Phosphoribosylaminoimidazole-succinocarboxamide synthase (P0A7D7)

Identification
Name:Phosphoribosylaminoimidazole-succinocarboxamide synthase
Synonyms:
  • SAICAR synthetase
Gene Name:purC
Enzyme Class:
Biological Properties
General Function:Involved in ATP binding
Specific Function:ATP + 5-amino-1-(5-phospho-D- ribosyl)imidazole-4-carboxylate + L-aspartate = ADP + phosphate + (S)-2-(5-amino-1-(5-phospho-D-ribosyl)imidazole-4- carboxamido)succinate
Cellular Location:Not Available
SMPDB Pathways:
  • 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
1.05-Amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate + 1.0L-Aspartic acid + 1.0Adenosine triphosphate ↔ 1.0SAICAR + 1.0ADP + 1.0Hydrogen ion + 1.0Phosphate
ReactionCard
1.0Thumb+1.0Thumb+1.0Thumb ↔ 1.0Thumb+1.0Thumb+1.0Thumb
1.0Adenosine triphosphate + 1.05-Amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate + 1.0L-Aspartic acid ↔ 1.0ADP + 1.0Phosphate + 1.0SAICAR
ReactionCard
1.0Thumb+1.0Thumb+1.0Thumb → 1.0Thumb+1.0Thumb+1.0Thumb+1.0Thumb
1.0Adenosine triphosphate + 1.05-Amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate + 1.0L-Aspartic acid → 1.0Hydrogen ion + 1.0ADP + 1.0Phosphate + 1.0SAICAR
ReactionCard
SMPDB Reactions:
1.0Thumb+1.0L-Aspartic acid+1.0Thumb+1.0Thumb → 1.0SAICAR+1.0Thumb+1.0Adenosine diphosphate+1.0Thumb+1.0Thumb+1.0Thumb
1.05-Amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate + 1.0L-Aspartic acid + 1.0Adenosine triphosphate + 1.0L-Aspartic acid → 1.0SAICAR + 1.0Phosphate + 1.0Adenosine diphosphate + 1.0Hydrogen ion + 1.0SAICAR + 1.0ADP
ReactionCard
EcoCyc Reactions:
1.0Thumb+1.0Thumb+1.0Thumb ↔ 1.0Thumb+1.0Thumb+1.0Thumb+1.0Thumb
1.05-Amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate + 1.0L-Aspartic acid + 1.0Adenosine triphosphate ↔ 1.0SAICAR + 1.0ADP + 1.0Hydrogen ion + 1.0Phosphate
ReactionCard
1.0Thumb+1.0Thumb+1.0Thumb → 1.0Thumb+1.0Thumb+1.0Thumb+1.0Thumb
1.0Adenosine triphosphate + 1.05-Amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate + 1.0L-Aspartic acid → 1.0Hydrogen ion + 1.0ADP + 1.0Phosphate + 1.0SAICAR
ReactionCard
Complex Reactions:
1.0Thumb+1.0Thumb+1.0Thumb → 1.0Thumb+1.0Thumb+1.0Thumb
1.0Adenosine triphosphate + 1.05-Amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate + 1.0L-Aspartic acid → 1.0ADP + 1.0Inorganic phosphate + 1.0SAICAR
ReactionCard
Metabolites:
ECMDB IDNameView
ECMDB062735-Amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylateMetaboCard
ECMDB00538Adenosine triphosphateMetaboCard
ECMDB01341ADPMetaboCard
ECMDB21225Hydrogen ionMetaboCard
ECMDB21380Inorganic phosphateMetaboCard
ECMDB00191L-Aspartic acidMetaboCard
ECMDB01429PhosphateMetaboCard
ECMDB00797SAICARMetaboCard
GO Classification:
Function
acid-amino acid ligase activity
adenyl nucleotide binding
adenyl ribonucleotide binding
ATP binding
binding
catalytic activity
ligase activity
ligase activity, forming carbon-nitrogen bonds
nucleoside binding
phosphoribosylaminoimidazolesuccinocarboxamide synthase activity
purine nucleoside binding
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
Gene Properties
Blattner:b2476
Gene OrientationCounterclockwise
Centisome Percentage:55.93
Left Sequence End2594927
Right Sequence End2595640
Gene Sequence:
>714 bp
ATGGAATCATACTCGCAAAACAGCAATAAATTAGATTTTCAGCACGAGGCCAGGATATTA
AACGGTATATGGCTCATTACCGCTTTAGGTTTGGTGGCAACCGCAGGACTAGCCTGGGGA
GCTAAGTATATCGAAATTACGGCAACCAAATATGATTCACCACCAATGTATGTCGCCATA
GGGTTATTATTACTTTGTATGTATGGCTTAAGTAAGGATATCAACAAGATAAATGCCGCC
ATCGCGGGCGTAATATATCTGTTTTTACTCTCTTTGGTGGCGATTGTCGTTGCAAGTTTA
GTTCCTGTATATGCCATTATCATCGTGTTCAGCACTGCGGGCGCGATGTTTTTAATCAGT
ATGCTGGCCGGTTTATTATTTAATGTTGATCCTGGTTCTCACCGTTTTATCATTATGATG
ACGTTGACAGGGTTGGCCCTGGTAATCATCGTGAATGCGGCATTAATGAGTGAACGGCCC
ATTTGGATAATAAGTTGCTTAATGATTGTGTTATGGTCAGGCATTATCTCGCATGGACGA
AATAAGCTCCTTGAATTGGCGGGGAAATGCCATAGTGAAGAGTTGTGGAGTCCGGTTCGT
TGCGCTTTTACAGGTGCATTAACACTCTATTACTATTTTATCGGCTTCTTTGGGATACTT
GCCGCGATAGCTATAACGCTTGTCTGGCAAAGGCATACGCGTTTTTTTCATTAG
Protein Properties
Pfam Domain Function:
Protein Residues:237
Protein Molecular Weight:26995
Protein Theoretical pI:5
Signaling Regions:
  • None
Transmembrane Regions:
  • None
Protein Sequence:
>Phosphoribosylaminoimidazole-succinocarboxamide synthase
MQKQAELYRGKAKTVYSTENPDLLVLEFRNDTSAGDGARIEQFDRKGMVNNKFNYFIMSK
LAEAGIPTQMERLLSDTECLVKKLDMVPVECVVRNRAAGSLVKRLGIEEGIELNPPLFDL
FLKNDAMHDPMVNESYCETFGWVSKENLARMKELTYKANDVLKKLFDDAGLILVDFKLEF
GLYKGEVVLGDEFSPDGSRLWDKETLEKMDKDRFRQSLGGLIEAYEAVARRLGVQLD
References
External Links:
ResourceLink
Uniprot ID:P0A7D7
Uniprot Name:PUR7_ECOLI
GenBank Gene ID:AP009048
Genebank Protein ID:4062344
Ecogene ID:EG10791
Ecocyc:EG10791
ColiBase:b2476
Kegg Gene:b2476
EchoBASE ID:EB0784
CCDB:PUR7_ECOLI
BacMap:16130401
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
  • Bouvier, J., Pugsley, A. P., Stragier, P. (1991). "A gene for a new lipoprotein in the dapA-purC interval of the Escherichia coli chromosome." J Bacteriol 173:5523-5531. Pubmed: 1885529
  • 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
  • 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
  • Meyer, E., Leonard, N. J., Bhat, B., Stubbe, J., Smith, J. M. (1992). "Purification and characterization of the purE, purK, and purC gene products: identification of a previously unrecognized energy requirement in the purine biosynthetic pathway." Biochemistry 31:5022-5032. Pubmed: 1534690
  • Tiedeman, A. A., DeMarini, D. J., Parker, J., Smith, J. M. (1990). "DNA sequence of the purC gene encoding 5'-phosphoribosyl-5-aminoimidazole-4-N-succinocarboxamide synthetase and organization of the dapA-purC region of Escherichia coli K-12." J Bacteriol 172:6035-6041. Pubmed: 2120198
  • 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