MetaCyc Enzyme: threonyl-tRNA synthetase

Gene: thrS Accession Numbers: EG11001 (MetaCyc), b1719, ECK1717

Species: Escherichia coli K-12 substr. MG1655

Subunit composition of threonyl-tRNA synthetase = [ThrS]2
         threonyl-tRNA synthetase = ThrS

Threonyl-tRNA synthetase (ThrRS) 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. ThrRS belongs to the Class II aminoacyl tRNA synthetases, which share three regions of homology [Eriani90a, Cusack91].

Specificity determinants within tRNAThr that are important for recognition by ThrRS have been identified [Theobald88, Schulman90, Hasegawa92]. Specificity determinants within ThrRS have been investigated and support an induced fit model for the adenylation reaction [Bovee03]. The N-terminal domain contains an editing function that is able to deacylate mischarged Ser-tRNAThr [DockBregeon00, DockBregeon04]. A zinc ion at the active site is used to discriminate against valine at the activation step [Sankaranarayana00]. Mutations in the zinc binding site inactivate the enzymatic function of ThrRS, but not its regulatory function, leading to a dominant negative phenotype when overexpressed in wild-type [Caillet07].

Threonyl-tRNA synthetase represses its own expression at the translational level [Lestienne84, Springer85, Butler86]. Mutations that affect autoregulation map to a region between the transcription start site and the start of the thrS open reading frame; the site has sequence and structural similarity to parts of tRNAThr [Springer86, Moine88a, Springer88]. ThrRS interacts with both an anticodon- and an acceptor-like structure in the mRNA leader region [Romby90, Brunel92, Brunel93, Bedouelle93].

Defects in the regulatory and aminoacylation functions in ThrRS are correlated, suggesting that the enzyme recognizes its mRNA and tRNA ligands in analogous ways [Springer89]; however, one ThrRS dimer binds only one operator region, but each of the two ThrRS subunits binds one tRNAThr [Romby96]. A change in the leader region according to tRNA identity rules to resemble the tRNAMet anticodon leads to translational regulation of ThrRS by MetRS [Graffe92]. tRNAThr acts as an antirepressor [Moine90], and the operator site of the mRNA acts as a competitive inhibitor of tRNAThr aminoacylation [Romby92].

Binding of ThrRS to its mRNA target sites prevents the ribosome from binding and initiating translation [Moine90a]. Competition between ThrRS and the ribosome for binding to the mRNA can be explained by steric hindrance [Sacerdot98]. The catalytic C-terminal domain of ThrRS is responsible for operator binding, while the N-terminal domain of ThrRS is responsible for competition with the ribosome [Caillet03].

ThrRS is a dimer in solution [Hennecke77]. Crystal structures of ThrRS in various conformations have been determined, elucidating the role of the zinc ion in the active site, the nature of the editing domain, and the structural basis for translational control [Sankaranarayana99, Sankaranarayana00, TorresLarios02, DockBregeon04].

ThrRS is under growth rate-dependent control which acts at the level of translation and requires feedback regulation by ThrRS [Comer96].

thrS is essential for growth [Baba06].

Reviews: [Ibba00, Maloy93, MusierForsyth00, Romby03, Schlax03]

Locations: cytosol

Map Position: [1,798,666 <- 1,800,594]

Molecular Weight of Polypeptide: 74.014 kD (from nucleotide sequence), 76 kD (experimental) [Hennecke77 ]

Molecular Weight of Multimer: 150 kD (experimental) [Hennecke77]

Unification Links: ASAP:ABE-0005736 , CGSC:108 , DIP:DIP-35823N , EchoBASE:EB0994 , EcoGene:EG11001 , EcoliWiki:b1719 , Mint:MINT-1229097 , ModBase:P0A8M3 , OU-Microarray:b1719 , PortEco:thrS , PR:PRO_000024069 , Pride:P0A8M3 , Protein Model Portal:P0A8M3 , RefSeq:NP_416234 , RegulonDB:EG11001 , SMR:P0A8M3 , String:511145.b1719 , UniProt:P0A8M3

Relationship Links: InterPro:IN-FAMILY:IPR002314 , InterPro:IN-FAMILY:IPR002320 , InterPro:IN-FAMILY:IPR004095 , InterPro:IN-FAMILY:IPR004154 , InterPro:IN-FAMILY:IPR006195 , InterPro:IN-FAMILY:IPR012675 , InterPro:IN-FAMILY:IPR012676 , InterPro:IN-FAMILY:IPR012947 , InterPro:IN-FAMILY:IPR018163 , PDB:Structure:1EVK , PDB:Structure:1EVL , PDB:Structure:1FYF , PDB:Structure:1KOG , PDB:Structure:1QF6 , PDB:Structure:1TJE , PDB:Structure:1TKE , PDB:Structure:1TKG , PDB:Structure:1TKY , PDB:Structure:4HWO , PDB:Structure:4HWP , PDB:Structure:4HWR , PDB:Structure:4HWS , Pfam:IN-FAMILY:PF00587 , Pfam:IN-FAMILY:PF02824 , Pfam:IN-FAMILY:PF03129 , Pfam:IN-FAMILY:PF07973 , Prints:IN-FAMILY:PR01047 , Prosite:IN-FAMILY:PS50862 , Smart:IN-FAMILY:SM00863

Gene-Reaction Schematic: ?

Gene-Reaction Schematic

GO Terms:

Biological Process: GO:0006418 - tRNA aminoacylation for protein translation Inferred from experiment Inferred by computational analysis [GOA01a, Hennecke77]
GO:0006435 - threonyl-tRNA aminoacylation Inferred from experiment Inferred by computational analysis [GOA06, GOA01a, Hennecke77, Springer89]
GO:0043039 - tRNA aminoacylation Inferred from experiment Inferred by computational analysis [GOA01a, Hennecke77]
GO:0045947 - negative regulation of translational initiation Inferred from experiment [Springer85]
GO:0006412 - translation Inferred by computational analysis [UniProtGOA11]
GO:0006417 - regulation of translation Inferred by computational analysis [UniProtGOA11]
Molecular Function: GO:0000900 - translation repressor activity, nucleic acid binding Inferred from experiment [Moine90a]
GO:0003723 - RNA binding Inferred from experiment Inferred by computational analysis [UniProtGOA11, Sankaranarayana99]
GO:0004829 - threonine-tRNA ligase activity Inferred from experiment Inferred by computational analysis [GOA06, GOA01, GOA01a, Hennecke77, Springer89]
GO:0005515 - protein binding Inferred from experiment [Sankaranarayana99, Butland05]
GO:0005524 - ATP binding Inferred from experiment Inferred by computational analysis [UniProtGOA11, GOA06, GOA01a, Sankaranarayana99]
GO:0008144 - drug binding Inferred from experiment [Hennecke77]
GO:0008270 - zinc ion binding Inferred from experiment [Sankaranarayana99]
GO:0016876 - ligase activity, forming aminoacyl-tRNA and related compounds Inferred from experiment Inferred by computational analysis [GOA01a, Hennecke77]
GO:0000166 - nucleotide binding Inferred by computational analysis [UniProtGOA11, GOA01a]
GO:0004812 - aminoacyl-tRNA ligase activity Inferred by computational analysis [UniProtGOA11, GOA01a]
GO:0016874 - ligase activity Inferred by computational analysis [UniProtGOA11]
GO:0046872 - metal ion binding Inferred by computational analysis [UniProtGOA11]
Cellular Component: GO:0005737 - cytoplasm Inferred from experiment Inferred by computational analysis [UniProtGOA11a, UniProtGOA11, GOA06, GOA01a, Hennecke77]
GO:0005829 - cytosol Inferred from experiment Inferred by computational analysis [DiazMejia09, Ishihama08]

MultiFun Terms: information transfer protein related amino acid -activation
regulation type of regulation posttranscriptional translation attenuation and efficiency

Imported from EcoCyc 02-Jun-2015 by Paley S , SRI International

Enzymatic reaction of: threonyl-tRNA synthetase

Synonyms: ThrRS

EC Number:

a tRNAthr + L-threonine + ATP + H+ <=> an L-threonyl-[tRNAthr] + AMP + diphosphate

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

Imported from EcoCyc 02-Jun-2015 by Paley S , SRI International

Citations: [Nass74]

Cofactors or Prosthetic Groups: Zn2+ [Caillet07, Nureki93]

Inhibitors (Noncompetitive): borrelidin [Ruan05, Nass69]

Kinetic Parameters:

Km (μM)
kcat (sec-1)
kcat/Km (sec-1 μM-1)
[Ruan05, BRENDA14]
3.0, 37.0
0.017, 0.21
[Sankaranarayana00, BRENDA14]
[Bovee03, BRENDA14]
[Bovee03, BRENDA14]
a tRNAthr
0.03, 0.43
[TorresLarios02, BRENDA14]
a tRNAthr
a tRNAthr
[Ling10, BRENDA14]
a tRNAthr
0.05, 0.085
10.4, 6.12
[Zheltonosova94, BRENDA14]

T(opt): 37 °C [BRENDA14, Zheltonosova94]

pH(opt): 8.4 [BRENDA14, Paetz73]

Sequence Features

Feature Class Location Common Name Attached Group Citations Comment State
Sequence-Conflict 195    
[Mayaux83, UniProt10a]
UniProt: (in Ref. 1; CAA23560);
Protein-Segment 243 -> 534    
UniProt: Catalytic; Sequence Annotation Type: region of interest;
N6-acetyllysine-Modification 286    
[Zhang09, UniProt15]
UniProt: N6-acetyllysine.
Mutagenesis-Variant 334    
UniProt: Activity very strongly affected.
Metal-Binding-Site 334    
UniProt: Zinc; catalytic.
Metal-Binding-Site 334, 385, 511 Zn2+ binding site Zn2+
Mutagenesis-Variant 385    
A or N: Activity very strongly affected.
Metal-Binding-Site 385    
UniProt: Zinc; catalytic.
Mutagenesis-Variant 511    
A or N: Activity very strongly affected.
Metal-Binding-Site 511    
UniProt: Zinc; catalytic.

10/20/97 Gene b1719 from Blattner lab Genbank (v. M52) entry merged into EcoCyc gene EG11001; 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

Bedouelle93: Bedouelle H (1993). "Symmetrical interactions between the translational operator of the thrS gene and dimeric threonyl transfer RNA synthetase." J Mol Biol 230(3);704-8. PMID: 7683056

Bovee03: Bovee ML, Pierce MA, Francklyn CS (2003). "Induced fit and kinetic mechanism of adenylation catalyzed by Escherichia coli threonyl-tRNA synthetase." Biochemistry 42(51);15102-13. PMID: 14690420

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

Brunel92: Brunel C, Caillet J, Lesage P, Graffe M, Dondon J, Moine H, Romby P, Ehresmann C, Ehresmann B, Grunberg-Manago M (1992). "Domains of the Escherichia coli threonyl-tRNA synthetase translational operator and their relation to threonine tRNA isoacceptors." J Mol Biol 227(3);621-34. PMID: 1383551

Brunel93: Brunel C, Romby P, Moine H, Caillet J, Grunberg-Manago M, Springer M, Ehresmann B, Ehresmann C (1993). "Translational regulation of the Escherichia coli threonyl-tRNA synthetase gene: structural and functional importance of the thrS operator domains." Biochimie 75(12);1167-79. PMID: 8199252

Butland05: Butland G, Peregrin-Alvarez JM, Li J, Yang W, Yang X, Canadien V, Starostine A, Richards D, Beattie B, Krogan N, Davey M, Parkinson J, Greenblatt J, Emili A (2005). "Interaction network containing conserved and essential protein complexes in Escherichia coli." Nature 433(7025);531-7. PMID: 15690043

Butler86: Butler JS, Springer M, Dondon J, Grunberg-Manago M (1986). "Posttranscriptional autoregulation of Escherichia coli threonyl tRNA synthetase expression in vivo." J Bacteriol 165(1);198-203. PMID: 3510186

Caillet03: Caillet J, Nogueira T, Masquida B, Winter F, Graffe M, Dock-Bregeon AC, Torres-Larios A, Sankaranarayanan R, Westhof E, Ehresmann B, Ehresmann C, Romby P, Springer M (2003). "The modular structure of Escherichia coli threonyl-tRNA synthetase as both an enzyme and a regulator of gene expression." Mol Microbiol 47(4);961-74. PMID: 12581352

Caillet07: Caillet J, Graffe M, Eyermann F, Romby P, Springer M (2007). "Mutations in residues involved in zinc binding in the catalytic site of Escherichia coli threonyl-tRNA synthetase confer a dominant lethal phenotype." J Bacteriol 189(19);6839-48. PMID: 17644600

Comer96: Comer MM, Dondon J, Graffe M, Yarchuk O, Springer M (1996). "Growth rate-dependent control, feedback regulation and steady-state mRNA levels of the threonyl-tRNA synthetase gene of Escherichia coli." J Mol Biol 261(2);108-24. PMID: 8757280

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

DockBregeon00: Dock-Bregeon A, Sankaranarayanan R, Romby P, Caillet J, Springer M, Rees B, Francklyn CS, Ehresmann C, Moras D (2000). "Transfer RNA-mediated editing in threonyl-tRNA synthetase. The class II solution to the double discrimination problem." Cell 103(6);877-84. PMID: 11136973

DockBregeon04: Dock-Bregeon AC, Rees B, Torres-Larios A, Bey G, Caillet J, Moras D (2004). "Achieving error-free translation; the mechanism of proofreading of threonyl-tRNA synthetase at atomic resolution." Mol Cell 16(3);375-86. PMID: 15525511

Eriani90a: 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, MGI (2001). "Gene Ontology annotation based on Enzyme Commission mapping." Genomics 74;121-128.

GOA01a: GOA, DDB, FB, MGI, ZFIN (2001). "Gene Ontology annotation through association of InterPro records with GO terms."

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

Graffe92: Graffe M, Dondon J, Caillet J, Romby P, Ehresmann C, Ehresmann B, Springer M (1992). "The specificity of translational control switched with transfer RNA identity rules." Science 255(5047);994-6. PMID: 1372129

Hasegawa92: Hasegawa T, Miyano M, Himeno H, Sano Y, Kimura K, Shimizu M (1992). "Identity determinants of E. coli threonine tRNA." Biochem Biophys Res Commun 184(1);478-84. PMID: 1567450

Hennecke77: Hennecke H, Bock A, Thomale J, Nass G (1977). "Threonyl-transfer ribonucleic acid synthetase from Escherichia coli: subunit structure and genetic analysis of the structural gene by means of a mutated enzyme and of a specialized transducing lambda bacteriophage." J Bacteriol 131(3);943-50. PMID: 330505

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

Lestienne84: Lestienne P, Plumbridge JA, Grunberg-Manago M, Blanquet S (1984). "Autogenous repression of Escherichia coli threonyl-tRNA synthetase expression in vitro." J Biol Chem 259(8);5232-7. PMID: 6325425

Ling10: Ling J, Soll D (2010). "Severe oxidative stress induces protein mistranslation through impairment of an aminoacyl-tRNA synthetase editing site." Proc Natl Acad Sci U S A 107(9);4028-33. PMID: 20160114

Maloy93: Maloy S, Stewart V (1993). "Autogenous regulation of gene expression." J Bacteriol 175(2);307-16. PMID: 8419283

Mayaux83: Mayaux JF, Fayat G, Fromant M, Springer M, Grunberg-Manago M, Blanquet S (1983). "Structural and transcriptional evidence for related thrS and infC expression." Proc Natl Acad Sci U S A 80(20);6152-6. PMID: 6353409

Moine88a: Moine H, Romby P, Springer M, Grunberg-Manago M, Ebel JP, Ehresmann C, Ehresmann B (1988). "Messenger RNA structure and gene regulation at the translational level in Escherichia coli: the case of threonine:tRNAThr ligase." Proc Natl Acad Sci U S A 85(21);7892-6. PMID: 3054873

Moine90: Moine H, Romby P, Springer M, Grunberg-Manago M, Ebel JP, Ehresmann B, Ehresmann C (1990). "Escherichia coli threonyl-tRNA synthetase and tRNA(Thr) modulate the binding of the ribosome to the translational initiation site of the thrS mRNA." J Mol Biol 216(2);299-310. PMID: 2254931

Moine90a: Moine H, Ehresmann B, Romby P, Ebel JP, Grunberg-Manago M, Springer M, Ehresmann C (1990). "The translational regulation of threonyl-tRNA synthetase. Functional relationship between the enzyme, the cognate tRNA and the ribosome." Biochim Biophys Acta 1050(1-3);343-50. PMID: 2207165

MusierForsyth00: Musier-Forsyth K, Beuning PJ (2000). "Role of zinc ion in translational accuracy becomes crystal clear." Nat Struct Biol 7(6);435-6. PMID: 10881182

Nass69: Nass G, Poralla K, Zahner H (1969). "Effect of the antibiotic Borrelidin on the regulation of threonine biosynthetic enzymes in E. coli." Biochem Biophys Res Commun 34(1);84-91. PMID: 4883496

Nass74: Nass G, Thomale J (1974). "Alteration of structure of level of threonyl-tRNA-synthetase in Borrelidin resistant mutants of E. coli." FEBS Lett 39(2);182-6. PMID: 4368395

Nureki93: Nureki O, Kohno T, Sakamoto K, Miyazawa T, Yokoyama S (1993). "Chemical modification and mutagenesis studies on zinc binding of aminoacyl-tRNA synthetases." J Biol Chem 268(21);15368-73. PMID: 8340367

Paetz73: Paetz W, Nass G (1973). "Biochemical and immunological characterization of threonyl-tRNA synthetase of two borrelidin-resistant mutants of Escherichia coli K12." Eur J Biochem 35(2);331-7. PMID: 4577856

Romby03: Romby P, Springer M (2003). "Bacterial translational control at atomic resolution." Trends Genet 19(3);155-61. PMID: 12615010

Romby90: Romby P, Moine H, Lesage P, Graffe M, Dondon J, Ebel JP, Grunberg-Manago M, Ehresmann B, Ehresmann C, Springer M (1990). "The relation between catalytic activity and gene regulation in the case of E coli threonyl-tRNA synthetase." Biochimie 72(6-7);485-94. PMID: 1701663

Romby92: Romby P, Brunel C, Caillet J, Springer M, Grunberg-Manago M, Westhof E, Ehresmann C, Ehresmann B (1992). "Molecular mimicry in translational control of E. coli threonyl-tRNA synthetase gene. Competitive inhibition in tRNA aminoacylation and operator-repressor recognition switch using tRNA identity rules." Nucleic Acids Res 20(21);5633-40. PMID: 1280807

Romby96: Romby P, Caillet J, Ebel C, Sacerdot C, Graffe M, Eyermann F, Brunel C, Moine H, Ehresmann C, Ehresmann B, Springer M (1996). "The expression of E.coli threonyl-tRNA synthetase is regulated at the translational level by symmetrical operator-repressor interactions." EMBO J 15(21);5976-87. PMID: 8918475

Ruan05: Ruan B, Bovee ML, Sacher M, Stathopoulos C, Poralla K, Francklyn CS, Soll D (2005). "A unique hydrophobic cluster near the active site contributes to differences in borrelidin inhibition among threonyl-tRNA synthetases." J Biol Chem 280(1);571-7. PMID: 15507440

Sacerdot98: Sacerdot C, Caillet J, Graffe M, Eyermann F, Ehresmann B, Ehresmann C, Springer M, Romby P (1998). "The Escherichia coli threonyl-tRNA synthetase gene contains a split ribosomal binding site interrupted by a hairpin structure that is essential for autoregulation." Mol Microbiol 29(4);1077-90. PMID: 9767575

Sankaranarayana00: Sankaranarayanan R, Dock-Bregeon AC, Rees B, Bovee M, Caillet J, Romby P, Francklyn CS, Moras D (2000). "Zinc ion mediated amino acid discrimination by threonyl-tRNA synthetase." Nat Struct Biol 7(6);461-5. PMID: 10881191

Sankaranarayana99: Sankaranarayanan R, Dock-Bregeon AC, Romby P, Caillet J, Springer M, Rees B, Ehresmann C, Ehresmann B, Moras D (1999). "The structure of threonyl-tRNA synthetase-tRNA(Thr) complex enlightens its repressor activity and reveals an essential zinc ion in the active site." Cell 97(3);371-81. PMID: 10319817

Schlax03: Schlax PJ, Worhunsky DJ (2003). "Translational repression mechanisms in prokaryotes." Mol Microbiol 48(5);1157-69. PMID: 12787346

Schulman90: Schulman LH, Pelka H (1990). "An anticodon change switches the identity of E. coli tRNA(mMet) from methionine to threonine." Nucleic Acids Res 18(2);285-9. PMID: 2109304

Springer85: Springer M, Plumbridge JA, Butler JS, Graffe M, Dondon J, Mayaux JF, Fayat G, Lestienne P, Blanquet S, Grunberg-Manago M (1985). "Autogenous control of Escherichia coli threonyl-tRNA synthetase expression in vivo." J Mol Biol 185(1);93-104. PMID: 3930755

Springer86: Springer M, Graffe M, Butler JS, Grunberg-Manago M (1986). "Genetic definition of the translational operator of the threonine-tRNA ligase gene in Escherichia coli." Proc Natl Acad Sci U S A 83(12);4384-8. PMID: 3086882

Springer88: Springer M, Graffe M, Dondon J, Grunberg-Manago M, Romby P, Ehresmann B, Ehresmann C, Ebel JP (1988). "Translational control in E. coli: the case of threonyl-tRNA synthetase." Biosci Rep 8(6);619-32. PMID: 3072027

Springer89: Springer M, Graffe M, Dondon J, Grunberg-Manago M (1989). "tRNA-like structures and gene regulation at the translational level: a case of molecular mimicry in Escherichia coli." EMBO J 8(8);2417-24. PMID: 2676521

Theobald88: Theobald A, Springer M, Grunberg-Manago M, Ebel JP, Giege R (1988). "Tertiary structure of Escherichia coli tRNA(3Thr) in solution and interaction of this tRNA with the cognate threonyl-tRNA synthetase." Eur J Biochem 175(3);511-24. PMID: 2457500

TorresLarios02: Torres-Larios A, Dock-Bregeon AC, Romby P, Rees B, Sankaranarayanan R, Caillet J, Springer M, Ehresmann C, Ehresmann B, Moras D (2002). "Structural basis of translational control by Escherichia coli threonyl tRNA synthetase." Nat Struct Biol 9(5);343-7. PMID: 11953757

UniProt10: UniProt Consortium (2010). "UniProt version 2010-07 released on 2010-06-15 00:00:00." Database.

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

UniProt15: UniProt Consortium (2015). "UniProt version 2015-01 released on 2015-01-16 00:00:00." 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."

Zhang09: Zhang J, Sprung R, Pei J, Tan X, Kim S, Zhu H, Liu CF, Grishin NV, Zhao Y (2009). "Lysine acetylation is a highly abundant and evolutionarily conserved modification in Escherichia coli." Mol Cell Proteomics 8(2);215-25. PMID: 18723842

Zheltonosova94: Zheltonosova J, Melnikova E, Garber M, Reinbolt J, Kern D, Ehresmann C, Ehresmann B (1994). "Threonyl-tRNA synthetase from Thermus thermophilus: purification and some structural and kinetic properties." Biochimie 76(1);71-7. PMID: 8031907

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Please cite the following article in publications resulting from the use of MetaCyc: Caspi et al, Nucleic Acids Research 42:D459-D471 2014
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