Phosphoribosylformylglycinamidine cyclo-ligase (P08178)

Identification
Name:Phosphoribosylformylglycinamidine cyclo-ligase
Synonyms:
  • AIR synthase
  • AIRS
  • Phosphoribosyl-aminoimidazole synthetase
Gene Name:purM
Enzyme Class:
Biological Properties
General Function:Involved in catalytic activity
Specific Function:ATP + 2-(formamido)-N(1)-(5-phospho-D- ribosyl)acetamidine = ADP + phosphate + 5-amino-1-(5-phospho-D- ribosyl)imidazole
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+1.0Thumb+2.0Thumb+1.0Thumb
1.0Adenosine triphosphate + 1.0Phosphoribosylformylglycineamidine ↔ 1.0ADP + 1.05-Aminoimidazole ribonucleotide + 2.0Hydrogen ion + 1.0Phosphate
ReactionCard
1.0Thumb+1.0Thumb ↔ 1.0Thumb+1.0Thumb+1.0Thumb
1.0Adenosine triphosphate + 1.0Phosphoribosylformylglycineamidine ↔ 1.0ADP + 1.0Phosphate + 1.05-Aminoimidazole ribonucleotide
ReactionCard
1.0Thumb+1.0Thumb → 1.0Thumb+1.0Thumb+1.0Thumb+1.0Thumb
1.0Adenosine triphosphate + 1.0Phosphoribosylformylglycineamidine → 1.0Hydrogen ion + 1.0ADP + 1.0Phosphate + 1.05-Aminoimidazole ribonucleotide
ReactionCard
SMPDB Reactions:
1.0Thumb+1.0Thumb → 1.0Thumb+1.0Thumb+1.0Adenosine diphosphate+1.0Thumb+1.0Thumb
1.02-(Formamido)-N1-(5-phospho-D-ribosyl)acetamidine + 1.0Adenosine triphosphate → 1.05-Aminoimidazole ribonucleotide + 1.0Phosphate + 1.0Adenosine diphosphate + 1.0Hydrogen ion + 1.0ADP
ReactionCard
EcoCyc Reactions:
1.0Thumb+1.0Thumb ↔ 1.0Thumb+1.0Thumb+2.0Thumb+1.0Thumb
1.0Adenosine triphosphate + 1.0Phosphoribosylformylglycineamidine ↔ 1.0ADP + 1.05-Aminoimidazole ribonucleotide + 2.0Hydrogen ion + 1.0Phosphate
ReactionCard
1.0Thumb+1.0Thumb → 1.0Thumb+1.0Thumb+1.0Thumb+1.0Thumb
1.0Adenosine triphosphate + 1.0Phosphoribosylformylglycineamidine → 1.0Hydrogen ion + 1.0ADP + 1.0Phosphate + 1.05-Aminoimidazole ribonucleotide
ReactionCard
Complex Reactions:
1.0Thumb+1.0Thumb → 1.0Thumb+1.0Thumb+1.0Thumb
1.0Adenosine triphosphate + 1.02-(Formamido)-N(1)-(5-phospho-D-ribosyl)acetamidine → 1.0ADP + 1.0Inorganic phosphate + 1.05-Aminoimidazole ribonucleotide
ReactionCard
Metabolites:
ECMDB IDNameView
ECMDB230262-(Formamido)-N(1)-(5-phospho-D-ribosyl)acetamidineMetaboCard
ECMDB240892-(Formamido)-N1-(5-phospho-D-ribosyl)acetamidineMetaboCard
ECMDB012355-Aminoimidazole ribonucleotideMetaboCard
ECMDB00538Adenosine triphosphateMetaboCard
ECMDB01341ADPMetaboCard
ECMDB21225Hydrogen ionMetaboCard
ECMDB21380Inorganic phosphateMetaboCard
ECMDB01429PhosphateMetaboCard
ECMDB00999PhosphoribosylformylglycineamidineMetaboCard
GO Classification:
Component
cell part
cytoplasm
intracellular part
Function
catalytic activity
cyclo-ligase activity
ligase activity
ligase activity, forming carbon-nitrogen bonds
phosphoribosylformylglycinamidine cyclo-ligase 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:b2499
Gene OrientationClockwise
Centisome Percentage:56.45
Left Sequence End2619219
Right Sequence End2620256
Gene Sequence:
>1038 bp
ATGGGGCAACAAAAGCAGCGTAATCGACGTTGGGTTCTGGCCTCGCGTCCACATGGCGCA
CCTGTTCCGGAGAATTTCCGTCTTGAAGAAGATGATGTCGCCACACCGGGTGAAGGACAG
GTGTTACTGCGCACAGTTTATTTGTCCCTGGACCCGTATATGCGTGGACGTATGAGCGAT
GAGCCATCTTATTCACCGCCTGTTGATATTGGCGGCGTGATGGTCGGCGGTACGGTGAGC
CGTGTCGTGGAGTCGAATCATCCTGATTATCAGTCTGGCGACTGGGTGCTGGGCTACAGT
GGATGGCAAGACTATGACATATCCAGTGGTGATGATCTGGTGAAACTTGGCGATCATCCG
CAAAATCCATCGTGGTCGCTGGGTGTGCTAGGGATGCCAGGCTTTACCGCTTATATGGGC
CTACTGGATATCGGTCAGCCTAAAGAGGGCGAAACGTTGGTGGTAGCTGCGGCGACAGGA
CCAGTGGGGGCGACGGTGGGGCAAATCGGCAAACTTAAAGGTTGCAGAGTGGTGGGGGTA
GCCGGTGGCGCGGAAAAATGCCGCCATGCTACCGAGGTGTTAGGCTTCGATGTTTGTCTT
GATCACCACGCGGATGATTTTGCCGAACAACTGGCGAAAGCGTGCCCAAAAGGTATTGAT
ATCTATTATGAAAACGTGGGCGGTAAGGTATTCGATGCGGTGCTACCGTTACTTAATACA
TCTGCGCGCATTCCCGTCTGCGGATTAGTGAGCAGCTATAACGCTACAGAGCTACCACCC
GGTCCGGATCGTTTACCTCTGTTGATGGCTACAGTGCTGAAAAAACGTATTCGCTTGCAA
GGTTTTATTATCGCTCAGGATTATGGTCACCGCATCCATGAGTTTCAGAGGGAGATGGGG
CAATGGGTGAAAGAGGATAAAATCCACTACCGCGAAGAAATTACTGACGGTTTAGAGAAT
GCGCCACAGACGTTTATCGGCCTGCTGAAGGGTAAAAACTTCGGCAAAGTGGTGATCCGC
GTGGCGGGTGATGATTAA
Protein Properties
Pfam Domain Function:
Protein Residues:345
Protein Molecular Weight:36854
Protein Theoretical pI:5
PDB File:1CLI
Signaling Regions:
  • None
Transmembrane Regions:
  • None
Protein Sequence:
>Phosphoribosylformylglycinamidine cyclo-ligase
MTDKTSLSYKDAGVDIDAGNALVGRIKGVVKKTRRPEVMGGLGGFGALCALPQKYREPVL
VSGTDGVGTKLRLAMDLKRHDTIGIDLVAMCVNDLVVQGAEPLFFLDYYATGKLDVDTAS
AVISGIAEGCLQSGCSLVGGETAEMPGMYHGEDYDVAGFCVGVVEKSEIIDGSKVSDGDV
LIALGSSGPHSNGYSLVRKILEVSGCDPQTTELDGKPLADHLLAPTRIYVKSVLELIEKV
DVHAIAHLTGGGFWENIPRVLPDNTQAVIDESSWQWPEVFNWLQTAGNVEHHEMYRTFNC
GVGMIIALPAPEVDKALALLNANGENAWKIGIIKASDSEQRVVIE
References
External Links:
ResourceLink
Uniprot ID:P08178
Uniprot Name:PUR5_ECOLI
GenBank Gene ID:AP009048
Genebank Protein ID:85674970
PDB ID:1CLI
Ecogene ID:EG10798
Ecocyc:EG10798
ColiBase:b2499
Kegg Gene:b2499
EchoBASE ID:EB0791
CCDB:PUR5_ECOLI
BacMap:16130424
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
  • Li, C., Kappock, T. J., Stubbe, J., Weaver, T. M., Ealick, S. E. (1999). "X-ray crystal structure of aminoimidazole ribonucleotide synthetase (PurM), from the Escherichia coli purine biosynthetic pathway at 2.5 A resolution." Structure 7:1155-1166. Pubmed: 10508786
  • Link, A. J., Robison, K., Church, G. M. (1997). "Comparing the predicted and observed properties of proteins encoded in the genome of Escherichia coli K-12." Electrophoresis 18:1259-1313. Pubmed: 9298646
  • Schrimsher, J. L., Schendel, F. J., Stubbe, J., Smith, J. M. (1986). "Purification and characterization of aminoimidazole ribonucleotide synthetase from Escherichia coli." Biochemistry 25:4366-4371. Pubmed: 3530323
  • Smith, J. M., Daum, H. A. 3rd (1986). "Nucleotide sequence of the purM gene encoding 5'-phosphoribosyl-5-aminoimidazole synthetase of Escherichia coli K12." J Biol Chem 261:10632-10636. Pubmed: 3015935
  • 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