Phosphoribosylglycinamide formyltransferase (P08179)

Identification
Name:Phosphoribosylglycinamide formyltransferase
Synonyms:
  • 5'-phosphoribosylglycinamide transformylase
  • GAR transformylase
  • GART
Gene Name:purN
Enzyme Class:
Biological Properties
General Function:Involved in hydroxymethyl-, formyl- and related transferase activity
Specific Function:10-formyltetrahydrofolate + N(1)-(5-phospho-D- ribosyl)glycinamide = tetrahydrofolate + N(2)-formyl-N(1)-(5- phospho-D-ribosyl)glycinamide
Cellular Location:Not Available
SMPDB Pathways:
KEGG Pathways:
KEGG Reactions:
1.0Thumb+1.0Thumb ↔ 1.0Thumb+1.0Thumb+1.0Thumb
1.0N10-Formyl-THF + 1.0Glycineamideribotide ↔ 1.05'-Phosphoribosyl-N-formylglycineamide + 1.0Hydrogen ion + 1.0Tetrahydrofolic acid
ReactionCard
1.0Thumb+1.0Thumb ↔ 1.0Thumb+1.0Thumb
1.0N10-Formyl-THF + 1.0Glycineamideribotide ↔ 1.0Tetrahydrofolic acid + 1.05'-Phosphoribosyl-N-formylglycineamide
ReactionCard
1.0Thumb+1.0Thumb+1.0Thumb ↔ 1.0Thumb+1.0Thumb
1.0Glycineamideribotide + 1.05,10-Methenyltetrahydrofolate + 1.0Water ↔ 1.05'-Phosphoribosyl-N-formylglycineamide + 1.0Tetrahydrofolic acid
ReactionCard
SMPDB Reactions:
1.010-formyl-tetrahydrofolate mono-L-glutamate+1.0Thumb → 1.0Thumb+1.0Thumb+1.0Thumb
1.010-formyl-tetrahydrofolate mono-L-glutamate + 1.0N1-(5-phospho-β-D-ribosyl)glycinamide → 1.0Hydrogen ion + 1.0tetrahydropteroyl mono-L-glutamate + 1.05'-Phosphoribosyl-N-formylglycineamide
ReactionCard
EcoCyc Reactions:
1.0Thumb+1.0Thumb ↔ 1.0Thumb+1.0Thumb+1.0Thumb
1.0N10-Formyl-THF + 1.0Glycineamideribotide ↔ 1.05'-Phosphoribosyl-N-formylglycineamide + 1.0Hydrogen ion + 1.0Tetrahydrofolic acid
ReactionCard
Metabolites:
ECMDB IDNameView
ECMDB230415'-Phospho-ribosylglycinamideMetaboCard
ECMDB013085'-Phosphoribosyl-N-formylglycineamideMetaboCard
ECMDB211765,10-MethenyltetrahydrofolateMetaboCard
ECMDB01567GlycineamideribotideMetaboCard
ECMDB21225Hydrogen ionMetaboCard
ECMDB24246N1-(5-phospho-β-D-ribosyl)glycinamideMetaboCard
ECMDB00972N10-Formyl-THFMetaboCard
ECMDB01846Tetrahydrofolic acidMetaboCard
ECMDB24261tetrahydropteroyl mono-L-glutamateMetaboCard
ECMDB00494WaterMetaboCard
GO Classification:
Function
catalytic activity
glycine hydroxymethyltransferase activity
hydroxymethyl-, formyl- and related transferase activity
methyltransferase activity
phosphoribosylglycinamide formyltransferase 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:b2500
Gene OrientationClockwise
Centisome Percentage:56.47
Left Sequence End2620256
Right Sequence End2620894
Gene Sequence:
>639 bp
ATGAATATTGTGGTGCTTATTTCCGGCAACGGAAGTAATTTACAGGCAATTATTGACGCC
TGTAAAACCAACAAAATTAAAGGCACCGTACGGGCAGTTTTCAGCAATAAGGCCGACGCG
TTCGGCCTTGAACGCGCCCGCCAGGCGGGTATTGCAACGCATACGCTCATCGCCAGCGCG
TTTGACAGTCGTGAAGCCTATGACCGGGAGTTGATTCATGAAATCGACATGTACGCACCC
GATGTGGTCGTGCTGGCTGGTTTTATGCGCATTCTCAGCCCGGCGTTTGTCTCCCACTAT
GCCGGGCGTTTGCTGAACATTCACCCTTCTCTGCTGCCGAAATATCCCGGATTACACACC
CATCGTCAGGCGCTGGAAAATGGCGATGAAGAGCACGGTACATCGGTGCATTTCGTCACC
GATGAACTGGACGGTGGCCCGGTTATTTTACAGGCGAAAGTCCCGGTATTTGCTGGTGAT
TCGGAAGATGACATCACCGCCCGCGTGCAAACCCAGGAACACGCCATTTATCCACTGGTG
ATTAGCTGGTTTGCCGATGGTCGTCTGAAAATGCACGAAAACGCCGCGTGGCTGGATGGT
CAACGTCTGCCGCCGCAGGGCTACGCTGCCGACGAGTAA
Protein Properties
Pfam Domain Function:
Protein Residues:212
Protein Molecular Weight:23238
Protein Theoretical pI:6
PDB File:1JKX
Signaling Regions:
  • None
Transmembrane Regions:
  • None
Protein Sequence:
>Phosphoribosylglycinamide formyltransferase
MNIVVLISGNGSNLQAIIDACKTNKIKGTVRAVFSNKADAFGLERARQAGIATHTLIASA
FDSREAYDRELIHEIDMYAPDVVVLAGFMRILSPAFVSHYAGRLLNIHPSLLPKYPGLHT
HRQALENGDEEHGTSVHFVTDELDGGPVILQAKVPVFAGDSEDDITARVQTQEHAIYPLV
ISWFADGRLKMHENAAWLDGQRLPPQGYAADE
References
External Links:
ResourceLink
Uniprot ID:P08179
Uniprot Name:PUR3_ECOLI
GenBank Gene ID:AF293167
Genebank Protein ID:10186029
PDB ID:1JKX
Ecogene ID:EG10799
Ecocyc:EG10799
ColiBase:b2500
Kegg Gene:b2500
EchoBASE ID:EB0792
CCDB:PUR3_ECOLI
BacMap:16130425
General Reference:
  • Almassy, R. J., Janson, C. A., Kan, C. C., Hostomska, Z. (1992). "Structures of apo and complexed Escherichia coli glycinamide ribonucleotide transformylase." Proc Natl Acad Sci U S A 89:6114-6118. Pubmed: 1631098
  • 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
  • Chen, P., Schulze-Gahmen, U., Stura, E. A., Inglese, J., Johnson, D. L., Marolewski, A., Benkovic, S. J., Wilson, I. A. (1992). "Crystal structure of glycinamide ribonucleotide transformylase from Escherichia coli at 3.0 A resolution. A target enzyme for chemotherapy." J Mol Biol 227:283-292. Pubmed: 1522592
  • Greasley, S. E., Yamashita, M. M., Cai, H., Benkovic, S. J., Boger, D. L., Wilson, I. A. (1999). "New insights into inhibitor design from the crystal structure and NMR studies of Escherichia coli GAR transformylase in complex with beta-GAR and 10-formyl-5,8,10-trideazafolic acid." Biochemistry 38:16783-16793. Pubmed: 10606510
  • 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
  • Inglese, J., Smith, J. M., Benkovic, S. J. (1990). "Active-site mapping and site-specific mutagenesis of glycinamide ribonucleotide transformylase from Escherichia coli." Biochemistry 29:6678-6687. Pubmed: 2204419
  • Pupo, G. M., Lan, R., Reeves, P. R. (2000). "Multiple independent origins of Shigella clones of Escherichia coli and convergent evolution of many of their characteristics." Proc Natl Acad Sci U S A 97:10567-10572. Pubmed: 10954745
  • Shim, J. H., Benkovic, S. J. (1999). "Catalytic mechanism of Escherichia coli glycinamide ribonucleotide transformylase probed by site-directed mutagenesis and pH-dependent studies." Biochemistry 38:10024-10031. Pubmed: 10433709
  • Smith, J. M., Daum, H. A. 3rd (1987). "Identification and nucleotide sequence of a gene encoding 5'-phosphoribosylglycinamide transformylase in Escherichia coli K12." J Biol Chem 262:10565-10569. Pubmed: 3301838
  • Su, Y., Yamashita, M. M., Greasley, S. E., Mullen, C. A., Shim, J. H., Jennings, P. A., Benkovic, S. J., Wilson, I. A. (1998). "A pH-dependent stabilization of an active site loop observed from low and high pH crystal structures of mutant monomeric glycinamide ribonucleotide transformylase at 1.8 to 1.9 A." J Mol Biol 281:485-499. Pubmed: 9698564
  • Warren, M. S., Marolewski, A. E., Benkovic, S. J. (1996). "A rapid screen of active site mutants in glycinamide ribonucleotide transformylase." Biochemistry 35:8855-8862. Pubmed: 8688421
  • 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