Formyltetrahydrofolate deformylase (P37051)

Identification
Name:Formyltetrahydrofolate deformylase
Synonyms:
  • Formyl-FH(4) hydrolase
Gene Name:purU
Enzyme Class:
Biological Properties
General Function:Involved in amino acid binding
Specific Function:Produces formate from formyl-tetrahydrofolate. Provides the major source of formate for the purT-dependent synthesis of 5'-phosphoribosyl-N-formylglycinamide (FGAR) during aerobic growth. Has a role in regulating the one-carbon pool
Cellular Location:Cytoplasmic
SMPDB Pathways:
KEGG Pathways:
  • Glyoxylate and dicarboxylate metabolism ec00630
  • One carbon pool by folate ec00670
KEGG Reactions:
1.0Thumb+1.0Thumb ↔ 1.0Thumb+1.0Thumb+1.0Thumb
1.0N10-Formyl-THF + 1.0Water ↔ 1.0Formic acid + 1.0Hydrogen ion + 1.0Tetrahydrofolic acid
ReactionCard
1.0Thumb+1.0Thumb ↔ 1.0Thumb+1.0Thumb
1.0N10-Formyl-THF + 1.0Water ↔ 1.0Formic acid + 1.0Tetrahydrofolic acid
ReactionCard
SMPDB Reactions:
1.0Thumb+1.0Tetrahydrofolic acid+1.0Thumb → 1.0Thumb+1.010-Formyltetrahydrofolate+1.0Thumb
1.0Formic acid + 1.0Tetrahydrofolic acid + 1.0Tetrahydrofolic acid → 1.0Water + 1.010-Formyltetrahydrofolate + 1.0N10-Formyl-THF
ReactionCard
EcoCyc Reactions:
1.0Thumb+1.0Thumb ↔ 1.0Thumb+1.0Thumb+1.0Thumb
1.0N10-Formyl-THF + 1.0Water ↔ 1.0Formic acid + 1.0Hydrogen ion + 1.0Tetrahydrofolic acid
ReactionCard
Complex Reactions:
1.0Thumb+1.0Thumb → 1.0Thumb+1.0Thumb
1.0N10-Formyl-THF + 1.0Water → 1.0Formic acid + 1.0Tetrahydrofolic acid
ReactionCard
Metabolites:
ECMDB IDNameView
ECMDB00142Formic acidMetaboCard
ECMDB21225Hydrogen ionMetaboCard
ECMDB00972N10-Formyl-THFMetaboCard
ECMDB01846Tetrahydrofolic acidMetaboCard
ECMDB00494WaterMetaboCard
GO Classification:
Function
amino acid binding
binding
carboxylic acid binding
catalytic activity
formyltetrahydrofolate deformylase activity
glycine hydroxymethyltransferase activity
hydrolase activity
hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds
hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amides
hydroxymethyl-, formyl- and related transferase activity
methyltransferase activity
transferase activity
transferase activity, transferring one-carbon groups
Process
'de novo' IMP biosynthetic process
biosynthetic process
cellular nitrogen compound metabolic process
IMP biosynthetic process
metabolic process
nitrogen compound metabolic process
nucleobase, nucleoside and nucleotide metabolic process
nucleobase, nucleoside, nucleotide and nucleic acid metabolic process
nucleoside phosphate metabolic process
nucleotide metabolic process
purine nucleoside monophosphate biosynthetic process
purine nucleotide biosynthetic process
purine nucleotide metabolic process
purine ribonucleoside monophosphate biosynthetic process
Gene Properties
Blattner:b1232
Gene OrientationCounterclockwise
Centisome Percentage:27.74
Left Sequence End1287005
Right Sequence End1287847
Gene Sequence:
>843 bp
ATGCATTCACTCCAACGTAAAGTTCTGCGTACTATTTGTCCGGACCAAAAAGGTCTGATC
GCACGTATTACCAATATTTGCTACAAGCACGAGTTAAATATCGTACAGAACAATGAATTT
GTTGATCACCGTACCGGGCGCTTTTTTATGCGCACGGAACTGGAAGGGATTTTTAATGAT
TCCACCCTGCTGGCGGATCTCGATAGCGCATTGCCAGAAGGCTCCGTGCGTGAGCTGAAT
CCTGCCGGTCGTCGCCGGATAGTGATTCTGGTCACTAAAGAAGCGCATTGCCTTGGCGAT
TTGTTGATGAAAGCCAATTACGGCGGCCTGGATGTCGAAATCGCGGCAGTTATTGGTAAC
CACGATACTTTACGTTCTCTGGTTGAGCGTTTTGATATTCCGTTTGAGCTGGTAAGCCAT
GAAGGGTTAACCCGCAACGAGCACGATCAAAAGATGGCGGATGCCATTGATGCTTATCAA
CCTGACTACGTGGTGCTGGCGAAGTATATGCGGGTATTAACGCCGGAATTTGTGGCACGC
TTCCCGAATAAGATCATCAATATTCACCATTCATTCCTGCCAGCGTTTATTGGCGCACGT
CCTTATCACCAGGCCTATGAACGTGGTGTGAAGATTATTGGCGCAACCGCTCACTATGTG
AATGACAATCTGGACGAAGGCCCAATCATCATGCAGGACGTTATTCATGTCGATCATACC
TACACAGCTGAAGATATGATGCGCGCAGGTCGTGACGTCGAGAAAAACGTCTTAAGTCGT
GCACTATACAAAGTACTGGCACAGCGCGTCTTTGTTTACGGTAATCGAACGATTATTCTT
TAA
Protein Properties
Pfam Domain Function:
Protein Residues:280
Protein Molecular Weight:31934
Protein Theoretical pI:7
Signaling Regions:
  • None
Transmembrane Regions:
  • None
Protein Sequence:
>Formyltetrahydrofolate deformylase
MHSLQRKVLRTICPDQKGLIARITNICYKHELNIVQNNEFVDHRTGRFFMRTELEGIFND
STLLADLDSALPEGSVRELNPAGRRRIVILVTKEAHCLGDLLMKANYGGLDVEIAAVIGN
HDTLRSLVERFDIPFELVSHEGLTRNEHDQKMADAIDAYQPDYVVLAKYMRVLTPEFVAR
FPNKIINIHHSFLPAFIGARPYHQAYERGVKIIGATAHYVNDNLDEGPIIMQDVIHVDHT
YTAEDMMRAGRDVEKNVLSRALYKVLAQRVFVYGNRTIIL
References
External Links:
ResourceLink
Uniprot ID:P37051
Uniprot Name:PURU_ECOLI
GenBank Gene ID:AP009048
Genebank Protein ID:1651625
Ecogene ID:EG11819
Ecocyc:EG11819
ColiBase:b1232
Kegg Gene:b1232
EchoBASE ID:EB1766
CCDB:PURU_ECOLI
BacMap:16129193
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
  • Bosl, M., Kersten, H. (1994). "Organization and functions of genes in the upstream region of tyrT of Escherichia coli: phenotypes of mutants with partial deletion of a new gene (tgs)." J Bacteriol 176:221-231. Pubmed: 8282700
  • 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
  • Nagy, P. L., Marolewski, A., Benkovic, S. J., Zalkin, H. (1995). "Formyltetrahydrofolate hydrolase, a regulatory enzyme that functions to balance pools of tetrahydrofolate and one-carbon tetrahydrofolate adducts in Escherichia coli." J Bacteriol 177:1292-1298. Pubmed: 7868604
  • Nagy, P. L., McCorkle, G. M., Zalkin, H. (1993). "purU, a source of formate for purT-dependent phosphoribosyl-N-formylglycinamide synthesis." J Bacteriol 175:7066-7073. Pubmed: 8226647
  • Oshima, T., Aiba, H., Baba, T., Fujita, K., Hayashi, K., Honjo, A., Ikemoto, K., Inada, T., Itoh, T., Kajihara, M., Kanai, K., Kashimoto, K., Kimura, S., Kitagawa, M., Makino, K., Masuda, S., Miki, T., Mizobuchi, K., Mori, H., Motomura, K., Nakamura, Y., Nashimoto, H., Nishio, Y., Saito, N., Horiuchi, T., et, a. l. .. (1996). "A 718-kb DNA sequence of the Escherichia coli K-12 genome corresponding to the 12.7-28.0 min region on the linkage map." DNA Res 3:137-155. Pubmed: 8905232