Bifunctional protein folD (P24186)

Identification
Name:Bifunctional protein folD
Synonyms:
  • Methylenetetrahydrofolate dehydrogenase
  • Methenyltetrahydrofolate cyclohydrolase
Gene Name:folD
Enzyme Class:
Biological Properties
General Function:Involved in nucleotide binding
Specific Function:Catalyzes the oxidation of 5,10- methylenetetrahydrofolate to 5,10-methenyltetrahydrofolate and then the hydrolysis of 5,10-methenyltetrahydrofolate to 10- formyltetrahydrofolate. This enzyme is specific for NADP
Cellular Location:Not Available
SMPDB Pathways:
KEGG Pathways:
  • Glyoxylate and dicarboxylate metabolism ec00630
  • Metabolic pathways eco01100
  • Microbial metabolism in diverse environments ec01120
  • One carbon pool by folate ec00670
  • Reductive carboxylate cycle (CO2 fixation) ec00720
KEGG Reactions:
1.0Thumb+1.0Thumb ↔ 1.0Thumb+1.0Thumb
1.0Water + 1.05,10-Methenyltetrahydrofolate ↔ 1.0N10-Formyl-THF + 1.0Hydrogen ion
ReactionCard
1.0Thumb+1.0Thumb ↔ 1.0Thumb+1.0Thumb+1.0Thumb
1.05,10-Methylene-THF + 1.0NADP ↔ 1.05,10-Methenyltetrahydrofolate + 1.0NADPH + 1.0Hydrogen ion
ReactionCard
1.0Thumb+1.0Thumb ↔ 1.0Thumb+1.0Thumb
1.05,10-Methylene-THF + 1.0NADP ↔ 1.05,10-Methenyltetrahydrofolate + 1.0NADPH
ReactionCard
SMPDB Reactions:
1.010-Formyltetrahydrofolate+1.0Thumb ↔ 1.0 5,10-Methenyltetrahydrofolic acid +1.0Thumb
1.010-Formyltetrahydrofolate + 1.0Hydrogen ion ↔ 1.0 5,10-Methenyltetrahydrofolic acid + 1.0Water
ReactionCard
1.0 5,10-Methenyltetrahydrofolic acid +1.0NADPH+1.0Thumb → 1.05,10-Methylene-THF+1.0Thumb+1.0Thumb
1.0 5,10-Methenyltetrahydrofolic acid + 1.0NADPH + 1.0NADPH → 1.05,10-Methylene-THF + 1.0NADP + 1.05,10-Methylene-THF
ReactionCard
EcoCyc Reactions:
1.0Thumb+1.0Thumb ↔ 1.0Thumb+1.0Thumb
1.0Water + 1.05,10-Methenyltetrahydrofolate ↔ 1.0N10-Formyl-THF + 1.0Hydrogen ion
ReactionCard
1.0Thumb+1.0Thumb ↔ 1.0Thumb+1.0Thumb+1.0Thumb
1.05,10-Methylene-THF + 1.0NADP ↔ 1.05,10-Methenyltetrahydrofolate + 1.0NADPH + 1.0Hydrogen ion
ReactionCard
Complex Reactions:
1.0Thumb+1.0Thumb → 1.0Thumb+1.0Thumb
1.05,10-Methylene-THF + 1.0NADP → 1.05,10-Methenyltetrahydrofolate + 1.0NADPH
ReactionCard
1.0Thumb+1.0Thumb → 1.0Thumb
1.05,10-Methenyltetrahydrofolate + 1.0Water → 1.0N10-Formyl-THF
ReactionCard
Metabolites:
ECMDB IDNameView
ECMDB211765,10-MethenyltetrahydrofolateMetaboCard
ECMDB013545,10-Methylene-THFMetaboCard
ECMDB21225Hydrogen ionMetaboCard
ECMDB00972N10-Formyl-THFMetaboCard
ECMDB00217NADPMetaboCard
ECMDB04111NADPHMetaboCard
ECMDB00494WaterMetaboCard
GO Classification:
Function
binding
catalytic activity
Process
cellular aromatic compound metabolic process
cellular metabolic process
folic acid and derivative biosynthetic process
folic acid and derivative metabolic process
metabolic process
Gene Properties
Blattner:b0529
Gene OrientationCounterclockwise
Centisome Percentage:11.99
Left Sequence End556098
Right Sequence End556964
Gene Sequence:
>867 bp
ATGAAGTATGTCTTTATTGAAAAACATCAGGCTGAGTTCAGCATCAAAGCAATGTGCCGC
GTGCTCCGGGTGGCCCGCAGCGGCTGGTATACGTGGTGTCAGCGGCGGACAAGGATAAGC
ACGCGTCAGCAGTTCCGCCAACACTGCGACAGCGTTGTCCTCGCGGCTTTTACCCGGTCA
AAACAGCGTTACGGTGCCCCACGCCTGACGGATGAACTGCGTGCTCAGGGTTACCCCTTT
AACGTAAAAACCGTGGCGGCAAGCCTGCGCCGTCAGGGACTGAGGGCAAAGGCCTCCCGG
AAGTTCAGCCCGGTCAGCTACCGCGCACACGGCCTGCCTGTGTCAGAAAATCTGTTGGAG
CAGGATTTTTACGCCAGTGGCCCGAACCAGAAGTGGGCAGGAGACATCACGTACTTACGT
ACAGATGAAGGCTGGCTGTATCTGGCAGTGGTCATTGACCTGTGGTCACGTGCCGTTATT
GGCTGGTCAATGTCGCCACGCATGACGGCGCAACTGGCCTGCGATGCCCTGCAGATGGCG
CTGTGGCGGCGTAAGAGGCCCCGGAACGTTATCGTTCACACGGACCGTGGAGGCCAGTAC
TGTTCAGCAGATTATCAGGCGCAACTGAAGCGGCATAATCTGCGTGGAAGTATGAGCGCA
AAAGGTTGCTGCTACGATAATGCCTGCGTGGAAAGCTTCTTTCATTCGCTGAAAGTGGAA
TGTATCCATGGAGAACACTTTATCAGCCGGGAAATAATGCGGGCAACGGTGTTTAATTAT
ATCGAATGTGATTACAATCGGTGGCGGCGGCACAGTTGGTGTGGCGGCCTCAGTCCGGAA
CAATTTGAAAACAAGAACCTCGCTTAG
Protein Properties
Pfam Domain Function:
Protein Residues:288
Protein Molecular Weight:31044
Protein Theoretical pI:6
PDB File:1B0A
Signaling Regions:
  • None
Transmembrane Regions:
  • None
Protein Sequence:
>Bifunctional protein folD
MAAKIIDGKTIAQQVRSEVAQKVQARIAAGLRAPGLAVVLVGSNPASQIYVASKRKACEE
VGFVSRSYDLPETTSEAELLELIDTLNADNTIDGILVQLPLPAGIDNVKVLERIHPDKDV
DGFHPYNVGRLCQRAPRLRPCTPRGIVTLLERYNIDTFGLNAVVIGASNIVGRPMSMELL
LAGCTTTVTHRFTKNLRHHVENADLLIVAVGKPGFIPGDWIKEGAIVIDVGINRLENGKV
VGDVVFEDAAKRASYITPVPGGVGPMTVATLIENTLQACVEYHDPQDE
References
External Links:
ResourceLink
Uniprot ID:P24186
Uniprot Name:FOLD_ECOLI
GenBank Gene ID:AP009048
Genebank Protein ID:85674444
PDB ID:1B0A
Ecogene ID:EG10328
Ecocyc:EG10328
ColiBase:b0529
Kegg Gene:b0529
EchoBASE ID:EB0324
CCDB:FOLD_ECOLI
BacMap:16128513
General Reference:
  • Blattner, F. R., Plunkett, G. 3rd, Bloch, C. A., Perna, N. T., Burland, V., Riley, M., Collado-Vides, J., Glasner, J. D., Rode, C. K., Mayhew, G. F., Gregor, J., Davis, N. W., Kirkpatrick, H. A., Goeden, M. A., Rose, D. J., Mau, B., Shao, Y. (1997). "The complete genome sequence of Escherichia coli K-12." Science 277:1453-1462. Pubmed: 9278503
  • D'Ari, L., Rabinowitz, J. C. (1991). "Purification, characterization, cloning, and amino acid sequence of the bifunctional enzyme 5,10-methylenetetrahydrofolate dehydrogenase/5,10-methenyltetrahydrofolate cyclohydrolase from Escherichia coli." J Biol Chem 266:23953-23958. Pubmed: 1748668
  • Hayashi, K., Morooka, N., Yamamoto, Y., Fujita, K., Isono, K., Choi, S., Ohtsubo, E., Baba, T., Wanner, B. L., Mori, H., Horiuchi, T. (2006). "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110." Mol Syst Biol 2:2006.0007. Pubmed: 16738553
  • Shen, B. W., Dyer, D. H., Huang, J. Y., D'Ari, L., Rabinowitz, J., Stoddard, B. L. (1999). "The crystal structure of a bacterial, bifunctional 5,10 methylene-tetrahydrofolate dehydrogenase/cyclohydrolase." Protein Sci 8:1342-1349. Pubmed: 10386884