Identification
Name:Phosphoribosylformylglycinamidine synthase
Synonyms:
  • FGAM synthase
  • FGAMS
  • Formylglycinamide ribotide amidotransferase
  • FGARAT
  • Formylglycinamide ribotide synthetase
Gene Name:purL
Enzyme Class:
Biological Properties
General Function:Involved in catalytic activity
Specific Function:ATP + N(2)-formyl-N(1)-(5-phospho-D- ribosyl)glycinamide + L-glutamine + H(2)O = ADP + phosphate + 2- (formamido)-N(1)-(5-phospho-D-ribosyl)acetamidine + L-glutamate
Cellular Location:Cytoplasm
SMPDB Pathways:
  • 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+1.0Thumb1.0Thumb+1.0Thumb+1.0Thumb+1.0Thumb+1.0Thumb
1.0Thumb+1.0Thumb+1.0Thumb+1.0Thumb1.0Thumb+1.0Thumb+1.0Thumb+1.0Thumb
SMPDB Reactions:
1.05'-Phosphoribosyl-N-formylglycinamide+1.0Thumb+1.0Thumb+1.0Thumb+1.0Thumb1.0Thumb+1.0L-Glutamic acid+1.0Thumb+1.0Adenosine diphosphate+1.0Thumb+1.0Thumb+1.0Thumb
1.05'-Phosphoribosyl-N-formylglycinamide + 1.0Water + 1.0L-Glutamine + 1.0Adenosine triphosphate + 1.05'-Phosphoribosyl-N-formylglycineamide → 1.02-(Formamido)-N1-(5-phospho-D-ribosyl)acetamidine + 1.0L-Glutamic acid + 1.0Phosphate + 1.0Adenosine diphosphate + 1.0Hydrogen ion + 1.0L-Glutamate + 1.0ADP
ReactionCard
EcoCyc Reactions:
1.0Thumb+1.0Thumb+1.0Thumb+1.0Thumb1.0Thumb+1.0Thumb+1.0Thumb+1.0Thumb+1.0Thumb
1.0Thumb+1.0Thumb+1.0Thumb+1.0Thumb1.0Thumb+1.0Thumb+1.0Thumb+1.0Thumb
1.0Thumb+1.0Thumb+1.0Thumb+1.0Thumb1.0Thumb+1.0Thumb+1.0Thumb+1.0Thumb+1.0Thumb
Metabolites:
ECMDB IDNameView
ECMDB230262-(Formamido)-N(1)-(5-phospho-D-ribosyl)acetamidineMetaboCard
ECMDB240892-(Formamido)-N1-(5-phospho-D-ribosyl)acetamidineMetaboCard
ECMDB013085'-Phosphoribosyl-N-formylglycineamideMetaboCard
ECMDB00538Adenosine triphosphateMetaboCard
ECMDB01341ADPMetaboCard
ECMDB21225Hydrogen ionMetaboCard
ECMDB21380Inorganic phosphateMetaboCard
ECMDB00148L-GlutamateMetaboCard
ECMDB00641L-GlutamineMetaboCard
ECMDB01429PhosphateMetaboCard
ECMDB00999PhosphoribosylformylglycineamidineMetaboCard
ECMDB00494WaterMetaboCard
GO Classification:
Function
carbon-nitrogen ligase activity, with glutamine as amido-N-donor
catalytic activity
ligase activity
ligase activity, forming carbon-nitrogen bonds
phosphoribosylformylglycinamidine synthase activity
Process
'de novo' IMP 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:b2557
Gene OrientationCounterclockwise
Centisome Percentage:57.97
Left Sequence End2689678
Right Sequence End2693565
Gene Sequence:
>3888 bp
ATGATGGAAATTCTGCGTGGTTCGCCTGCACTGTCGGCATTCCGAATCAACAAACTGCTG
GCACGTTTTCAGGCTGCCAGGCTCCCGGTTCACAATATTTACGCCGAGTATGTCCATTTT
GCTGACCTCAATGCGCCGTTAAACGATGATGAGCACGCACAACTTGAACGCCTGCTGAAA
TATGGCCCGGCACTCGCCAGCCACGCCCCGCAAGGCAAACTCCTGCTGGTGACCCCGCGT
CCTGGCACCATCTCTCCCTGGTCTTCGAAAGCGACCGATATTGCCCATAACTGCGGGCTA
CAACAGGTAAACCGCCTTGAGCGCGGCGTTGCTTACTATATAGAAGCCGGTACGCTGACC
AATGAACAATGGCAGCAGGTTACCGCTGAACTGCACGACCGCATGATGGAAACGGTCTTT
TTTGCTTTAGATGATGCAGAGCAGTTGTTTGCCCACCATCAACCGACTCCGGTTACCAGC
GTTGATTTGCTGGGGCAGGGCCGTCAGGCGCTGATCGACGCTAACCTGCGTCTTGGCTTG
GCTCTGGCGGAAGATGAAATTGACTATCTGCAGGATGCTTTCACAAAGCTTGGTCGTAAC
CCGAACGACATCGAACTGTATATGTTTGCCCAGGCGAACTCCGAGCACTGCCGCCACAAA
ATTTTTAACGCCGACTGGGTTATCGATGGTGAACAGCAGCCGAAATCGCTGTTCAAGATG
ATCAAAAATACTTTCGAAACCACGCCAGATCACGTTCTCTCTGCTTATAAAGATAACGCC
GCCGTAATGGAAGGTTCTGAAGTGGGCCGCTACTTTGCTGACCACGAAACGGGCCGCTAC
GATTTCCATCAGGAACCGGCGCATATTCTGATGAAAGTCGAAACTCACAACCACCCGACG
GCGATTTCTCCGTGGCCGGGCGCGGCGACCGGTTCCGGCGGTGAAATCCGCGATGAAGGT
GCCACCGGGCGCGGCGCAAAGCCGAAAGCGGGTCTGGTTGGTTTCTCCGTTTCCAACCTG
CGAATTCCTGGCTTCGAACAGCCGTGGGAAGAAGATTTCGGTAAGCCTGAGCGCATTGTC
ACCGCGCTGGACATCATGACCGAAGGCCCGCTGGGCGGCGCGGCGTTTAACAACGAATTT
GGTCGTCCGGCACTGAACGGCTACTTCCGTACTTATGAAGAAAAAGTGAACAGCCACAAC
GGCGAAGAGCTGCGCGGTTATCACAAACCGATCATGCTGGCGGGCGGGATCGGCAACATT
CGCGCCGATCACGTACAAAAAGGCGAGATCAACGTCGGTGCGAAGCTGGTCGTTCTCGGC
GGCCCGGCAATGAACATCGGTCTTGGCGGTGGTGCAGCGTCTTCTATGGCGTCTGGTCAG
TCTGATGCCGACCTCGACTTTGCTTCCGTACAGCGCGACAACCCGGAGATGGAGCGTCGC
TGCCAGGAAGTGATCGACCGTTGCTGGCAGCTTGGTGATGCCAACCCAATCCTGTTTATC
CACGACGTTGGCGCTGGCGGTCTTTCTAACGCCATGCCGGAACTGGTGAGCGACGGCGGG
CGCGGCGGTAAATTTGAACTGCGCGAGATTCTAAGCGACGAACCGGGCATGAGCCCGCTG
GAAATCTGGTGTAACGAATCCCAGGAACGCTACGTGCTGGCGGTTGCTGCCGATCAATTA
CCGCTGTTTGACGAACTGTGTAAGCGTGAGCGCGCACCCTACGCGGTGATTGGTGAAGCG
ACCGAAGAACTGCATCTTTCTCTGCACGATCGTCATTTTGATAATCAGCCGATCGATCTG
CCGCTGGACGTCCTGCTTGGTAAAACGCCGAAGATGACCCGCGATGTACAAACGCTGAAA
GCGAAAGGCGACGCGCTGGCCCGTGAAGGGATCACCATTGCAGACGCGGTGAAACGTGTG
CTGCATCTGCCGACTGTGGCGGAAAAAACCTTCCTGGTGACCATTGGCGACCGCAGCGTA
ACCGGCATGGTAGCGCGCGATCAGATGGTGGGGCCGTGGCAGGTGCCGGTCGCTAACTGC
GCGGTCACTACCGCCAGCCTCGACAGCTACTACGGTGAAGCGATGGCGATTGGCGAGCGT
GCGCCGGTTGCGCTGCTGGATTTCGCCGCCTCTGCCCGTCTGGCGGTCGGTGAAGCGTTA
ACCAACATCGCCGCAACACAAATTGGCGATATCAAACGCATCAAACTTTCCGCCAACTGG
ATGGCGGCGGCAGGCCACCCTGGTGAAGATGCGGGCCTGTATGAAGCCGTTAAAGCCGTG
GGCGAAGAGCTTTGTCCGGCGCTGGGCCTGACGATCCCGGTGGGTAAAGACTCCATGTCG
ATGAAAACCCGCTGGCAGGAAGGTAACGAAGAGCGCGAAATGACGTCGCCGCTGTCGCTG
GTGATTTCTGCATTTGCCCGCGTGGAAGATGTACGTCACACCATCACGCCGCAGCTTTCT
ACCGAAGATAACGCACTGCTGCTGATTGATTTGGGCAAAGGCAATAACGCGCTGGGCGCA
ACGGCGCTGGCGCAGGTTTATCGTCAGCTTGGCGACAAACCGGCAGATGTACGCGATGTC
GCGCAACTGAAAGGCTTCTATGACGCGATTCAGGCGCTGGTTGCACAGCGTAAGCTGCTG
GCGTATCACGACCGCTCTGATGGCGGCCTGCTGGTAACGCTGGCGGAAATGGCCTTTGCT
GGTCATTGTGGCATTGACGCGGATATCGCCACTCTGGGTGACGATCGCCTGGCGGCGTTG
TTTAACGAAGAACTGGGTGCGGTGATTCAGGTTCGTGCCGCTGACCGTGAAGCGGTCGAG
TCCGTACTGGCACAGCATGGGCTTGCTGATTGTGTCCATTATGTAGGGCAGGCGGTTTCC
GGTGACCGTTTTGTGATTACCGCCAACGGGCAGACTGTATTCAGCGAAAGCCGCACCACG
TTGCGTGTCTGGTGGGCAGAAACTACCTGGCAGATGCAGCGCCTGCGTGACAACCCGGAG
TGTGCCGATCAGGAGCATCAGGCGAAATCTAACGACGCCGATCCGGGCCTGAATGTAAAA
CTGTCGTTCGATATCAACGAAGATGTGGCAGCACCGTATATTGCCACTGGCGCACGTCCG
AAAGTTGCCGTACTGCGTGAGCAGGGCGTGAACTCGCATGTTGAAATGGCGGCAGCTTTC
CACCGTGCAGGCTTTGATGCTATCGACGTGCATATGAGTGACCTGCTGACCGGACGCACG
GGCCTGGAAGATTTCCACGCCCTGGTCGCGTGCGGTGGTTTCTCCTACGGTGATGTGCTG
GGTGCCGGTGAAGGTTGGGCGAAGTCAATCCTGTTCAATGACCGTGTACGCGATGAGTTT
GCAACCTTCTTCCACCGTCCGCAAACGCTGGCGCTGGGGGTATGTAACGGTTGCCAGATG
ATGTCTAATCTGCGTGAACTGATCCCAGGTAGTGAGTTGTGGCCACGTTTTGTGCGCAAT
ACCTCCGATCGCTTTGAAGCGCGTTTCAGCCTGGTTGAAGTAACCCAAAGCCCGTCTCTG
CTGTTGCAGGGGATGGTGGGCTCGCAAATGCCGATTGCTGTCTCTCATGGTGAAGGGCGC
GTGGAAGTGCGTGATGCGGCGCATCTGGCGGCACTGGAAAGCAAAGGGCTGGTGGCACTG
CGCTATGTCGATAACTTCGGCAAAGTCACTGAAACCTACCCGGCTAACCCGAACGGTTCA
CCGAACGGTATTACGGCAGTCACGACTGAAAGTGGTCGAGTCACCATTATGATGCCGCAC
CCGGAACGTGTTTTCCGTACTGTCAGCAACTCCTGGCATCCGGAAAACTGGGGCGAGGAT
GGCCCATGGATGCGCATTTTCCGCAATGCGCGTAAGCAGTTGGGGTAA
Protein Properties
Pfam Domain Function:
Protein Residues:1295
Protein Molecular Weight:141402
Protein Theoretical pI:5
PDB File:1T3T
Signaling Regions:
  • None
Transmembrane Regions:
  • None
Protein Sequence:
>Phosphoribosylformylglycinamidine synthase
MMEILRGSPALSAFRINKLLARFQAARLPVHNIYAEYVHFADLNAPLNDDEHAQLERLLK
YGPALASHAPQGKLLLVTPRPGTISPWSSKATDIAHNCGLQQVNRLERGVAYYIEAGTLT
NEQWQQVTAELHDRMMETVFFALDDAEQLFAHHQPTPVTSVDLLGQGRQALIDANLRLGL
ALAEDEIDYLQDAFTKLGRNPNDIELYMFAQANSEHCRHKIFNADWVIDGEQQPKSLFKM
IKNTFETTPDHVLSAYKDNAAVMEGSEVGRYFADHETGRYDFHQEPAHILMKVETHNHPT
AISPWPGAATGSGGEIRDEGATGRGAKPKAGLVGFSVSNLRIPGFEQPWEEDFGKPERIV
TALDIMTEGPLGGAAFNNEFGRPALNGYFRTYEEKVNSHNGEELRGYHKPIMLAGGIGNI
RADHVQKGEINVGAKLVVLGGPAMNIGLGGGAASSMASGQSDADLDFASVQRDNPEMERR
CQEVIDRCWQLGDANPILFIHDVGAGGLSNAMPELVSDGGRGGKFELREILSDEPGMSPL
EIWCNESQERYVLAVAADQLPLFDELCKRERAPYAVIGEATEELHLSLHDRHFDNQPIDL
PLDVLLGKTPKMTRDVQTLKAKGDALAREGITIADAVKRVLHLPTVAEKTFLVTIGDRSV
TGMVARDQMVGPWQVPVANCAVTTASLDSYYGEAMAIGERAPVALLDFAASARLAVGEAL
TNIAATQIGDIKRIKLSANWMAAAGHPGEDAGLYEAVKAVGEELCPALGLTIPVGKDSMS
MKTRWQEGNEEREMTSPLSLVISAFARVEDVRHTITPQLSTEDNALLLIDLGKGNNALGA
TALAQVYRQLGDKPADVRDVAQLKGFYDAIQALVAQRKLLAYHDRSDGGLLVTLAEMAFA
GHCGIDADIATLGDDRLAALFNEELGAVIQVRAADREAVESVLAQHGLADCVHYVGQAVS
GDRFVITANGQTVFSESRTTLRVWWAETTWQMQRLRDNPECADQEHQAKSNDADPGLNVK
LSFDINEDVAAPYIATGARPKVAVLREQGVNSHVEMAAAFHRAGFDAIDVHMSDLLTGRT
GLEDFHALVACGGFSYGDVLGAGEGWAKSILFNDRVRDEFATFFHRPQTLALGVCNGCQM
MSNLRELIPGSELWPRFVRNTSDRFEARFSLVEVTQSPSLLLQGMVGSQMPIAVSHGEGR
VEVRDAAHLAALESKGLVALRYVDNFGKVTETYPANPNGSPNGITAVTTESGRVTIMMPH
PERVFRTVSNSWHPENWGEDGPWMRIFRNARKQLG
References
External Links:
ResourceLink
Uniprot ID:P15254
Uniprot Name:PUR4_ECOLI
GenBank Gene ID:AP009048
Genebank Protein ID:85675448
PDB ID:1T3T
Ecogene ID:EG10797
Ecocyc:EG10797
ColiBase:b2557
Kegg Gene:b2557
EchoBASE ID:EB0790
CCDB:PUR4_ECOLI
BacMap:49176239
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
  • Riley, M., Abe, T., Arnaud, M. B., Berlyn, M. K., Blattner, F. R., Chaudhuri, R. R., Glasner, J. D., Horiuchi, T., Keseler, I. M., Kosuge, T., Mori, H., Perna, N. T., Plunkett, G. 3rd, Rudd, K. E., Serres, M. H., Thomas, G. H., Thomson, N. R., Wishart, D., Wanner, B. L. (2006). "Escherichia coli K-12: a cooperatively developed annotation snapshot--2005." Nucleic Acids Res 34:1-9. Pubmed: 16397293
  • Sampei, G., Mizobuchi, K. (1989). "The organization of the purL gene encoding 5'-phosphoribosylformylglycinamide amidotransferase of Escherichia coli." J Biol Chem 264:21230-21238. Pubmed: 2531746
  • Schendel, F. J., Mueller, E., Stubbe, J., Shiau, A., Smith, J. M. (1989). "Formylglycinamide ribonucleotide synthetase from Escherichia coli: cloning, sequencing, overproduction, isolation, and characterization." Biochemistry 28:2459-2471. Pubmed: 2659070