|Gene:||glyQ||Accession Numbers: EG10409 (EcoCyc), b3560, ECK3548|
Synonyms: cfcA, glyS(A)
Component of: glycyl-tRNA synthetase (summary available)
Gene Citations: [Webster83]
|Map Position: [3,722,430 <- 3,723,341] (80.23 centisomes, 289°)||Length: 912 bp / 303 aa|
Molecular Weight of Polypeptide: 34.774 kD (from nucleotide sequence), 35 kD (experimental) [Keng82]
Unification Links: ASAP:ABE-0011626, CGSC:33775, DIP:DIP-9816N, EchoBASE:EB0404, EcoGene:EG10409, EcoliWiki:b3560, Mint:MINT-1225336, ModBase:P00960, OU-Microarray:b3560, PortEco:glyQ, PR:PRO_000022817, Pride:P00960, Protein Model Portal:P00960, RefSeq:NP_418017, RegulonDB:EG10409, SMR:P00960, String:511145.b3560, Swiss-Model:P00960, UniProt:P00960
|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]|
Subunit of: glycyl-tRNA synthetase
Subunit composition of
glycyl-tRNA synthetase = [GlyS]2[GlyQ]2
glycyl-tRNA synthetase, β subunit = GlyS (summary available)
glycyl-tRNA synthetase, α subunit = GlyQ
Glycyl-tRNA synthetase (GlyRS) 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. GlyRS belongs to the Class II aminoacyl tRNA synthetases, which share three regions of homology [Eriani90, Cusack91].
GlyRS is a tetramer consisting of two α and two β subunits. Both subunits are required for catalytic activity [Ostrem70, McDonald80]. An enzyme in which the α and β subunits are fused into a single polypeptide chain is catalytically active [Toth86].
Specificity determinants within tRNAGly that are important for recognition by GlyRS have been identified [Roberts75, McClain91, Hipps95, Nameki97]. The tRNA binding site is located in the β subunit of GlyRS [Nagel84].
Molecular Weight: 205 kD (experimental) [McDonald80]
Enzymatic reaction of: glycyl-tRNA synthetase
EC Number: 22.214.171.124a tRNAgly + glycine + ATP + H+ → a glycyl-[tRNAgly] + AMP + diphosphate
The direction shown, i.e. which substrates are on the left and right sides, is in accordance with the direction in which it was curated.
The reaction is physiologically favored in the direction shown.
In Pathways: tRNA chargingKinetic Parameters:
|ATP||14.0, 40.0, 42.0||[Ostrem74, BRENDA14]|
|glycine||30.0, 140.0, 160.0||[Ostrem74, BRENDA14]|
|a tRNAgly||0.2||[Ostrem74, BRENDA14]|
|a tRNAgly||0.68, 2.1||[Nameki97, BRENDA14]|
|Pfam PF02091||9 -> 291|
10/20/97 Gene b3560 from Blattner lab Genbank (v. M52) entry merged into EcoCyc gene EG10409; confirmed by SwissProt match.
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
Finn14: Finn RD, Bateman A, Clements J, Coggill P, Eberhardt RY, Eddy SR, Heger A, Hetherington K, Holm L, Mistry J, Sonnhammer EL, Tate J, Punta M (2014). "Pfam: the protein families database." Nucleic Acids Res 42(Database issue);D222-30. PMID: 24288371
Hauser14: Hauser R, Ceol A, Rajagopala SV, Mosca R, Siszler G, Wermke N, Sikorski P, Schwarz F, Schick M, Wuchty S, Aloy P, Uetz P (2014). "A Second-generation Protein-Protein Interaction Network of Helicobacter pylori." Mol Cell Proteomics 13(5);1318-29. PMID: 24627523
Keng82: Keng T, Webster TA, Sauer RT, Schimmel P (1982). "Gene for Escherichia coli glycyl-tRNA synthetase has tandem subunit coding regions in the same reading frame." J Biol Chem 257(21);12503-8. PMID: 6290471
McDonald80: McDonald T, Breite L, Pangburn KL, Hom S, Manser J, Nagel GM (1980). "Overproduction, purification, and subunit structure of Escherichia coli glycyl transfer ribonucleic acid synthetase." Biochemistry 19(7);1402-9. PMID: 6992865
Nagel84: Nagel GM, Cumberledge S, Johnson MS, Petrella E, Weber BH (1984). "The beta subunit of E. coli glycyl-tRNA synthetase plays a major role in tRNA recognition." Nucleic Acids Res 12(10);4377-84. PMID: 6374618
Rajagopala14: Rajagopala SV, Sikorski P, Kumar A, Mosca R, Vlasblom J, Arnold R, Franca-Koh J, Pakala SB, Phanse S, Ceol A, Hauser R, Siszler G, Wuchty S, Emili A, Babu M, Aloy P, Pieper R, Uetz P (2014). "The binary protein-protein interaction landscape of Escherichia coli." Nat Biotechnol 32(3);285-90. PMID: 24561554
Roberts75: Roberts JW, Carbon J (1975). "Nucleotide sequence studies of normal and genetically altered glycine transfer ribonucleic acids from Escherichia coli." J Biol Chem 250(14);5530-41. PMID: 167016
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