Phosphoribosylglycinamide formyltransferase 2 (P33221)

Identification
Name:Phosphoribosylglycinamide formyltransferase 2
Synonyms:
  • GART 2
  • 5'-phosphoribosylglycinamide transformylase 2
  • Formate-dependent GAR transformylase
  • GAR transformylase 2
Gene Name:purT
Enzyme Class:
Biological Properties
General Function:Involved in ATP binding
Specific Function:Catalyzes two reactions:the first one is the production of beta-formyl glycinamide ribonucleotide (GAR) from formate, ATP and beta GAR; the second, a side reaction, is the production of acetyl phosphate and ADP from acetate and ATP
Cellular Location:Not Available
SMPDB Pathways:
  • One Carbon Pool by Folate I PW001735
  • One carbon pool by folate PW000773
  • Thiamin diphosphate biosynthesis PW002028
  • purine nucleotides de novo biosynthesis PW000910
  • purine nucleotides de novo biosynthesis 1435709748 PW000960
  • purine nucleotides de novo biosynthesis 2 PW002033
KEGG Pathways:
KEGG Reactions:
1.0Thumb+1.0Thumb ↔ 1.0Thumb+1.0Thumb
1.0Acetic acid + 1.0Adenosine triphosphate ↔ 1.0Acetylphosphate + 1.0ADP
ReactionCard
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:
1.0Tetrahydrofolic acid+1.05'-Phosphoribosyl-N-formylglycinamide+1.0Thumb+1.0Thumb → 1.0Thumb+1.0Thumb+1.0Glycineamideribotide+1.0Thumb
1.0Tetrahydrofolic acid + 1.05'-Phosphoribosyl-N-formylglycinamide + 1.0Tetrahydrofolic acid + 1.05'-Phosphoribosyl-N-formylglycineamide → 1.0Water + 1.05,10-Methenyltetrahydrofolic acid + 1.0Glycineamideribotide + 1.0Glycineamideribotide
ReactionCard
1.0Tetrahydrofolic acid+1.05'-Phosphoribosyl-N-formylglycinamide+1.0Thumb+1.0Thumb → 1.010-Formyltetrahydrofolate+1.0Glycineamideribotide+1.0Thumb+1.0Thumb
1.0Tetrahydrofolic acid + 1.05'-Phosphoribosyl-N-formylglycinamide + 1.0Tetrahydrofolic acid + 1.05'-Phosphoribosyl-N-formylglycineamide → 1.010-Formyltetrahydrofolate + 1.0Glycineamideribotide + 1.0N10-Formyl-THF + 1.0Glycineamideribotide
ReactionCard
1.0Thumb+1.0Tetrahydrofolic acid+1.0Thumb → 1.0Thumb+1.0Glycineamideribotide+1.0Thumb+1.0Thumb
1.05'-phosphoribosyl-a-N-formylglycineamidine + 1.0Tetrahydrofolic acid + 1.0Tetrahydrofolic acid → 1.0Water + 1.0Glycineamideribotide + 1.05,10-Methenyltetrahydrofolic acid + 1.0Glycineamideribotide
ReactionCard
1.0Thumb+1.0Thumb+1.0Thumb → 1.05'-Phosphoribosyl-N-formylglycinamide+1.0Adenosine diphosphate+1.0Thumb+1.0Thumb+1.0Thumb+1.0Thumb
1.0N1-(5-phospho-β-D-ribosyl)glycinamide + 1.0Adenosine triphosphate + 1.0Formic acid → 1.05'-Phosphoribosyl-N-formylglycinamide + 1.0Adenosine diphosphate + 1.0Phosphate + 1.0Hydrogen ion + 1.05'-Phosphoribosyl-N-formylglycineamide + 1.0ADP
ReactionCard
EcoCyc Reactions:
1.0Thumb+1.0Thumb ↔ 1.0Thumb+1.0Thumb
1.0Acetic acid + 1.0Adenosine triphosphate ↔ 1.0Acetylphosphate + 1.0ADP
ReactionCard
1.0Thumb+1.0Thumb+1.0Thumb → 1.0Thumb+1.0Thumb+1.0Thumb+1.0Thumb
1.0Adenosine triphosphate + 1.0Formic acid + 1.0Glycineamideribotide → 1.0ADP + 1.05'-Phosphoribosyl-N-formylglycineamide + 1.0Hydrogen ion + 1.0Phosphate
ReactionCard
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
Complex Reactions:
1.0Thumb+1.0Thumb+1.0Thumb → 1.0Thumb+1.0Thumb+1.0Thumb
1.0Formic acid + 1.0Adenosine triphosphate + 1.05'-Phospho-ribosylglycinamide → 1.05'-Phosphoribosyl-N-formylglycineamide + 1.0ADP + 1.0Pyrophosphate
ReactionCard
Metabolites:
ECMDB IDNameView
ECMDB230415'-Phospho-ribosylglycinamideMetaboCard
ECMDB240785'-phosphoribosyl-a-N-formylglycineamidineMetaboCard
ECMDB013085'-Phosphoribosyl-N-formylglycineamideMetaboCard
ECMDB211765,10-MethenyltetrahydrofolateMetaboCard
ECMDB240675,10-Methenyltetrahydrofolic acidMetaboCard
ECMDB00042Acetic acidMetaboCard
ECMDB01494AcetylphosphateMetaboCard
ECMDB00538Adenosine triphosphateMetaboCard
ECMDB01341ADPMetaboCard
ECMDB00142Formic acidMetaboCard
ECMDB01567GlycineamideribotideMetaboCard
ECMDB21225Hydrogen ionMetaboCard
ECMDB24246N1-(5-phospho-β-D-ribosyl)glycinamideMetaboCard
ECMDB00972N10-Formyl-THFMetaboCard
ECMDB01429PhosphateMetaboCard
ECMDB04142PyrophosphateMetaboCard
ECMDB01846Tetrahydrofolic acidMetaboCard
ECMDB00494WaterMetaboCard
GO Classification:
Function
adenyl nucleotide binding
adenyl ribonucleotide binding
ATP binding
binding
catalytic activity
cation binding
glycine hydroxymethyltransferase activity
hydroxymethyl-, formyl- and related transferase activity
ion binding
magnesium ion binding
metal ion binding
methyltransferase activity
nucleoside binding
purine nucleoside binding
transferase activity
transferase activity, transferring one-carbon groups
Process
cellular nitrogen compound metabolic 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 nucleotide biosynthetic process
purine nucleotide metabolic process
purine ribonucleotide biosynthetic process
Gene Properties
Blattner:b1849
Gene OrientationClockwise
Centisome Percentage:41.57
Left Sequence End1928905
Right Sequence End1930083
Gene Sequence:
>1179 bp
ATGATCTGGATAATGACGATGGCTCGCCGTATGAACGGTGTTTACGCGGCATTTATGCTG
GTCGCTTTTATGATGGGGGTGGCCGGGGCGCTACAGGCTCCTACATTGAGCTTATTTCTG
AGTCGTGAGGTTGGCGCGCAACCTTTCTGGATCGGCCTCTTTTATACGGTGAATGCTATT
GCTGGGATCGGCGTAAGCCTCTGGTTGGCAAAACGTTCTGACAGTCAGGGCGATCGGCGA
AAACTGATTATATTTTGCTGTTTGATGGCTATCGGCAATGCGCTATTGTTTGCATTTAAT
CGTCATTATCTGACGCTTATCACCTGTGGTGTGCTTCTGGCATCTCTGGCCAATACGGCA
ATGCCACAGTTATTTGCTCTGGCGCGGGAATATGCGGATAACTCGGCGCGAGAAGTGGTG
ATGTTTAGCTCGGTGATGCGTGCGCAGCTTTCTCTGGCATGGGTTATCGGTCCACCGTTG
GCCTTTATGCTGGCGTTGAATTACGGCTTTACGGTGATGTTTTCGATTGCCGCCGGGATA
TTCACACTCAGTCTGGTATTGATTGCATTTATGCTTCCGTCTGTGGCGCGGGTAGAACTG
CCGTCGGAAAATGCTTTATCAATGCAAGGTGGCTGGCAGGATAGTAACGTACGGATGTTA
TTTGTCGCCTCGACGTTAATGTGGACCTGCAACACCATGTACATTATTGATATGCCGTTG
TGGATCAGTAGCGAGTTAGGATTGCCAGACAAACTGGCGGGTTTCCTGATGGGGACGGCA
GCTGGACTGGAAATACCAGCAATGATTCTGGCTGGCTACTATGTCAAACGTTATGGTAAG
CGGCGAATGATGGTCATAGCAGTGGCGGCAGGAGTACTGTTTTACACCGGATTGATTTTC
TTTAATAGCCGTATGGCGTTGATGACGCTGCAACTTTTTAACGCTGTATTTATCGGCATT
GTTGCGGGTATTGGGATGCTATGGTTTCAGGATTTAATGCCTGGAAGAGCGGGGGCAGCT
ACCACCTTATTTACTAACAGTATTTCTACCGGGGTAATTCTGGCTGGCGTTATTCAGGGA
GCAATTGCACAAAGTTGGGGGCACTTTGCTGTCTACTGGGTAATTGCGGTTATTTCTGTT
GTCGCATTATTTTTAACCGCAAAGGTTAAAGACGTTTGA
Protein Properties
Pfam Domain Function:
Protein Residues:392
Protein Molecular Weight:42433
Protein Theoretical pI:5
PDB File:1EZ1
Signaling Regions:
  • None
Transmembrane Regions:
  • None
Protein Sequence:
>Phosphoribosylglycinamide formyltransferase 2
MTLLGTALRPAATRVMLLGSGELGKEVAIECQRLGVEVIAVDRYADAPAMHVAHRSHVIN
MLDGDALRRVVELEKPHYIVPEIEAIATDMLIQLEEEGLNVVPCARATKLTMNREGIRRL
AAEELQLPTSTYRFADSESLFREAVADIGYPCIVKPVMSSSGKGQTFIRSAEQLAQAWKY
AQQGGRAGAGRVIVEGVVKFDFEITLLTVSAVDGVHFCAPVGHRQEDGDYRESWQPQQMS
PLALERAQEIARKVVLALGGYGLFGVELFVCGDEVIFSEVSPRPHDTGMVTLISQDLSEF
ALHVRAFLGLPVGGIRQYGPAASAVILPQLTSQNVTFDNVQNAVGADLQIRLFGKPEIDG
SRRLGVALATAESVVDAIERAKHAAGQVKVQG
References
External Links:
ResourceLink
Uniprot ID:P33221
Uniprot Name:PURT_ECOLI
GenBank Gene ID:AP009048
Genebank Protein ID:85674315
PDB ID:1EZ1
Ecogene ID:EG11809
Ecocyc:EG11809
ColiBase:b1849
Kegg Gene:b1849
EchoBASE ID:EB1757
CCDB:PURT_ECOLI
BacMap:16129802
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
  • 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
  • Itoh, T., Aiba, H., Baba, T., Hayashi, K., Inada, T., Isono, K., Kasai, H., Kimura, S., Kitakawa, M., Kitagawa, M., Makino, K., Miki, T., Mizobuchi, K., Mori, H., Mori, T., Motomura, K., Nakade, S., Nakamura, Y., Nashimoto, H., Nishio, Y., Oshima, T., Saito, N., Sampei, G., Seki, Y., Horiuchi, T., et, a. l. .. (1996). "A 460-kb DNA sequence of the Escherichia coli K-12 genome corresponding to the 40.1-50.0 min region on the linkage map." DNA Res 3:379-392. Pubmed: 9097040
  • Marolewski, A., Smith, J. M., Benkovic, S. J. (1994). "Cloning and characterization of a new purine biosynthetic enzyme: a non-folate glycinamide ribonucleotide transformylase from E. coli." Biochemistry 33:2531-2537. Pubmed: 8117714
  • Thoden, J. B., Firestine, S. M., Benkovic, S. J., Holden, H. M. (2002). "PurT-encoded glycinamide ribonucleotide transformylase. Accommodation of adenosine nucleotide analogs within the active site." J Biol Chem 277:23898-23908. Pubmed: 11953435
  • Thoden, J. B., Firestine, S., Nixon, A., Benkovic, S. J., Holden, H. M. (2000). "Molecular structure of Escherichia coli PurT-encoded glycinamide ribonucleotide transformylase." Biochemistry 39:8791-8802. Pubmed: 10913290
  • Zhang, J., Sprung, R., Pei, J., Tan, X., Kim, S., Zhu, H., Liu, C. F., Grishin, N. V., Zhao, Y. (2009). "Lysine acetylation is a highly abundant and evolutionarily conserved modification in Escherichia coli." Mol Cell Proteomics 8:215-225. Pubmed: 18723842