|Gene:||asnS||Accession Numbers: EG10094 (EcoCyc), b0930, ECK0921|
Synonyms: lcs, tss
Asparaginyl-tRNA synthetase (AsnRS) is a member of the family of aminoacyl-tRNA synthetases, which interpret the genetic code by covalently linking amino acids to their specific tRNA molecules. The reaction is driven by ATP hydrolysis. AsnRS belongs to the Class II aminoacyl tRNA synthetases, which share three regions of homology [Eriani90].
AsnRS is a dimer in solution [Anselme89, Aoki92]. Analysis of mutants suggests that the Y426 residue is involved in ATP binding [Anselme91]; a P231L mutation, which is located in the conserved motif 2 of class II aminoacyl-tRNA synthetases, leads to increases in the Km for asparagine and ATP [Madern92].
|Map Position: [986,808 <- 988,208] (21.27 centisomes, 77°)||Length: 1401 bp / 466 aa|
Molecular Weight of Polypeptide: 52.57 kD (from nucleotide sequence), 54 kD (experimental) [Anselme89 ]
Unification Links: ASAP:ABE-0003162 , CGSC:993 , DIP:DIP-9179N , EchoBASE:EB0092 , EcoGene:EG10094 , EcoliWiki:b0930 , Mint:MINT-1319001 , OU-Microarray:b0930 , PortEco:asnS , PR:PRO_000022170 , Pride:P0A8M0 , Protein Model Portal:P0A8M0 , RefSeq:NP_415450 , RegulonDB:EG10094 , SMR:P0A8M0 , String:511145.b0930 , UniProt:P0A8M0
Relationship Links: InterPro:IN-FAMILY:IPR002312 , InterPro:IN-FAMILY:IPR004364 , InterPro:IN-FAMILY:IPR004365 , InterPro:IN-FAMILY:IPR004522 , InterPro:IN-FAMILY:IPR006195 , InterPro:IN-FAMILY:IPR012340 , InterPro:IN-FAMILY:IPR018150 , Panther:IN-FAMILY:PTHR22594 , Panther:IN-FAMILY:PTHR22594:SF6 , Pfam:IN-FAMILY:PF00152 , Pfam:IN-FAMILY:PF01336 , Prints:IN-FAMILY:PR01042 , Prosite:IN-FAMILY:PS50862
In Paralogous Gene Group: 225 (4 members)
|Biological Process:||GO:0006418 - tRNA aminoacylation for protein translation
GO:0006421 - asparaginyl-tRNA aminoacylation [GOA06, GOA01a, Madern92]
GO:0006412 - translation [UniProtGOA11a]
|Molecular Function:||GO:0004816 - asparagine-tRNA ligase activity
[GOA06, GOA01, GOA01a, Madern92]
GO:0005524 - ATP binding [UniProtGOA11a, GOA06, GOA01a, Anselme91]
GO:0000166 - nucleotide binding [UniProtGOA11a]
GO:0003676 - nucleic acid binding [GOA01a]
GO:0004812 - aminoacyl-tRNA ligase activity [UniProtGOA11a, GOA01a]
GO:0016874 - ligase activity [UniProtGOA11a]
|Cellular Component:||GO:0005737 - cytoplasm
[UniProtGOA11, UniProtGOA11a, GOA06, GOA01a]
GO:0005829 - cytosol [DiazMejia09]
|MultiFun Terms:||information transfer → protein related → amino acid -activation|
|Growth Medium||Growth?||T (°C)||O2||pH||Osm/L||Growth Observations|
|LB Lennox||No||37||Aerobic||7||No [Baba06, Comment 1]|
Enzymatic reaction of: asparaginyl-tRNA synthetase
EC Number: 188.8.131.52
The reaction direction shown, that is, A + B ↔ C + D versus C + D ↔ A + B, is in accordance with the direction in which it was curated.
The reaction is physiologically favored in the direction shown.
In Pathways: tRNA charging
Kinetic parameters of purified wild type and mutant enzymes were measured under various conditions [Madern92]. Reported below are the values measured for the aminoacylation reaction at 37° C.
|Chain||2 -> 466|
10/20/97 Gene b0930 from Blattner lab Genbank (v. M52) entry merged into EcoCyc gene EG10094; confirmed by SwissProt match.
Anselme91: Anselme J, Hartlein M (1991). "Tyr-426 of the Escherichia coli asparaginyl-tRNA synthetase, an amino acid in a C-terminal conserved motif, is involved in ATP binding." FEBS Lett 280(1);163-6. PMID: 2009959
Aoki92: Aoki H, Yaworsky PJ, Patel SD, Margolin-Brzezinski D, Park KS, Ganoza MC (1992). "The asparaginyl-tRNA synthetase gene encodes one of the complementing factors for thermosensitive translation in the Escherichia coli mutant strain, N4316." Eur J Biochem 209(2);511-21. PMID: 1425658
Baba06: Baba T, Ara T, Hasegawa M, Takai Y, Okumura Y, Baba M, Datsenko KA, Tomita M, Wanner BL, Mori H (2006). "Construction of Escherichia coli K-12 in-frame, single-gene knockout mutants: the Keio collection." Mol Syst Biol 2;2006.0008. PMID: 16738554
DiazMejia09: Diaz-Mejia JJ, Babu M, Emili A (2009). "Computational and experimental approaches to chart the Escherichia coli cell-envelope-associated proteome and interactome." FEMS Microbiol Rev 33(1);66-97. PMID: 19054114
Eriani90: Eriani G, Delarue M, Poch O, Gangloff J, Moras D (1990). "Partition of tRNA synthetases into two classes based on mutually exclusive sets of sequence motifs." Nature 347(6289);203-6. PMID: 2203971
Link97: Link AJ, Robison K, Church GM (1997). "Comparing the predicted and observed properties of proteins encoded in the genome of Escherichia coli K-12." Electrophoresis 18(8);1259-313. PMID: 9298646
Madern92: Madern D, Anselme J, Hartlein M (1992). "Asparaginyl-tRNA synthetase from the Escherichia coli temperature-sensitive strain HO202. A proline replacement in motif 2 is responsible for a large increase in Km for asparagine and ATP." FEBS Lett 299(1);85-9. PMID: 1544480
MendozaVargas09: Mendoza-Vargas A, Olvera L, Olvera M, Grande R, Vega-Alvarado L, Taboada B, Jimenez-Jacinto V, Salgado H, Juarez K, Contreras-Moreira B, Huerta AM, Collado-Vides J, Morett E (2009). "Genome-wide identification of transcription start sites, promoters and transcription factor binding sites in E. coli." PLoS One 4(10);e7526. PMID: 19838305
©2014 SRI International, 333 Ravenswood Avenue, Menlo Park, CA 94025-3493