Bifunctional protein folC (P08192)

Identification
Name:Bifunctional protein folC
Synonyms:
  • Folylpolyglutamate synthase
  • Folylpoly-gamma-glutamate synthetase
  • FPGS
  • Tetrahydrofolylpolyglutamate synthase
  • Tetrahydrofolate synthase
  • Dihydrofolate synthase
Gene Name:folC
Enzyme Class:
Biological Properties
General Function:Involved in tetrahydrofolylpolyglutamate synthase activity
Specific Function:Conversion of folates to polyglutamate derivatives
Cellular Location:Not Available
SMPDB Pathways:
KEGG Pathways:
KEGG Reactions:
1.0Thumb+1.0Thumb+1.0Thumb ↔ 1.0Thumb+1.0Thumb+1.0Thumb+1.0Thumb
1.0Adenosine triphosphate + 1.07,8-Dihydropteroic acid + 1.0L-Glutamate ↔ 1.0ADP + 1.0Dihydrofolic acid + 1.0Hydrogen ion + 1.0Phosphate
ReactionCard
1.0Thumb+1.0Thumb+1.0Thumb ↔ 1.0Thumb+1.0Thumb+1.0Thumb
1.0Adenosine triphosphate + 1.0Tetrahydrofolic acid + 1.0L-Glutamate ↔ 1.0ADP + 1.0Phosphate + 1.0Tetrahydrofolyl-[Glu](2)
ReactionCard
1.0Thumb+1.0Thumb+1.0Thumb ↔ 1.0Thumb+1.0Thumb+1.0Thumb
1.0Adenosine triphosphate + 1.07,8-Dihydropteroic acid + 1.0L-Glutamate ↔ 1.0ADP + 1.0Phosphate + 1.0Dihydrofolic acid
ReactionCard
1.0Thumb+1.0Thumb+1.0Thumb ↔ 1.0Thumb+1.0Thumb
1.0Adenosine triphosphate + 1.0THF-polyglutamate + 1.0L-Glutamate ↔ 1.0ADP + 1.0Phosphate
ReactionCard
SMPDB Reactions:
1.0Thumb+1.0Thumb+1.0L-Glutamic acid+1.0Thumb → 1.0Adenosine diphosphate+1.0Thumb+1.0Thumb+1.07,8-dihydrofolate monoglutamate+1.0Thumb+1.0Thumb
1.07,8-Dihydropteroic acid + 1.0Adenosine triphosphate + 1.0L-Glutamic acid + 1.0L-Glutamate → 1.0Adenosine diphosphate + 1.0Phosphate + 1.0Hydrogen ion + 1.07,8-dihydrofolate monoglutamate + 1.0ADP + 1.0Dihydrofolic acid
ReactionCard
EcoCyc Reactions:
1.0Thumb+1.0Thumb+1.0Thumb ↔ 1.0Thumb+1.0Thumb+1.0Thumb+1.0Thumb
1.0Adenosine triphosphate + 1.07,8-Dihydropteroic acid + 1.0L-Glutamate ↔ 1.0ADP + 1.0Dihydrofolic acid + 1.0Hydrogen ion + 1.0Phosphate
ReactionCard
1.0Thumb+1.0Thumb+1.0Thumb → 1.0Thumb+1.0Thumb+1.0Thumb+1.0Thumb
1.0L-Glutamate + 1.07,8-Dihydropteroic acid + 1.0Adenosine triphosphate → 1.0Hydrogen ion + 1.0Dihydrofolic acid + 1.0Phosphate + 1.0ADP
ReactionCard
1.0a tetrahydrofolate-glutamate+1.0Thumb+1.0Thumb → 1.0a tetrahydrofolate-glutamate+1.0Thumb+1.0Thumb
1.0a tetrahydrofolate-glutamate + 1.0L-Glutamate + 1.0Adenosine triphosphate → 1.0a tetrahydrofolate-glutamate + 1.0Phosphate + 1.0ADP
ReactionCard
1.0an N10-formyl-tetrahydrofolate+1.0Thumb+1.0Thumb → 1.0an N10-formyl-tetrahydrofolate+1.0Thumb+1.0Thumb
1.0an N10-formyl-tetrahydrofolate + 1.0L-Glutamate + 1.0Adenosine triphosphate → 1.0an N10-formyl-tetrahydrofolate + 1.0ADP + 1.0Phosphate
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1.0a 5,10-methylene-tetrahydrofolate+1.0Thumb+1.0Thumb → 1.0a 5,10-methylene-tetrahydrofolate+1.0Thumb+1.0Thumb
1.0a 5,10-methylene-tetrahydrofolate + 1.0L-Glutamate + 1.0Adenosine triphosphate → 1.0a 5,10-methylene-tetrahydrofolate + 1.0Phosphate + 1.0ADP
ReactionCard
Complex Reactions:
1.0Thumb+1.0tetrahydropteroyl-(gamma-Glu)(n)+1.0Thumb → 1.0Thumb+1.0Thumb+1.0tetrahydropteroyl-(gamma-Glu)(n+1)
1.0Adenosine triphosphate + 1.0tetrahydropteroyl-(gamma-Glu)(n) + 1.0L-Glutamate → 1.0ADP + 1.0Inorganic phosphate + 1.0tetrahydropteroyl-(gamma-Glu)(n+1)
ReactionCard
1.0Thumb+1.0Thumb+1.0Thumb → 1.0Thumb+1.0Thumb+1.0Thumb
1.0Adenosine triphosphate + 1.07,8-Dihydropteroic acid + 1.0L-Glutamate → 1.0ADP + 1.0Inorganic phosphate + 1.0Dihydrofolic acid
ReactionCard
Metabolites:
ECMDB IDNameView
ECMDB014127,8-Dihydropteroic acidMetaboCard
ECMDB00538Adenosine triphosphateMetaboCard
ECMDB01341ADPMetaboCard
ECMDB01056Dihydrofolic acidMetaboCard
ECMDB21225Hydrogen ionMetaboCard
ECMDB21380Inorganic phosphateMetaboCard
ECMDB00148L-GlutamateMetaboCard
ECMDB01429PhosphateMetaboCard
ECMDB01846Tetrahydrofolic acidMetaboCard
ECMDB21661Tetrahydrofolyl-[Glu](2)MetaboCard
GO Classification:
Function
acid-amino acid ligase activity
adenyl nucleotide binding
adenyl ribonucleotide binding
ATP binding
binding
catalytic activity
ligase activity
ligase activity, forming carbon-nitrogen bonds
nucleoside binding
purine nucleoside binding
tetrahydrofolylpolyglutamate synthase activity
Process
biosynthetic 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:b2315
Gene OrientationCounterclockwise
Centisome Percentage:52.37
Left Sequence End2429696
Right Sequence End2430964
Gene Sequence:
>1269 bp
ATGTTTGCCCTCTGTGATGTAAACGCGTTTTATGCCAGCTGTGAGACGGTGTTTCGCCCT
GATTTATGGGGTAAACCGGTGGTTGTGCTATCGAATAATGACGGTTGCGTTATCGCCCGA
AACGCTGAGGCAAAGGCGCTTGGCGTTAAAATGGGCGATCCCTGGTTCAAACAAAAAGAT
CTGTTTCGTCGCTGTGGCGTGGTTTGCTTTAGCAGCAATTATGAGCTTTACGCAGACATG
AGCAATCGGGTGATGTCGACGCTGGAAGAGCTATCGCCCCGCGTCGAGATTTACAGTATT
GATGAGGCATTCTGCGATCTGACAGGTGTGCGTAATTGTCGCGATCTGACTGATTTTGGC
AGAGAAATTCGCGCAACGGTGCTACAACGTACCCATCTTACTGTTGGTGTGGGGATCGCC
CAGACCAAAACGCTGGCTAAGCTTGCCAATCATGCGGCAAAAAAATGGCAGCGGCAGACG
GGTGGGGTGGTGGATTTATCAAATCTGGAACGCCAGCGTAAATTAATGTCTGCTCTCCCC
GTGGATGACGTCTGGGGGATTGGACGGCGGATCAGCAAAAAACTGGACGCGATGGGGATC
AAAACCGTTCTCGATTTGGCGGATACAGATATCCGGTTTATCCGTAAACATTTTAATGTC
GTGCTCGAAAGAACGGTGCGTGAACTGCGCGGCGAACCCTGTTTGCAACTGGAAGAGTTT
GCACCGACGAAGCAGGAAATTATCTGTTCCCGCTCGTTTGGTGAACGCATCACGGATTAT
CCGTCGATGCGGCAGGCCATTTGTAGTTACGCTGCCCGGGCGGCGGAAAAACTTCGCAGC
GAGCATCAATATTGTCGGTTTATCTCCACGTTTATTAAGACGTCACCATTTGCGCTCAAT
GAACCTTATTACGGCAATAGCGCGTCGGTAAAACTGCTGACGCCCACTCAGGACAGCAGG
GATATCATTAACGCTGCTACGCGATCTCTGGATGCCATCTGGCAAGCGGGCCATCGTTAC
CAAAAAGCGGGCGTGATGCTGGGGGATTTCTTCAGTCAGGGAGTCGCGCAGCTCAATTTA
TTCGATGACAACGCACCGCGCCCCGGGAGTGAGCAATTGATGACGGTAATGGATACACTG
AATGCTAAAGAGGGCAGAGGAACACTCTATTTTGCCGGGCAGGGGATCCAGCAACAATGG
CAGATGAAGCGAGCCATGCTTTCACCACGTTATACAACGCGAAGTTCTGATTTACTGAGG
GTCAAATAA
Protein Properties
Pfam Domain Function:
Protein Residues:422
Protein Molecular Weight:45405
Protein Theoretical pI:6
PDB File:1W7K
Signaling Regions:
  • None
Transmembrane Regions:
  • None
Protein Sequence:
>Bifunctional protein folC
MIIKRTPQAASPLASWLSYLENLHSKTIDLGLERVSLVAARLGVLKPAPFVFTVAGTNGK
GTTCRTLESILMAAGYKVGVYSSPHLVRYTERVRVQGQELPESAHTASFAEIESARGDIS
LTYFEYGTLSALWLFKQAQLDVVILEVGLGGRLDATNIVDADVAVVTSIALDHTDWLGPD
RESIGREKAGIFRSEKPAIVGEPEMPSTIADVAQEKGALLQRRGVEWNYSVTDHDWAFSD
AHGTLENLPLPLVPQPNAATALAALRASGLEVSENAIRDGIASAILPGRFQIVSESPRVI
FDVAHNPHAAEYLTGRMKALPKNGRVLAVIGMLHDKDIAGTLAWLKSVVDDWYCAPLEGP
RGATAEQLLEHLGNGKSFDSVAQAWDAAMADAKAEDTVLVCGSFHTVAHVMEVIDARRSG
GK
References
External Links:
ResourceLink
Uniprot ID:P08192
Uniprot Name:FOLC_ECOLI
GenBank Gene ID:AP009048
Genebank Protein ID:1651581
PDB ID:1W7K
Ecogene ID:EG10327
Ecocyc:EG10327
ColiBase:b2315
Kegg Gene:b2315
EchoBASE ID:EB0323
CCDB:FOLC_ECOLI
BacMap:16130250
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
  • Bognar, A. L., Osborne, C., Shane, B. (1987). "Primary structure of the Escherichia coli folC gene and its folylpolyglutamate synthetase-dihydrofolate synthetase product and regulation of expression by an upstream gene." J Biol Chem 262:12337-12343. Pubmed: 3040739
  • 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
  • Kimlova, L. J., Pyne, C., Keshavjee, K., Huy, J., Beebakhee, G., Bognar, A. L. (1991). "Mutagenesis of the folC gene encoding folylpolyglutamate synthetase-dihydrofolate synthetase in Escherichia coli." Arch Biochem Biophys 284:9-16. Pubmed: 1989505
  • Nonet, M. L., Marvel, C. C., Tolan, D. R. (1987). "The hisT-purF region of the Escherichia coli K-12 chromosome. Identification of additional genes of the hisT and purF operons." J Biol Chem 262:12209-12217. Pubmed: 3040734
  • Yamamoto, Y., Aiba, H., Baba, T., Hayashi, K., Inada, T., Isono, K., Itoh, T., Kimura, S., Kitagawa, M., Makino, K., Miki, T., Mitsuhashi, N., Mizobuchi, K., Mori, H., Nakade, S., Nakamura, Y., Nashimoto, H., Oshima, T., Oyama, S., Saito, N., Sampei, G., Satoh, Y., Sivasundaram, S., Tagami, H., Horiuchi, T., et, a. l. .. (1997). "Construction of a contiguous 874-kb sequence of the Escherichia coli -K12 genome corresponding to 50.0-68.8 min on the linkage map and analysis of its sequence features." DNA Res 4:91-113. Pubmed: 9205837