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Escherichia coli K-12 substr. MG1655 Polypeptide: glycyl-tRNA synthetase, α subunit

Gene: glyQ Accession Numbers: EG10409 (EcoCyc), b3560, ECK3548

Synonyms: cfcA, glyS(A)

Regulation Summary Diagram

Regulation summary diagram for glyQ

Component of: glycyl-tRNA synthetase (summary available)

Gene Citations: [Webster83]

Locations: cytosol

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

Relationship Links: InterPro:IN-FAMILY:IPR002310, InterPro:IN-FAMILY:IPR006194, Pfam:IN-FAMILY:PF02091, Prints:IN-FAMILY:PR01044, Prosite:IN-FAMILY:PS50861

Gene-Reaction Schematic

Gene-Reaction Schematic

GO Terms:
Biological Process:
Inferred by computational analysisGO:0006412 - translation [UniProtGOA11]
Inferred by computational analysisGO:0006426 - glycyl-tRNA aminoacylation [GOA06, GOA01]
Molecular Function:
Inferred from experimentGO:0005515 - protein binding [Hauser14, Rajagopala14]
Inferred by computational analysisGO:0000166 - nucleotide binding [UniProtGOA11]
Inferred by computational analysisGO:0004812 - aminoacyl-tRNA ligase activity [UniProtGOA11]
Inferred by computational analysisGO:0004820 - glycine-tRNA ligase activity [GOA06, GOA01a, GOA01]
Inferred by computational analysisGO:0005524 - ATP binding [UniProtGOA11, GOA06, GOA01]
Inferred by computational analysisGO:0016874 - ligase activity [UniProtGOA11]
Cellular Component:
Inferred from experimentInferred by computational analysisGO:0005829 - cytosol [Gaudet10, DiazMejia09, Ishihama08]
Inferred by computational analysisGO:0005737 - cytoplasm [UniProtGOA11a, UniProtGOA11, GOA06, GOA01]

MultiFun Terms: information transferprotein relatedamino acid -activation

Essentiality data for glyQ knockouts:

Growth Medium Growth? T (°C) O2 pH Osm/L Growth Observations
LB LennoxNo 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].

Review: [Ibba00]

Molecular Weight: 205 kD (experimental) [McDonald80]

Last-Curated 20-Jun-2006 by Keseler I, SRI International

Enzymatic reaction of: glycyl-tRNA synthetase

Inferred from experiment

Synonyms: GlyRS

EC Number:

a 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 charging

Kinetic Parameters:
Substrate Km (μM) Citations
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]

Sequence Features

Protein sequence of glycyl-tRNA synthetase, alpha subunit with features indicated

Feature Class Location Citations Comment
Pfam PF02091 9 -> 291
Inferred by computational analysis[Finn14]
tRNA-synt_2e : Glycyl-tRNA synthetase alpha subunit
Sequence-Conflict 48
Inferred by curator[Webster83, UniProt15]
UniProt: (in Ref. 1; AAA23914).
Sequence-Conflict 65
Inferred by curator[Webster83, UniProt15]
UniProt: (in Ref. 1; AAA23914).

Gene Local Context (not to scale -- see Genome Browser for correct scale)

Gene local context diagram

Transcription Unit

Transcription-unit diagram


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

BRENDA14: BRENDA team (2014). Imported from BRENDA version existing on Aug 2014.

Cusack91: Cusack S, Hartlein M, Leberman R (1991). "Sequence, structural and evolutionary relationships between class 2 aminoacyl-tRNA synthetases." Nucleic Acids Res 19(13);3489-98. PMID: 1852601

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

Gaudet10: Gaudet P, Livstone M, Thomas P (2010). "Annotation inferences using phylogenetic trees." PMID: 19578431

GOA01: GOA, DDB, FB, MGI, ZFIN (2001). "Gene Ontology annotation through association of InterPro records with GO terms."

GOA01a: GOA, MGI (2001). "Gene Ontology annotation based on Enzyme Commission mapping." Genomics 74;121-128.

GOA06: GOA, SIB (2006). "Electronic Gene Ontology annotations created by transferring manual GO annotations between orthologous microbial proteins."

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

Hipps95: Hipps D, Schimmel P (1995). "Cell growth inhibition by sequence-specific RNA minihelices." EMBO J 14(16);4050-5. PMID: 7664744

Ibba00: Ibba M, Soll D (2000). "Aminoacyl-tRNA synthesis." Annu Rev Biochem 69;617-50. PMID: 10966471

Ishihama08: Ishihama Y, Schmidt T, Rappsilber J, Mann M, Hartl FU, Kerner MJ, Frishman D (2008). "Protein abundance profiling of the Escherichia coli cytosol." BMC Genomics 9;102. PMID: 18304323

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

McClain91: McClain WH, Foss K, Jenkins RA, Schneider J (1991). "Rapid determination of nucleotides that define tRNA(Gly) acceptor identity." Proc Natl Acad Sci U S A 88(14);6147-51. PMID: 2068095

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

Nameki97: Nameki N, Tamura K, Asahara H, Hasegawa T (1997). "Recognition of tRNA(Gly) by three widely diverged glycyl-tRNA synthetases." J Mol Biol 268(3);640-7. PMID: 9171287

Ostrem70: Ostrem DL, Berg P (1970). "Glycyl-tRNA synthetase: an oligomeric protein containing dissimilar subunits." Proc Natl Acad Sci U S A 67(4);1967-74. PMID: 4923123

Ostrem74: Ostrem DL, Berg P (1974). "Glycyl transfer ribonucleic acid synthetase from Escherichia coli: purification, properties, and substrate binding." Biochemistry 13(7);1338-48. PMID: 4594761

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

Toth86: Toth MJ, Schimmel P (1986). "Internal structural features of E. coli glycyl-tRNA synthetase examined by subunit polypeptide chain fusions." J Biol Chem 261(15);6643-6. PMID: 3009467

UniProt15: UniProt Consortium (2015). "UniProt version 2015-08 released on 2015-07-22." Database.

UniProtGOA11: UniProt-GOA (2011). "Gene Ontology annotation based on manual assignment of UniProtKB keywords in UniProtKB/Swiss-Prot entries."

UniProtGOA11a: UniProt-GOA (2011). "Gene Ontology annotation based on the manual assignment of UniProtKB Subcellular Location terms in UniProtKB/Swiss-Prot entries."

Webster83: Webster TA, Gibson BW, Keng T, Biemann K, Schimmel P (1983). "Primary structures of both subunits of Escherichia coli glycyl-tRNA synthetase." J Biol Chem 258(17);10637-41. PMID: 6309809

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Please cite the following article in publications resulting from the use of EcoCyc: Nucleic Acids Research 41:D605-12 2013
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