Adenylosuccinate synthetase (P0A7D4)

Identification
Name:Adenylosuccinate synthetase
Synonyms:
  • AMPSase
  • AdSS
  • IMP--aspartate ligase
Gene Name:purA
Enzyme Class:
Biological Properties
General Function:Involved in adenylosuccinate synthase activity
Specific Function:Plays an important role in the de novo pathway of purine nucleotide biosynthesis. Catalyzes the first commited step in the biosynthesis of AMP from IMP
Cellular Location:Cytoplasm
SMPDB Pathways:
  • Aspartate metabolism PW000787
  • 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+2.0Thumb+1.0Thumb
1.0L-Aspartic acid + 1.0Guanosine triphosphate + 1.0Inosinic acid ↔ 1.0Adenylsuccinic acid + 1.0Guanosine diphosphate + 2.0Hydrogen ion + 1.0Phosphate
ReactionCard
1.0Thumb+1.0Thumb+1.0Thumb ↔ 1.0Thumb+1.0Thumb+1.0Thumb
1.0Guanosine triphosphate + 1.0Inosinic acid + 1.0L-Aspartic acid ↔ 1.0Guanosine diphosphate + 1.0Phosphate + 1.0Adenylsuccinic acid
ReactionCard
SMPDB Reactions:
1.0Thumb+1.0Thumb+1.0L-Aspartic acid+1.0Thumb → 1.0Thumb+1.0Thumb+1.0N(6)-(1,2-dicarboxyethyl)AMP
1.0Guanosine triphosphate + 1.0Inosinic acid + 1.0L-Aspartic acid + 1.0L-Aspartic acid → 1.0Guanosine diphosphate + 1.0Phosphate + 1.0N(6)-(1,2-dicarboxyethyl)AMP
ReactionCard
1.0Thumb+1.0L-Aspartic acid+1.0Thumb+1.0Thumb → 1.0Thumb+1.0Thumb+2.0Thumb+1.0N(6)-(1,2-dicarboxyethyl)AMP+1.0Thumb
1.0Inosinic acid + 1.0L-Aspartic acid + 1.0Guanosine triphosphate + 1.0L-Aspartic acid → 1.0Guanosine diphosphate + 1.0Phosphate + 2.0Hydrogen ion + 1.0N(6)-(1,2-dicarboxyethyl)AMP + 1.0Adenylsuccinic acid
ReactionCard
Metabolites:
ECMDB IDNameView
ECMDB01332Adenylsuccinic acidMetaboCard
ECMDB01201Guanosine diphosphateMetaboCard
ECMDB01273Guanosine triphosphateMetaboCard
ECMDB21225Hydrogen ionMetaboCard
ECMDB21380Inorganic phosphateMetaboCard
ECMDB04085Inosinic acidMetaboCard
ECMDB00191L-Aspartic acidMetaboCard
ECMDB01429PhosphateMetaboCard
GO Classification:
Component
cell part
cytoplasm
intracellular part
Function
adenylosuccinate synthase activity
binding
catalytic activity
cation binding
GTP binding
guanyl nucleotide binding
guanyl ribonucleotide binding
ion binding
ligase activity
ligase activity, forming carbon-nitrogen bonds
magnesium ion binding
metal ion binding
nucleotide binding
purine nucleotide 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:b4177
Gene OrientationClockwise
Centisome Percentage:94.89
Left Sequence End4402710
Right Sequence End4404008
Gene Sequence:
>1299 bp
ATGACACTCACGCTCAATAGACAACTTCTCACCTCACGCCAGATTCTGGTGGCCTTTAGC
GGCGGGCTTGACTCCACCGTTCTGCTGCATCAGTTGGTGCAGTGGCGGACGGAAAATCCG
GGTGTCGCTCTGCGCGCTATTCATGTGCATCACGGTTTAAGTGCCAATGCCGATGCCTGG
GTTACGCATTGCGAAAACGTCTGCCAACAGTGGCAGGTGCCGCTGGTGGTCGAACGCGTA
CAACTTGCGCAAGAAGGACTGGGCATTGAGGCCCAGGCGCGGCAGGCACGTTATCAGGCA
TTTGCCCGCACCTTGTTGCCCGGTGAAGTGCTGGTCACCGCGCAACATCTCGACGATCAA
TGTGAAACCTTTCTGCTGGCGCTAAAACGCGGCAGTGGCCCTGCCGGGCTTTCGGCTATG
GCGGAAGTCTCGGAGTTTGCCGGAACGCGGCTTATTCGCCCGTTGCTCGCCCGCACGCGG
GGGGAACTGGTGCAGTGGGCGCGTCAGTATGATTTACGCTGGATTGAAGACGAAAGTAAT
CAGGACGACTCATACGATCGTAACTTTCTGCGCCTGCGCGTAGTGCCGTTATTGCAGCAG
CGTTGGCCGCATTTTGCCGAAGCAACGGCCCGCAGCGCCGCACTTTGTGCTGAACAAGAG
AGCCTGCTGGATGAACTGCTGGCAGATGATTTAGCACACTGTCAATCGCCGCAGGGGACG
CTGCAGATTGTGCCAATGCTGGCGATGAGTGATGCCCGCCGCGCGGCGATTATCCGCCGC
TGGCTGGCAGGGCAGAATGCACCGATGCCTTCCCGCGACGCGTTGGTGAGGATCTGGCAG
GAAGTGGCGCTGGCGCGGGAAGATGCCTCACCCTGTTTACGTTTGGGCGCGTTTGAAATC
CGACGCTATCAGTCGCAACTGTGGTGGATTAAATCCGTCACCGGGCAAAGCGAAAACATT
GTGCCGTGGCAGACGTGGCTTCAACCGCTGGAATTACCGGCGGGGCTGGGAAGTGTACAG
CTTAATGCGGGAGGCGATATTCGCCCTCCGCGTGCAGACGAAGCGGTCAGCGTGCGTTTC
AAAGCGCCAGGATTGCTGCATATTGTCGGGCGTAACGGCGGACGTAAGCTAAAGAAAATC
TGGCAAGAGCTGGGCGTGCCGCCGTGGCTACGTGACACCACGCCACTGCTGTTTTATGGC
GAAACGCTGATTGCGGCGGCAGGGGTATTTGTGACGCAAGAAGGTGTGGCTGAAGGTGAG
AATGGCGTAAGTTTTGTCTGGCAGAAAACGCTTAGTTAA
Protein Properties
Pfam Domain Function:
Protein Residues:432
Protein Molecular Weight:47345
Protein Theoretical pI:5
PDB File:1KKF
Signaling Regions:
  • None
Transmembrane Regions:
  • None
Protein Sequence:
>Adenylosuccinate synthetase
MGNNVVVLGTQWGDEGKGKIVDLLTERAKYVVRYQGGHNAGHTLVINGEKTVLHLIPSGI
LRENVTSIIGNGVVLSPAALMKEMKELEDRGIPVRERLLLSEACPLILDYHVALDNAREK
ARGAKAIGTTGRGIGPAYEDKVARRGLRVGDLFDKETFAEKLKEVMEYHNFQLVNYYKAE
AVDYQKVLDDTMAVADILTSMVVDVSDLLDQARQRGDFVMFEGAQGTLLDIDHGTYPYVT
SSNTTAGGVATGSGLGPRYVDYVLGILKAYSTRVGAGPFPTELFDETGEFLCKQGNEFGA
TTGRRRRTGWLDTVAVRRAVQLNSLSGFCLTKLDVLDGLKEVKLCVAYRMPDGREVTTTP
LAADDWKGVEPIYETMPGWSESTFGVKDRSGLPQAALNYIKRIEELTGVPIDIISTGPDR
TETMILRDPFDA
References
External Links:
ResourceLink
Uniprot ID:P0A7D4
Uniprot Name:PURA_ECOLI
GenBank Gene ID:AP009048
Genebank Protein ID:4902929
PDB ID:1KKF
Ecogene ID:EG10790
Ecocyc:EG10790
ColiBase:b4177
Kegg Gene:b4177
EchoBASE ID:EB0783
CCDB:PURA_ECOLI
BacMap:16131999
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
  • Burland, V., Plunkett, G. 3rd, Sofia, H. J., Daniels, D. L., Blattner, F. R. (1995). "Analysis of the Escherichia coli genome VI: DNA sequence of the region from 92.8 through 100 minutes." Nucleic Acids Res 23:2105-2119. Pubmed: 7610040
  • Choe, J. Y., Poland, B. W., Fromm, H. J., Honzatko, R. B. (1999). "Mechanistic implications from crystalline complexes of wild-type and mutant adenylosuccinate synthetases from Escherichia coli." Biochemistry 38:6953-6961. Pubmed: 10346917
  • Dong, Q., Fromm, H. J. (1990). "Chemical modification of adenylosuccinate synthetase from Escherichia coli by pyridoxal 5'-phosphate. Identification of an active site lysyl residue." J Biol Chem 265:6235-6240. Pubmed: 2108156
  • Dong, Q., Liu, F., Myers, A. M., Fromm, H. J. (1991). "Evidence for an arginine residue at the substrate binding site of Escherichia coli adenylosuccinate synthetase as studied by chemical modification and site-directed mutagenesis." J Biol Chem 266:12228-12233. Pubmed: 2061308
  • Fonne-Pfister, R., Chemla, P., Ward, E., Girardet, M., Kreuz, K. E., Honzatko, R. B., Fromm, H. J., Schar, H. P., Grutter, M. G., Cowan-Jacob, S. W. (1996). "The mode of action and the structure of a herbicide in complex with its target: binding of activated hydantocidin to the feedback regulation site of adenylosuccinate synthetase." Proc Natl Acad Sci U S A 93:9431-9436. Pubmed: 8790347
  • Hanessian, S., Lu, P. P., Sanceau, J. Y., Chemla, P., Gohda, K., Fonne-Pfister, R., Prade, L., Cowan-Jacob, S. W. (1999). "An Enzyme-Bound Bisubstrate Hybrid Inhibitor of Adenylosuccinate Synthetase." Angew Chem Int Ed Engl 38:3159-3162. Pubmed: 10556888
  • 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
  • Hou, Z., Cashel, M., Fromm, H. J., Honzatko, R. B. (1999). "Effectors of the stringent response target the active site of Escherichia coli adenylosuccinate synthetase." J Biol Chem 274:17505-17510. Pubmed: 10364182
  • Hou, Z., Wang, W., Fromm, H. J., Honzatko, R. B. (2002). "IMP Alone Organizes the Active Site of Adenylosuccinate Synthetase from Escherichia coli." J Biol Chem 277:5970-5976. Pubmed: 11741996
  • Iancu, C. V., Zhou, Y., Borza, T., Fromm, H. J., Honzatko, R. B. (2006). "Cavitation as a mechanism of substrate discrimination by adenylosuccinate synthetases." Biochemistry 45:11703-11711. Pubmed: 16981730
  • 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
  • Liu, F., Dong, Q., Fromm, H. J. (1992). "Site-directed mutagenesis of the phosphate-binding consensus sequence in Escherichia coli adenylosuccinate synthetase." J Biol Chem 267:2388-2392. Pubmed: 1733940
  • Poland, B. W., Bruns, C., Fromm, H. J., Honzatko, R. B. (1997). "Entrapment of 6-thiophosphoryl-IMP in the active site of crystalline adenylosuccinate synthetase from Escherichia coli." J Biol Chem 272:15200-15205. Pubmed: 9182542
  • Poland, B. W., Fromm, H. J., Honzatko, R. B. (1996). "Crystal structures of adenylosuccinate synthetase from Escherichia coli complexed with GDP, IMP hadacidin, NO3-, and Mg2+." J Mol Biol 264:1013-1027. Pubmed: 9000627
  • Poland, B. W., Hou, Z., Bruns, C., Fromm, H. J., Honzatko, R. B. (1996). "Refined crystal structures of guanine nucleotide complexes of adenylosuccinate synthetase from Escherichia coli." J Biol Chem 271:15407-15413. Pubmed: 8663109
  • Poland, B. W., Lee, S. F., Subramanian, M. V., Siehl, D. L., Anderson, R. J., Fromm, H. J., Honzatko, R. B. (1996). "Refined crystal structure of adenylosuccinate synthetase from Escherichia coli complexed with hydantocidin 5'-phosphate, GDP, HPO4(2-), Mg2+, and hadacidin." Biochemistry 35:15753-15759. Pubmed: 8961938
  • Silva, M. M., Poland, B. W., Hoffman, C. R., Fromm, H. J., Honzatko, R. B. (1995). "Refined crystal structures of unligated adenylosuccinate synthetase from Escherichia coli." J Mol Biol 254:431-446. Pubmed: 7490761
  • Wolfe, S. A., Smith, J. M. (1988). "Nucleotide sequence and analysis of the purA gene encoding adenylosuccinate synthetase of Escherichia coli K12." J Biol Chem 263:19147-19153. Pubmed: 3058695