275 |
Mainrole Category | Amino acid biosynthesis |
Subrole Category | Aspartate family |
Gene Ontology Term | GO:0004489: methylenetetrahydrofolate reductase (NADPH) activity molecular_function |
| GO:0009086: methionine biosynthetic process biological_process |
Author | Loftus BJ, Haft DH |
Entry Date | Jan 13 2000 2:40PM |
Last Modified | Feb 14 2011 3:27PM |
Comment | The enzyme activities methylenetetrahydrofolate reductase (EC 1.5.1.20) and 5,10-methylenetetrahydrofolate reductase (FADH) (EC 1.7.99.5) differ in that 1.5.1.20 (assigned in many eukaryotes) is defined to use NADP+ as an acceptor, while 1.7.99.5 (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 1.5.1.20 and 1.7.99.5, this model describes the subset of proteins found in bacteria, and currently designated 1.7.99.5.
This protein is an FAD-containing flavoprotein. |
References | RN [1]
RM 99215588
RT The structure and properties of methylenetetrahydrofolate reductase from Escherichia coli suggest how folate ameliorates human hyperhomocysteinemia.
RA Guenther BD, Sheppard CA, Tran P, Rozen R, Matthews RG, Ludwig ML
RL Nat Struct Biol 1999 Apr;6(4):359-65
DR ECOCYC; EG10585; metF
DR EXPERIMENTAL; EGAD|20689|EC3941; Escherichia coli
DR OUTGROUP; EGAD|145028|154652; Schizosaccharomyces pombe
DR OUTGROUP; EGAD|4286|4234; Homo sapiens |
Genome Property | GenProp0161: methionine biosynthesis from homoserine (HMM) |