Phosphoribosylamine--glycine ligase (P15640)

Identification
Name:Phosphoribosylamine--glycine ligase
Synonyms:
  • GARS
  • Glycinamide ribonucleotide synthetase
  • Phosphoribosylglycinamide synthetase
Gene Name:purD
Enzyme Class:
Biological Properties
General Function:Involved in ATP binding
Specific Function:ATP + 5-phospho-D-ribosylamine + glycine = ADP + phosphate + N(1)-(5-phospho-D-ribosyl)glycinamide
Cellular Location:Not Available
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+1.0Thumb+1.0Thumb+1.0Thumb
1.0Adenosine triphosphate + 1.0Glycine + 1.05-Phosphoribosylamine ↔ 1.0ADP + 1.0Glycineamideribotide + 1.0Hydrogen ion + 1.0Phosphate
ReactionCard
1.0Thumb+1.0Thumb+1.0Thumb ↔ 1.0Thumb+1.0Thumb+1.0Thumb
1.0Adenosine triphosphate + 1.05-Phosphoribosylamine + 1.0Glycine ↔ 1.0ADP + 1.0Phosphate + 1.0Glycineamideribotide
ReactionCard
SMPDB Reactions:
1.05-Phosphoribosylamine+1.0Thumb+1.0Thumb+1.0Thumb → 1.0Thumb+1.0Thumb+1.0Adenosine diphosphate+1.0Thumb+1.0Thumb
1.05-Phosphoribosylamine + 1.0Glycine + 1.0Adenosine triphosphate + 1.05-Phosphoribosylamine → 1.0N1-(5-phospho-β-D-ribosyl)glycinamide + 1.0Phosphate + 1.0Adenosine diphosphate + 1.0Hydrogen ion + 1.0ADP
ReactionCard
EcoCyc Reactions:
1.0Thumb+1.0Thumb+1.0Thumb ↔ 1.0Thumb+1.0Thumb+1.0Thumb+1.0Thumb
1.0Adenosine triphosphate + 1.0Glycine + 1.05-Phosphoribosylamine ↔ 1.0ADP + 1.0Glycineamideribotide + 1.0Hydrogen ion + 1.0Phosphate
ReactionCard
Complex Reactions:
1.0Thumb+1.0Thumb+1.0Thumb → 1.0Thumb+1.0Thumb+1.0Thumb
1.0Adenosine triphosphate + 1.05-Phosphoribosylamine + 1.0Glycine → 1.0ADP + 1.0Inorganic phosphate + 1.05'-Phospho-ribosylglycinamide
ReactionCard
Metabolites:
ECMDB IDNameView
ECMDB230415'-Phospho-ribosylglycinamideMetaboCard
ECMDB011285-PhosphoribosylamineMetaboCard
ECMDB00538Adenosine triphosphateMetaboCard
ECMDB01341ADPMetaboCard
ECMDB00123GlycineMetaboCard
ECMDB01567GlycineamideribotideMetaboCard
ECMDB21225Hydrogen ionMetaboCard
ECMDB21380Inorganic phosphateMetaboCard
ECMDB24246N1-(5-phospho-β-D-ribosyl)glycinamideMetaboCard
ECMDB01429PhosphateMetaboCard
GO Classification:
Function
adenyl nucleotide binding
adenyl ribonucleotide binding
ATP binding
binding
catalytic activity
ligase activity
ligase activity, forming carbon-nitrogen bonds
nucleoside binding
phosphoribosylamine-glycine ligase activity
purine nucleoside binding
Process
cellular aromatic compound metabolic process
cellular metabolic process
metabolic process
nucleobase metabolic process
purine base biosynthetic process
purine base metabolic process
Gene Properties
Blattner:b4005
Gene OrientationCounterclockwise
Centisome Percentage:90.58
Left Sequence End4202665
Right Sequence End4203954
Gene Sequence:
>1290 bp
ATGTCGGATGACAAATTTGATGCCATTGTGGTCGGTGCGGGCGTTGCTGGTAGCGTTGCC
GCACTGGTCATGGCACGAGCCGGGCTGGATGTCCTGGTGATAGAACGCGGCGACAGTGCC
GGATGTAAAAACATGACCGGCGGGCGTCTTTATGCCCACACACTTGAAGCAATCATTCCA
GGCTTTGCAGTATCAGCGCCGGTAGAACGCAAGGTCACACGCGAGAAAATCTCCTTCTTA
ACCGAAGAAAGCGCCGTTACCCTCGATTTTCACCGCGAGCAGCCAGATGTTCCGCAACAC
GCATCTTATACCGTATTGCGTAATCGTCTGGACCCGTGGTTGATGGAACAAGCCGAGCAG
GCGGGCGCGCAGTTTATCCCAGGCGTTCGCGTCGACGCGCTGGTTCGTGAAGGAAACAAG
GTCACTGGCGTGCAGGCTGGGGATGATATTCTCGAAGCGAATGTGGTGATTCTGGCTGAT
GGCGTTAACTCGATGCTTGGCCGCTCGCTGGGAATGGTTCCCGCTTCCGATCCGCATCAT
TACGCTGTTGGTGTTAAAGAGGTTATTGGCCTCACACCAGAACAGATCAACGATCGCTTT
AATATTACGGGCGAGGAAGGTGCCGCCTGGCTGTTTGCCGGTTCCCCTTCTGACGGCCTG
ATGGGCGGGGGATTTCTCTATACCAACAAGGATTCCATATCCTTGGGGCTGGTTTGTGGA
TTGGGTGATATCGCCCATGCGCAAAAAAGCGTGCCGCAAATGCTGGAAGATTTTAAACAA
CACCCCGCCATTCGCCCGCTGATTAGCGGCGGCAAACTGCTTGAATATTCCGCGCATATG
GTGCCGGAAGGCGGTCTGGCAATGGTGCCGCAACTGGTTAACGAGGGCGTGATGATCGTT
GGTGACGCCGCAGGCTTCTGCCTGAATTTGGGTTTTACGGTCCGCGGCATGGATTTAGCC
ATTGCATCGGCTCAGGCTGCCGCCACAACGGTGATCGCCGCCAAAGAACGCGCGGATTTC
TCCGCCAGCAGTCTGGCGCAATACAAACGTGAGCTGGAACAAAGCTGCGTCATGCGTGAT
ATGCAGCATTTTCGCAAGATCCCGGCGCTGATGGAAAACCCGCGCCTGTTTAGCCAATAC
CCACGAATGGTAGCCGACATCATGAACGAGATGTTCACCATCGACGGCAAACCAAACCAG
CCGGTACGAAAAATGATCATGGGACATGCGAAGAAAATTGGGCTGATCAACTTGCTGAAA
GATGGCATTAAGGGAGCAACCGCGCTATGA
Protein Properties
Pfam Domain Function:
Protein Residues:429
Protein Molecular Weight:45940
Protein Theoretical pI:5
PDB File:1GSO
Signaling Regions:
  • None
Transmembrane Regions:
  • None
Protein Sequence:
>Phosphoribosylamine--glycine ligase
MKVLVIGNGGREHALAWKAAQSPLVETVFVAPGNAGTALEPALQNVAIGVTDIPALLDFA
QNEKIDLTIVGPEAPLVKGVVDTFRAAGLKIFGPTAGAAQLEGSKAFTKDFLARHKIPTA
EYQNFTEVEPALAYLREKGAPIVIKADGLAAGKGVIVAMTLEEAEAAVHDMLAGNAFGDA
GHRIVIEEFLDGEEASFIVMVDGEHVLPMATSQDHKRVGDKDTGPNTGGMGAYSPAPVVT
DDVHQRTMERIIWPTVKGMAAEGNTYTGFLYAGLMIDKQGNPKVIEFNCRFGDPETQPIM
LRMKSDLVELCLAACESKLDEKTSEWDERASLGVVMAAGGYPGDYRTGDVIHGLPLEEVA
GGKVFHAGTKLADDEQVVTNGGRVLCVTALGHTVAEAQKRAYALMTDIHWDDCFCRKDIG
WRAIEREQN
References
External Links:
ResourceLink
Uniprot ID:P15640
Uniprot Name:PUR2_ECOLI
GenBank Gene ID:AP009048
Genebank Protein ID:1742778
PDB ID:1GSO
Ecogene ID:EG10792
Ecocyc:EG10792
ColiBase:b4005
Kegg Gene:b4005
EchoBASE ID:EB0785
CCDB:PUR2_ECOLI
BacMap:16131835
General Reference:
  • Aiba, A., Mizobuchi, K. (1989). "Nucleotide sequence analysis of genes purH and purD involved in the de novo purine nucleotide biosynthesis of Escherichia coli." J Biol Chem 264:21239-21246. Pubmed: 2687276
  • Blattner, F. R., Burland, V., Plunkett, G. 3rd, Sofia, H. J., Daniels, D. L. (1993). "Analysis of the Escherichia coli genome. IV. DNA sequence of the region from 89.2 to 92.8 minutes." Nucleic Acids Res 21:5408-5417. Pubmed: 8265357
  • 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
  • Cheng, Y. S., Shen, Y., Rudolph, J., Stern, M., Stubbe, J., Flannigan, K. A., Smith, J. M. (1990). "Glycinamide ribonucleotide synthetase from Escherichia coli: cloning, overproduction, sequencing, isolation, and characterization." Biochemistry 29:218-227. Pubmed: 2182115
  • 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
  • Wang, W., Kappock, T. J., Stubbe, J., Ealick, S. E. (1998). "X-ray crystal structure of glycinamide ribonucleotide synthetase from Escherichia coli." Biochemistry 37:15647-15662. Pubmed: 9843369