M00049
type: Enzyme
active site residues resources: Transfer RNA-mediated editing in threonyl-tRNA synthetase. The class II solution to the double discrimination problem.
active site residues resources: The modular structure of Escherichia coli threonyl-tRNA synthetase as both an enzyme and a regulator of gene expression.
active site residues resources: P0A8M3
cath: Ubiquitin-like (UB roll)
cath: Threonyl-tRNA Synthetase; Chain A, domain 2
cath: Replication Terminator Protein; Chain A, domain 2
cath: BirA Bifunctional Protein; domain 2
cath: Rossmann fold
csa: 1qf6
ec: https://purl.uniprot.org/enzyme/6.1.1.3
kegg cofactor: Zinc
kegg cofactor: Magnesium
kegg enzyme: threonine---tRNA ligase
kegg pathway: Glycine, serine and threonine metabolism
kegg pathway: Aminoacyl-tRNA biosynthesis
kegg product: Pyrophosphate
kegg product: AMP
kegg product: L-Threonyl-tRNA(Thr)
kegg substrate: ATP
kegg substrate: L-Threonine
kegg substrate: tRNA(Thr)
pdb: 1qf6A01
pdb: 1nyqA01
pdb: 1nyqB01
pdb: 1nyrA01
pdb: 1nyrB01
pdb: 1qf6A02
pdb: 1nyqA02
pdb: 1nyqB02
pdb: 1nyrA02
pdb: 1nyrB02
pdb: 1qf6A03
pdb: 1nyqA03
pdb: 1nyqB03
pdb: 1nyrA03
pdb: 1nyrB03
pdb: 1evkA01
pdb: 1evkB01
pdb: 1evlA01
pdb: 1evlB01
pdb: 1evlC01
pdb: 1evlD01
pdb: 1fyfA01
pdb: 1fyfB01
pdb: 1kogA01
pdb: 1kogB01
pdb: 1kogC01
pdb: 1kogD01
pdb: 1kogE01
pdb: 1kogF01
pdb: 1kogG01
pdb: 1kogH01
pdb: 1qf6A04
pdb: 1nyqA04
pdb: 1nyqB04
pdb: 1nyrA04
pdb: 1nyrB04
pdb: 1evkA02
pdb: 1evkB02
pdb: 1evlA02
pdb: 1evlB02
pdb: 1evlC02
pdb: 1evlD02
pdb: 1fyfA02
pdb: 1fyfB02
pdb: 1kogA02
pdb: 1kogB02
pdb: 1kogC02
pdb: 1kogD02
pdb: 1kogE02
pdb: 1kogF02
pdb: 1kogG02
pdb: 1kogH02
pdb: 1qf6A05
pdb: 1nyqA05
pdb: 1nyqB05
pdb: 1nyrA05
pdb: 1nyrB05
rlcp: p394

Ubiquitin-like (UB roll)
type: Cath
references: http://www.cathdb.info/version/latest/superfamily/3.10.20.30

Replication Terminator Protein; Chain A, domain 2
type: Cath
references: http://www.cathdb.info/version/latest/superfamily/3.30.54.20

BirA Bifunctional Protein; domain 2
type: Cath
catalytic domain: index.html
references: http://www.cathdb.info/version/latest/superfamily/3.30.930.10

Threonyl-tRNA Synthetase; Chain A, domain 2
type: Cath
references: http://www.cathdb.info/version/latest/superfamily/3.30.980.10

Rossmann fold
type: Cath
references: http://www.cathdb.info/version/latest/superfamily/3.40.50.800

Glycine, serine and threonine metabolism
type: KeggPathway
references: KEGG:MAP00260

Aminoacyl-tRNA biosynthesis
type: KeggPathway
references: KEGG:MAP00970

Crystals of threonyl-tRNA synthetase from Thermus thermophilus. Preliminary crystallographic data.
type: BibliographicResource
authors:
  item: Garber MB
  item: Yaremchuk AD
  item: Tukalo MA
  item: Egorova SP
  item: Fomenkova NP
  item: Nikonov SV
journal: J Mol Biol
pages: 819-20
published year: 1990
volume: 214
references: http://www.ncbi.nlm.nih.gov/pubmed/2388270

Structural basis of translational control by Escherichia coli threonyl tRNA synthetase.
type: BibliographicResource
authors:
  item: Torres-Larios A
  item: Moras D
  item: Dock-Bregeon AC
  item: Romby P
  item: Rees B
  item: Sankaranarayanan R
  item: Caillet J
  item: Springer M
  item: Ehresmann C
  item: Ehresmann B
journal: Nat Struct Biol
pages: 343-7
published year: 2002
volume: 9
references: http://www.ncbi.nlm.nih.gov/pubmed/11953757
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl

Induced fit and kinetic mechanism of adenylation catalyzed by Escherichia coli threonyl-tRNA synthetase.
type: BibliographicResource
authors:
  item: Bovee ML
  item: Pierce MA
  item: Francklyn CS
journal: Biochemistry
pages: 15102-13
published year: 2003
volume: 42
references: http://www.ncbi.nlm.nih.gov/pubmed/14690420

Elucidation of tRNA-dependent editing by a class II tRNA synthetase and significance for cell viability.
type: BibliographicResource
authors:
  item: Beebe K
  item: Ribas De Pouplana L
  item: Schimmel P
journal: EMBO J
pages: 668-75
published year: 2003
volume: 22
references: http://www.ncbi.nlm.nih.gov/pubmed/12554667

Conformational movements and cooperativity upon amino acid, ATP and tRNA binding in threonyl-tRNA synthetase.
type: BibliographicResource
authors:
  item: Torres-Larios A
  item: Sankaranarayanan R
  item: Rees B
  item: Dock-Bregeon AC
  item: Moras D
journal: J Mol Biol
pages: 201-11
published year: 2003
volume: 331
references: http://www.ncbi.nlm.nih.gov/pubmed/12875846
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl

Crystallization of threonyl-tRNA synthetase from Thermus thermophilus and preliminary crystallographic data.
type: BibliographicResource
authors:
  item: Cura V
  item: Kern D
  item: Mitschler A
  item: Moras D
journal: FEBS Lett
pages: 110-2
published year: 1995
volume: 374
references: http://www.ncbi.nlm.nih.gov/pubmed/7589494

The structure of threonyl-tRNA synthetase-tRNA(Thr) complex enlightens its repressor activity and reveals an essential zinc ion in the active site.
type: BibliographicResource
authors:
  item: Sankaranarayanan R
  item: Dock-Bregeon AC
  item: Romby P
  item: Caillet J
  item: Springer M
  item: Rees B
  item: Ehresmann C
  item: Ehresmann B
  item: Moras D
journal: Cell
medline id: 99251535
pages: 371-81
published year: 1999
volume: 97
references: http://www.ncbi.nlm.nih.gov/pubmed/10319817
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: P0A8M3
comment: X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS).

Structure of Hsp15 reveals a novel RNA-binding motif.
type: BibliographicResource
authors:
  item: Staker BL
  item: Korber P
  item: Bardwell JC
  item: Saper MA
journal: EMBO J
pages: 749-57
published year: 2000
volume: 19
references: http://www.ncbi.nlm.nih.gov/pubmed/10675344

Sequence analysis and modular organization of threonyl-tRNA synthetase from Thermus thermophilus and its interrelation with threonyl-tRNA synthetases of other origins.
type: BibliographicResource
authors:
  item: Cura V
  item: Moras D
  item: Kern D
journal: Eur J Biochem
pages: 379-93
published year: 2000
volume: 267
references: http://www.ncbi.nlm.nih.gov/pubmed/10632708

Role of zinc ion in translational accuracy becomes crystal clear.
type: BibliographicResource
authors:
  item: Musier-Forsyth K
  item: Beuning PJ
journal: Nat Struct Biol
pages: 435-6
published year: 2000
volume: 7
references: http://www.ncbi.nlm.nih.gov/pubmed/10881182

Zinc ion mediated amino acid discrimination by threonyl-tRNA synthetase.
type: BibliographicResource
authors:
  item: Sankaranarayanan R
  item: Dock-Bregeon AC
  item: Rees B
  item: Bovee M
  item: Caillet J
  item: Romby P
  item: Francklyn CS
  item: Moras D
journal: Nat Struct Biol
medline id: 20343005
pages: 461-5
published year: 2000
volume: 7
references: http://www.ncbi.nlm.nih.gov/pubmed/10881191
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: P0A8M3
comment: X-RAY CRYSTALLOGRAPHY (1.55 ANGSTROMS) OF 242-642.

The fidelity of the translation of the genetic code.
type: BibliographicResource
authors:
  item: Sankaranarayanan R
  item: Moras D
journal: Acta Biochim Pol
pages: 323-35
published year: 2001
volume: 48
references: http://www.ncbi.nlm.nih.gov/pubmed/11732604

The modular structure of Escherichia coli threonyl-tRNA synthetase as both an enzyme and a regulator of gene expression.
type: BibliographicResource
authors:
  item: Caillet J
  item: Ehresmann B
  item: Ehresmann C
  item: Romby P
  item: Springer M
  item: Nogueira T
  item: Masquida B
  item: Winter F
  item: Graffe M
  item: Dock-Bregeon AC
  item: Torres-Larios A
  item: Sankaranarayanan R
  item: Westhof E
journal: Mol Microbiol
pages: 961-74
published year: 2003
volume: 47
references: http://www.ncbi.nlm.nih.gov/pubmed/12581352

Transfer RNA-mediated editing in threonyl-tRNA synthetase. The class II solution to the double discrimination problem.
type: BibliographicResource
authors:
  item: Dock-Bregeon A
  item: Sankaranarayanan R
  item: Romby P
  item: Caillet J
  item: Springer M
  item: Rees B
  item: Francklyn CS
  item: Ehresmann C
  item: Moras D
journal: Cell
pages: 877-84
published year: 2000
volume: 103
references: http://www.ncbi.nlm.nih.gov/pubmed/11136973
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
comment: X-ray crystallography

1nyrA04
type: Pdb
catalytic residue: ARG 365;ARG 377;LYS 471
cofactor binding residue: CYS 336;HIS 387;HIS 517(Zinc binding);GLU 367(Magnesium binding)
references: 1nyr
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1nyr

1nyrB04
type: Pdb
catalytic residue: ARG 365;ARG 377;LYS 471
cofactor binding residue: CYS 336;HIS 387;HIS 517(Zinc binding);GLU 367(Magnesium binding)
references: 1nyr
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1nyr

1qf6A04
type: Pdb
catalytic residue: ARG 363;ARG 375;LYS 465
cofactor binding residue: CYS 334;HIS 385;HIS 511(Zinc binding);GLU 365(Magnesium binding)
references: 1qf6
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1qf6

1evkB01
type: Pdb
catalytic residue: ARG 363;ARG 375;LYS 465
cofactor binding residue: CYS 334;HIS 385;HIS 511(Zinc binding);GLU 365(Magnesium binding)
references: 1evk
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1evk

1evkA01
type: Pdb
catalytic residue: ARG 363;ARG 375;LYS 465
cofactor binding residue: CYS 334;HIS 385;HIS 511(Zinc binding);GLU 365(Magnesium binding)
references: 1evk
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1evk

1evlA01
type: Pdb
catalytic residue: ARG 363;ARG 375;LYS 465
cofactor binding residue: CYS 334;HIS 385;HIS 511(Zinc binding);GLU 365(Magnesium binding)
references: 1evl
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1evl

1evlB01
type: Pdb
catalytic residue: ARG 363;ARG 375;LYS 465
cofactor binding residue: CYS 334;HIS 385;HIS 511(Zinc binding);GLU 365(Magnesium binding)
references: 1evl
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1evl

1evlC01
type: Pdb
catalytic residue: ARG 363;ARG 375;LYS 465
cofactor binding residue: CYS 334;HIS 385;HIS 511(Zinc binding);GLU 365(Magnesium binding)
references: 1evl
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1evl

1evlD01
type: Pdb
catalytic residue: ARG 363;ARG 375;LYS 465
cofactor binding residue: CYS 334;HIS 385;HIS 511(Zinc binding);GLU 365(Magnesium binding)
references: 1evl
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1evl

1fyfA01
type: Pdb
catalytic residue: ARG 363;ARG 375;LYS 465
cofactor binding residue: CYS 334;HIS 385;HIS 511(Zinc binding);GLU 365(Magnesium binding)
references: 1fyf
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1fyf

1fyfB01
type: Pdb
catalytic residue: ARG 363;ARG 375;LYS 465
cofactor binding residue: CYS 334;HIS 385;HIS 511(Zinc binding);GLU 365(Magnesium binding)
references: 1fyf
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1fyf

1kogA01
type: Pdb
catalytic residue: ARG 363;ARG 375;LYS 465
cofactor binding residue: CYS 334;HIS 385;HIS 511(Zinc binding);GLU 365(Magnesium binding)
references: 1kog
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1kog

1kogB01
type: Pdb
catalytic residue: ARG 363;ARG 375;LYS 465
cofactor binding residue: CYS 334;HIS 385;HIS 511(Zinc binding);GLU 365(Magnesium binding)
references: 1kog
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1kog

1kogC01
type: Pdb
catalytic residue: ARG 363;ARG 375;LYS 465
cofactor binding residue: CYS 334;HIS 385;HIS 511(Zinc binding);GLU 365(Magnesium binding)
references: 1kog
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1kog

1kogD01
type: Pdb
catalytic residue: ARG 363;ARG 375;LYS 465
cofactor binding residue: CYS 334;HIS 385;HIS 511(Zinc binding);GLU 365(Magnesium binding)
references: 1kog
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1kog

1kogE01
type: Pdb
catalytic residue: ARG 363;ARG 375;LYS 465
cofactor binding residue: CYS 334;HIS 385;HIS 511(Zinc binding);GLU 365(Magnesium binding)
references: 1kog
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1kog

1kogF01
type: Pdb
catalytic residue: ARG 363;ARG 375;LYS 465
cofactor binding residue: CYS 334;HIS 385;HIS 511(Zinc binding);GLU 365(Magnesium binding)
references: 1kog
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1kog

1kogG01
type: Pdb
catalytic residue: ARG 363;ARG 375;LYS 465
cofactor binding residue: CYS 334;HIS 385;HIS 511(Zinc binding);GLU 365(Magnesium binding)
references: 1kog
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1kog

1kogH01
type: Pdb
catalytic residue: ARG 363;ARG 375;LYS 465
cofactor binding residue: CYS 334;HIS 385;HIS 511(Zinc binding);GLU 365(Magnesium binding)
references: 1kog
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1kog

1nyqA04
type: Pdb
catalytic residue: ARG 365;ARG 377;LYS 471
cofactor binding residue: CYS 336;HIS 387;HIS 517(Zinc binding);GLU 367(Magnesium binding)
references: 1nyq
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1nyq

1nyqB04
type: Pdb
catalytic residue: ARG 365;ARG 377;LYS 471
cofactor binding residue: CYS 336;HIS 387;HIS 517(Zinc binding);GLU 367(Magnesium binding)
references: 1nyq
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1nyq

Zinc
type: KeggCofactor
compound type: heavy metal
references: KEGG:C00038
references: CHEBI:29105
references: http://pubchem.ncbi.nlm.nih.gov/summary/summary.cgi

L-Threonine
type: KeggSubstrate
compound type: amino acids
compound type: carbohydrate
references: KEGG:C00188
references: CHEBI:16857
references: CHEBI:57926
references: http://pubchem.ncbi.nlm.nih.gov/summary/summary.cgi

ATP
type: KeggSubstrate
compound type: amine group
compound type: nucleotide
references: KEGG:C00002
references: CHEBI:15422
references: http://pubchem.ncbi.nlm.nih.gov/summary/summary.cgi

AMP
type: KeggProduct
compound type: amine group
compound type: nucleotide
references: KEGG:C00020
references: CHEBI:16027
references: http://pubchem.ncbi.nlm.nih.gov/summary/summary.cgi

tRNA(Thr)
type: KeggSubstrate
compound type: nucleic acids
references: KEGG:C01651

Pyrophosphate
type: KeggProduct
compound type: phosphate group/phosphate ion
references: KEGG:C00013
references: CHEBI:29888
references: http://pubchem.ncbi.nlm.nih.gov/summary/summary.cgi

Magnesium
type: KeggCofactor
compound type: divalent metal (Ca2+, Mg2+)
references: KEGG:C00305
references: CHEBI:18420
references: http://pubchem.ncbi.nlm.nih.gov/summary/summary.cgi

L-Threonyl-tRNA(Thr)
type: KeggProduct
compound type: amino acids
compound type: carbohydrate
compound type: nucleic acids
references: KEGG:C02992

threonyl-tRNA synthetase
type: KeggEnzyme

threonyl-transfer ribonucleate synthetase
type: KeggEnzyme

threonyl-transfer RNA synthetase
type: KeggEnzyme

threonyl-transfer ribonucleic acid synthetase
type: KeggEnzyme

threonyl ribonucleic synthetase
type: KeggEnzyme

threonine-transfer ribonucleate synthetase
type: KeggEnzyme

threonine translase
type: KeggEnzyme

threonyl-tRNA synthetase
type: KeggEnzyme

TRS
type: KeggEnzyme

IntermediateAnalogue
ligand het code: TSB
pdb: 1evlA01

IntermediateAnalogue
ligand het code: TSB
pdb: 1evlB01

IntermediateAnalogue
ligand het code: TSB
pdb: 1evlC01

IntermediateAnalogue
ligand het code: TSB
pdb: 1evlD01

IntermediateAnalogue
ligand het code: SSA
pdb: 1fyfA01

IntermediateAnalogue
ligand het code: SSA
pdb: 1fyfB01

IntermediateAnalogue
ligand het code: TSB
pdb: 1kogA01

IntermediateAnalogue
ligand het code: TSB
pdb: 1kogB01

IntermediateAnalogue
ligand het code: TSB
pdb: 1kogC01

IntermediateAnalogue
ligand het code: TSB
pdb: 1kogD01

IntermediateAnalogue
ligand het code: TSB
pdb: 1kogE01

IntermediateAnalogue
ligand het code: TSB
pdb: 1kogF01

IntermediateAnalogue
ligand het code: TSB
pdb: 1kogG01

IntermediateAnalogue
ligand het code: TSB
pdb: 1kogH01

IntermediateAnalogue
ligand het code: TSB
pdb: 1nyqA04

IntermediateAnalogue
ligand het code: TSB
pdb: 1nyqB04

ReferenceForCatalyticMechanism
reference index: 7
reference section: Fig.1, p.435

ReferenceForCatalyticMechanism
reference index: 13
reference section: p.206-207