Adenylosuccinate synthetase
Details
- Name
- Adenylosuccinate synthetase
- Synonyms
- 6.3.4.4
- adeK
- AMPSase
- IMP--aspartate ligase
- Gene Name
- purA
- Organism
- Escherichia coli (strain K12)
- Amino acid sequence
>lcl|BSEQ0019120|Adenylosuccinate synthetase MGNNVVVLGTQWGDEGKGKIVDLLTERAKYVVRYQGGHNAGHTLVINGEKTVLHLIPSGI LRENVTSIIGNGVVLSPAALMKEMKELEDRGIPVRERLLLSEACPLILDYHVALDNAREK ARGAKAIGTTGRGIGPAYEDKVARRGLRVGDLFDKETFAEKLKEVMEYHNFQLVNYYKAE AVDYQKVLDDTMAVADILTSMVVDVSDLLDQARQRGDFVMFEGAQGTLLDIDHGTYPYVT SSNTTAGGVATGSGLGPRYVDYVLGILKAYSTRVGAGPFPTELFDETGEFLCKQGNEFGA TTGRRRRTGWLDTVAVRRAVQLNSLSGFCLTKLDVLDGLKEVKLCVAYRMPDGREVTTTP LAADDWKGVEPIYETMPGWSESTFGVKDRSGLPQAALNYIKRIEELTGVPIDIISTGPDR TETMILRDPFDA
- Number of residues
- 432
- Molecular Weight
- 47344.585
- Theoretical pI
- 5.13
- GO Classification
- Functionsadenylosuccinate synthase activity / GTP binding / magnesium ion bindingProcesses'de novo' AMP biosynthetic process / adenosine biosynthetic process / cellular response to DNA damage stimulus / IMP metabolic process / nucleobase-containing small molecule interconversion / purine nucleotide biosynthetic processComponentscytoplasm / cytosol / membrane
- General Function
- Magnesium ion binding
- Specific Function
- Plays an important role in the de novo pathway of purine nucleotide biosynthesis. Catalyzes the first committed step in the biosynthesis of AMP from IMP.
- Pfam Domain Function
- Adenylsucc_synt (PF00709)
- Transmembrane Regions
- Not Available
- Cellular Location
- Cytoplasm
- Gene sequence
>lcl|BSEQ0019121|Adenylosuccinate synthetase (purA) ATGGGTAACAACGTCGTCGTACTGGGCACCCAATGGGGTGACGAAGGTAAAGGTAAGATC GTCGATCTTCTGACTGAACGGGCTAAATATGTTGTACGCTACCAGGGCGGTCACAACGCA GGCCATACTCTCGTAATCAACGGTGAAAAAACCGTTCTCCATCTTATTCCATCAGGTATT CTCCGCGAGAATGTAACCAGCATCATCGGTAACGGTGTTGTGCTGTCTCCGGCCGCGCTG ATGAAAGAGATGAAAGAACTGGAAGACCGTGGCATCCCCGTTCGTGAGCGTCTGCTGCTG TCTGAAGCATGTCCGCTGATCCTTGATTATCACGTTGCGCTGGATAACGCGCGTGAGAAA GCGCGTGGCGCGAAAGCGATCGGCACCACCGGTCGTGGTATCGGGCCTGCTTATGAAGAT AAAGTAGCACGTCGCGGTCTGCGTGTTGGCGACCTTTTCGACAAAGAAACCTTCGCTGAA AAACTGAAAGAAGTGATGGAATATCACAACTTCCAGTTGGTTAACTACTACAAAGCTGAA GCGGTTGATTACCAGAAAGTTCTGGATGATACGATGGCTGTTGCCGACATCCTGACTTCT ATGGTGGTTGACGTTTCTGACCTGCTCGACCAGGCGCGTCAGCGTGGCGATTTCGTCATG TTTGAAGGTGCGCAGGGTACGCTGCTGGATATCGACCACGGTACTTATCCGTACGTAACT TCTTCCAACACCACTGCTGGTGGCGTGGCGACCGGTTCCGGCCTGGGCCCGCGTTATGTT GATTACGTTCTGGGTATCCTCAAAGCTTACTCCACTCGTGTAGGTGCAGGTCCGTTCCCG ACCGAACTGTTTGATGAAACTGGCGAGTTCCTCTGCAAGCAGGGTAACGAATTCGGCGCA ACTACGGGGCGTCGTCGTCGTACCGGCTGGCTGGACACCGTTGCCGTTCGTCGTGCGGTA CAGCTGAACTCCCTGTCTGGCTTCTGCCTGACTAAACTGGACGTTCTGGATGGCCTGAAA GAGGTTAAACTCTGCGTGGCTTACCGTATGCCGGATGGTCGCGAAGTGACTACCACTCCG CTGGCAGCTGACGACTGGAAAGGTGTAGAGCCGATTTACGAAACCATGCCGGGCTGGTCT GAATCCACCTTCGGCGTGAAAGATCGTAGCGGCCTGCCGCAGGCGGCGCTGAACTATATC AAGCGTATTGAAGAGCTGACTGGTGTGCCGATCGATATCATCTCTACCGGTCCGGATCGT ACTGAAACCATGATTCTGCGCGACCCGTTCGACGCGTAA
- Chromosome Location
- Not Available
- Locus
- Not Available
- External Identifiers
Resource Link UniProtKB ID P0A7D4 UniProtKB Entry Name PURA_ECOLI GenBank Protein ID 147406 GenBank Gene ID J04199 - General References
- Wolfe SA, Smith JM: Nucleotide sequence and analysis of the purA gene encoding adenylosuccinate synthetase of Escherichia coli K12. J Biol Chem. 1988 Dec 15;263(35):19147-53. [Article]
- Burland V, Plunkett G 3rd, Sofia HJ, Daniels DL, Blattner FR: Analysis of the Escherichia coli genome VI: DNA sequence of the region from 92.8 through 100 minutes. Nucleic Acids Res. 1995 Jun 25;23(12):2105-19. [Article]
- Blattner FR, Plunkett G 3rd, Bloch CA, Perna NT, Burland V, Riley M, Collado-Vides J, Glasner JD, Rode CK, Mayhew GF, Gregor J, Davis NW, Kirkpatrick HA, Goeden MA, Rose DJ, Mau B, Shao Y: The complete genome sequence of Escherichia coli K-12. Science. 1997 Sep 5;277(5331):1453-62. [Article]
- Hayashi K, Morooka N, Yamamoto Y, Fujita K, Isono K, Choi S, Ohtsubo E, Baba T, Wanner BL, Mori H, Horiuchi T: Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110. Mol Syst Biol. 2006;2:2006.0007. Epub 2006 Feb 21. [Article]
- Dong Q, Liu F, Myers AM, Fromm HJ: 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. 1991 Jul 5;266(19):12228-33. [Article]
- Link AJ, Robison K, Church GM: Comparing the predicted and observed properties of proteins encoded in the genome of Escherichia coli K-12. Electrophoresis. 1997 Aug;18(8):1259-313. [Article]
- Dong Q, Fromm HJ: Chemical modification of adenylosuccinate synthetase from Escherichia coli by pyridoxal 5'-phosphate. Identification of an active site lysyl residue. J Biol Chem. 1990 Apr 15;265(11):6235-40. [Article]
- Liu F, Dong Q, Fromm HJ: Site-directed mutagenesis of the phosphate-binding consensus sequence in Escherichia coli adenylosuccinate synthetase. J Biol Chem. 1992 Feb 5;267(4):2388-92. [Article]
- Silva MM, Poland BW, Hoffman CR, Fromm HJ, Honzatko RB: Refined crystal structures of unligated adenylosuccinate synthetase from Escherichia coli. J Mol Biol. 1995 Dec 1;254(3):431-46. [Article]
- Poland BW, Lee SF, Subramanian MV, Siehl DL, Anderson RJ, Fromm HJ, Honzatko RB: Refined crystal structure of adenylosuccinate synthetase from Escherichia coli complexed with hydantocidin 5'-phosphate, GDP, HPO4(2-), Mg2+, and hadacidin. Biochemistry. 1996 Dec 10;35(49):15753-9. [Article]
- Poland BW, Hou Z, Bruns C, Fromm HJ, Honzatko RB: Refined crystal structures of guanine nucleotide complexes of adenylosuccinate synthetase from Escherichia coli. J Biol Chem. 1996 Jun 28;271(26):15407-13. [Article]
- Poland BW, Fromm HJ, Honzatko RB: Crystal structures of adenylosuccinate synthetase from Escherichia coli complexed with GDP, IMP hadacidin, NO3-, and Mg2+. J Mol Biol. 1996 Dec 20;264(5):1013-27. [Article]
- Fonne-Pfister R, Chemla P, Ward E, Girardet M, Kreuz KE, Honzatko RB, Fromm HJ, Schar HP, Grutter MG, Cowan-Jacob SW: 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. 1996 Sep 3;93(18):9431-6. [Article]
- Poland BW, Bruns C, Fromm HJ, Honzatko RB: Entrapment of 6-thiophosphoryl-IMP in the active site of crystalline adenylosuccinate synthetase from Escherichia coli. J Biol Chem. 1997 Jun 13;272(24):15200-5. [Article]
- Hanessian S, Lu PP, Sanceau JY, Chemla P, Gohda K, Fonne-Pfister R, Prade L, Cowan-Jacob SW: An Enzyme-Bound Bisubstrate Hybrid Inhibitor of Adenylosuccinate Synthetase. Angew Chem Int Ed Engl. 1999 Nov 2;38(21):3159-3162. [Article]
- Choe JY, Poland BW, Fromm HJ, Honzatko RB: Mechanistic implications from crystalline complexes of wild-type and mutant adenylosuccinate synthetases from Escherichia coli. Biochemistry. 1999 May 25;38(21):6953-61. [Article]
- Hou Z, Cashel M, Fromm HJ, Honzatko RB: Effectors of the stringent response target the active site of Escherichia coli adenylosuccinate synthetase. J Biol Chem. 1999 Jun 18;274(25):17505-10. [Article]
- Hou Z, Wang W, Fromm HJ, Honzatko RB: IMP Alone Organizes the Active Site of Adenylosuccinate Synthetase from Escherichia coli. J Biol Chem. 2002 Feb 22;277(8):5970-6. Epub 2001 Dec 12. [Article]
- Iancu CV, Zhou Y, Borza T, Fromm HJ, Honzatko RB: Cavitation as a mechanism of substrate discrimination by adenylosuccinate synthetases. Biochemistry. 2006 Sep 26;45(38):11703-11. [Article]
Drug Relations
- Drug Relations
DrugBank ID Name Drug group Pharmacological action? Actions Details DB02109 Hadacidin experimental unknown Details DB02493 Hydantocidin-5'-phosphate experimental unknown Details DB02666 (C8-R)-hydantocidin 5'-phosphate experimental unknown Details DB02836 Guanosine 5'-diphosphate 2':3'-cyclic monophosphate experimental unknown Details DB02954 (Carboxyhydroxyamino)Ethanoic Acid experimental unknown Details DB03146 2-deazo-6-thiophosphate guanosine-5'-monophosphate experimental unknown Details DB04315 Guanosine-5'-Diphosphate experimental unknown Details DB04460 (C8-S)-Hydantocidin 5'-phosphate experimental unknown Details DB04566 Inosinic Acid experimental unknown Details