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Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
BioCyc websites down
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Metabolic Modeling Tutorial
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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: ?

Component of: glycyl-tRNA synthetase (summary available)

Gene Citations: [Webster83]

Locations: cytosol

Map Position: [3,722,430 <- 3,723,341] (80.23 centisomes)
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: ?

GO Terms:

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

MultiFun Terms: information transfer protein related amino acid -activation

Essentiality data for glyQ knockouts: ?

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

Summary:
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]

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


Enzymatic reaction of: glycyl-tRNA synthetase

Synonyms: GlyRS

EC Number: 6.1.1.14

tRNAgly + glycine + ATP + H+ <=> glycyl-tRNAgly + AMP + diphosphate

The reaction direction shown, that is, A + B ↔ C + D versus C + D ↔ A + B, is in accordance with the direction of enzyme catalysis.

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]
tRNAgly
0.2
[Ostrem74, BRENDA14]
tRNAgly
0.68, 2.1
[Nameki97, BRENDA14]


Sequence Features

Feature Class Location Citations Comment
Sequence-Conflict 48
[Webster83, UniProt10a]
Alternate sequence: E → A; UniProt: (in Ref. 1; AAA23914);
Sequence-Conflict 65
[Webster83, UniProt10a]
Alternate sequence: P → A; UniProt: (in Ref. 1; AAA23914);


Gene Local Context (not to scale): ?

Transcription Unit:

Notes:

History:
10/20/97 Gene b3560 from Blattner lab Genbank (v. M52) entry merged into EcoCyc gene EG10409; confirmed by SwissProt match.


References

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." http://www.brenda-enzymes.org.

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

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.

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

UniProt10a: UniProt Consortium (2010). "UniProt version 2010-11 released on 2010-11-02 00:00:00." Database.

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

UniProtGOA11a: UniProt-GOA (2011). "Gene Ontology annotation based on manual assignment of UniProtKB keywords 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
Page generated by SRI International Pathway Tools version 18.5 on Sat Dec 20, 2014, BIOCYC13A.