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
- FunctionsFAD binding / methylenetetrahydrofolate reductase (NAD(P)H) activityProcessesmethionine biosynthetic process / one-carbon metabolic process / protein homotetramerization / tetrahydrofolate biosynthetic process / tetrahydrofolate interconversionComponentscytosol
- 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
- MTHFR (PF02219)
- 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
Resource Link UniProtKB ID P0AEZ1 UniProtKB Entry Name METF_ECOLI GenBank Gene ID V01502 - General References
- 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]
- 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]
- 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]
- 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]
- 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]
- 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]
- 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]
- 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]
- 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]
- 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]
- 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]