5,10-methylenetetrahydrofolate reductase

Details

Name
5,10-methylenetetrahydrofolate reductase
Synonyms
  • 1.5.1.20
Gene Name
metF
Organism
Escherichia coli (strain K12)
Amino acid sequence
>lcl|BSEQ0011494|5,10-methylenetetrahydrofolate reductase
MSFFHASQRDALNQSLAEVQGQINVSFEFFPPRTSEMEQTLWNSIDRLSSLKPKFVSVTY
GANSGERDRTHSIIKGIKDRTGLEAAPHLTCIDATPDELRTIARDYWNNGIRHIVALRGD
LPPGSGKPEMYASDLVTLLKEVADFDISVAAYPEVHPEAKSAQADLLNLKRKVDAGANRA
ITQFFFDVESYLRFRDRCVSAGIDVEIIPGILPVSNFKQAKKFADMTNVRIPAWMAQMFD
GLDDDAETRKLVGANIAMDMVKILSREGVKDFHFYTLNRAEMSYAICHTLGVRPGL
Number of residues
296
Molecular Weight
33102.375
Theoretical pI
6.4
GO Classification
Functions
FAD binding / methylenetetrahydrofolate reductase (NAD(P)H) activity
Processes
methionine biosynthetic process / one-carbon metabolic process / protein homotetramerization / tetrahydrofolate biosynthetic process / tetrahydrofolate interconversion
Components
cytosol
General Function
Methylenetetrahydrofolate reductase (nad(p)h) activity
Specific Function
Methylenetetrahydrofolate reductase required to generate the methyl groups necessary for methionine synthetase to convert homocysteine to methionine.
Pfam Domain Function
Transmembrane Regions
Not Available
Cellular Location
Not Available
Gene sequence
>lcl|BSEQ0011495|5,10-methylenetetrahydrofolate reductase (metF)
ATGAGCTTTTTTCACGCCAGCCAGCGGGATGCCCTGAATCAGAGCCTGGCAGAAGTCCAG
GGGCAGATTAACGTTTCGTTCGAGTTTTTCCCGCCGCGTACCAGTGAAATGGAGCAGACC
CTGTGGAACTCCATCGATCGCCTTAGCAGCCTGAAACCGAAGTTTGTATCGGTGACCTAT
GGCGCGAACTCCGGCGAGCGCGACCGTACGCACAGCATTATTAAAGGCATTAAAGATCGC
ACTGGTCTGGAAGCGGCACCGCATCTTACTTGCATTGATGCGACGCCCGACGAGCTGCGC
ACCATTGCACGCGACTACTGGAATAACGGTATTCGTCATATCGTGGCGCTGCGTGGCGAT
CTGCCGCCGGGAAGTGGTAAGCCAGAAATGTATGCTTCTGACCTGGTGACGCTGTTAAAA
GAAGTGGCAGATTTCGATATCTCCGTGGCGGCGTATCCGGAAGTTCACCCGGAAGCAAAA
AGCGCTCAGGCGGATTTGCTTAATCTGAAACGCAAAGTGGATGCCGGAGCCAACCGCGCG
ATTACTCAGTTCTTCTTCGATGTCGAAAGCTACCTGCGTTTTCGTGACCGCTGTGTATCG
GCGGGCATTGATGTGGAAATTATTCCGGGAATTTTGCCGGTATCTAACTTTAAACAGGCG
AAGAAATTTGCCGATATGACCAACGTGCGTATTCCGGCGTGGATGGCGCAAATGTTCGAC
GGTCTGGATGATGATGCCGAAACCCGCAAACTGGTTGGCGCGAATATTGCCATGGATATG
GTGAAGATTTTAAGCCGTGAAGGAGTGAAAGATTTCCACTTCTATACGCTTAACCGTGCT
GAAATGAGTTACGCGATTTGCCATACGCTGGGGGTTCGACCTGGTTTATAA
Chromosome Location
Not Available
Locus
Not Available
External Identifiers
ResourceLink
UniProtKB IDP0AEZ1
UniProtKB Entry NameMETF_ECOLI
GenBank Gene IDV01502
General References
  1. Saint-Girons I, Duchange N, Zakin MM, Park I, Margarita D, Ferrara P, Cohen GN: Nucleotide sequence of metF, the E. coli structural gene for 5-10 methylene tetrahydrofolate reductase and of its control region. Nucleic Acids Res. 1983 Oct 11;11(19):6723-32. [Article]
  2. Plunkett G 3rd, Burland V, Daniels DL, Blattner FR: Analysis of the Escherichia coli genome. III. DNA sequence of the region from 87.2 to 89.2 minutes. Nucleic Acids Res. 1993 Jul 25;21(15):3391-8. [Article]
  3. Blattner FR, Plunkett G 3rd, Bloch CA, Perna NT, Burland V, Riley M, Collado-Vides J, Glasner JD, Rode CK, Mayhew GF, Gregor J, Davis NW, Kirkpatrick HA, Goeden MA, Rose DJ, Mau B, Shao Y: The complete genome sequence of Escherichia coli K-12. Science. 1997 Sep 5;277(5331):1453-62. [Article]
  4. Hayashi K, Morooka N, Yamamoto Y, Fujita K, Isono K, Choi S, Ohtsubo E, Baba T, Wanner BL, Mori H, Horiuchi T: Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110. Mol Syst Biol. 2006;2:2006.0007. Epub 2006 Feb 21. [Article]
  5. KATZEN HM, BUCHANAN JM: ENZYMATIC SYNTHESIS OF THE METHYL GROUP OF METHIONINE. 8. REPRESSION-DEREPRESSION, PURIFICATION, AND PROPERTIES OF 5,10-METHYLENETETRAHYDROFOLATE REDUCTASE FROM ESCHERICHIA COLI. J Biol Chem. 1965 Feb;240:825-35. [Article]
  6. Zakin MM, Greene RC, Dautry-Varsat A, Duchange N, Ferrara P, Py MC, Margarita D, Cohen GN: Construction and physical mapping of plasmids containing the metJBLF gene cluster of E. coli K12. Mol Gen Genet. 1982;187(1):101-6. [Article]
  7. Trimmer EE, Ballou DP, Ludwig ML, Matthews RG: Folate activation and catalysis in methylenetetrahydrofolate reductase from Escherichia coli: roles for aspartate 120 and glutamate 28. Biochemistry. 2001 May 29;40(21):6216-26. [Article]
  8. 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. 1999 Apr;6(4):359-65. [Article]
  9. 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. 2005 Aug 30;44(34):11447-57. [Article]
  10. 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. 2006 Apr 18;45(15):4808-18. [Article]
  11. Lee MN, Takawira D, Nikolova AP, Ballou DP, Furtado VC, Phung NL, Still BR, Thorstad MK, Tanner JJ, Trimmer EE: Functional role for the conformationally mobile phenylalanine 223 in the reaction of methylenetetrahydrofolate reductase from Escherichia coli. Biochemistry. 2009 Aug 18;48(32):7673-85. doi: 10.1021/bi9007325. [Article]

Drug Relations

Drug Relations
DrugBank IDNameDrug groupPharmacological action?ActionsDetails
DB03147Flavin adenine dinucleotideapprovedunknownDetails