DB code: M00150

CATH domain -.-.-.- :
1.10.287.10 : Helix Hairpins
1.10.287.10 : Helix Hairpins
1.10.287.10 : Helix Hairpins
-.-.-.- :
E.C. 6.1.1.17 6.1.1.15
CSA
M-CSA
MACiE

CATH domain Related DB codes (homologues)

Uniprot Enzyme Name
UniprotKB Protein name Synonyms Includes RefSeq Pfam
P07814 Bifunctional aminoacyl-tRNA synthetase
Proliferation-inducing gene 32 protein
Glutamyl-tRNA synthetase
EC 6.1.1.17
Glutamate--tRNA ligase
Prolyl-tRNA synthetase
EC 6.1.1.15
Proline--tRNA ligase
NP_004437.2 (Protein)
NM_004446.2 (DNA/RNA sequence)
PF03129 (HGTP_anticodon)
PF09180 (ProRS-C_1)
PF00749 (tRNA-synt_1c)
PF03950 (tRNA-synt_1c_C)
PF00587 (tRNA-synt_2b)
PF00458 (WHEP-TRS)
[Graphical View]

KEGG enzyme name
glutamate---tRNA ligase
(EC 6.1.1.17 )
glutamyl-tRNA synthetase
(EC 6.1.1.17 )
glutamyl-transfer ribonucleate synthetase
(EC 6.1.1.17 )
glutamyl-transfer RNA synthetase
(EC 6.1.1.17 )
glutamyl-transfer ribonucleic acid synthetase
(EC 6.1.1.17 )
glutamate-tRNA synthetase
(EC 6.1.1.17 )
glutamic acid translase
(EC 6.1.1.17 )
proline---tRNA ligase
(EC 6.1.1.15 )
prolyl-tRNA synthetase
(EC 6.1.1.15 )
prolyl-transferRNA synthetase
(EC 6.1.1.15 )
prolyl-transfer ribonucleate synthetase
(EC 6.1.1.15 )
proline translase
(EC 6.1.1.15 )
prolyl-transfer ribonucleic acid synthetase
(EC 6.1.1.15 )
prolyl-s-RNA synthetase
(EC 6.1.1.15 )
prolinyl-tRNA ligase
(EC 6.1.1.15 )

UniprotKB: Accession Number Entry name Activity Subunit Subcellular location Cofactor
P07814 SYEP_HUMAN ATP + L-glutamate + tRNA(Glu) = AMP + diphosphate + L-glutamyl-tRNA(Glu). ATP + L-proline + tRNA(Pro) = AMP + diphosphate + L-prolyl-tRNA(Pro). Component of the multisynthetase complex which is comprised of a bifunctional glutamyl-prolyl-tRNA synthetase, the monospecific isoleucyl, leucyl, glutaminyl, methionyl, lysyl, arginyl, and aspartyl-tRNA synthetases as well as three auxiliary proteins, p18, p48 and p43. Interacts with DUS2L.

KEGG Pathways
Map code Pathways E.C.
MAP00251 Glutamate metabolism 6.1.1.17
MAP00330 Arginine and proline metabolism 6.1.1.15
MAP00860 Porphyrin and chlorophyll metabolism 6.1.1.17
MAP00970 Aminoacyl-tRNA biosynthesis 6.1.1.17 6.1.1.15

Compound table
Substrates Products Intermediates
KEGG-id C00002 C00025 C01640 C01641 C00148 C01649 C00013 C00020 C02987 C06112 C02702
E.C. 6.1.1.17
6.1.1.15
6.1.1.17
6.1.1.17
6.1.1.17
6.1.1.15
6.1.1.15
6.1.1.17
6.1.1.15
6.1.1.17
6.1.1.15
6.1.1.17
6.1.1.17
6.1.1.15
Compound ATP L-Glutamate tRNA(Gln) tRNA(Glu) L-Proline tRNA(Pro) Pyrophosphate AMP L-Glutamyl-tRNA(Glu) L-Glutamyl-tRNA(Gln) L-Prolyl-tRNA(Pro)
Type amine group,nucleotide amino acids,carboxyl group nucleic acids nucleic acids amino acids nucleic acids phosphate group/phosphate ion amine group,nucleotide amino acids,carboxyl group,nucleic acids amino acids,carboxyl group,nucleic acids amino acids,nucleic acids
ChEBI 15422
 15422
 		16015
 16015
 		17203
 60039
 17203
 60039
 		29888
 29888
 		16027
 16027
PubChem 5957
 5957
 		33032
 44272391
 88747398
 33032
 44272391
 88747398
 		145742
 6971047
 145742
 6971047
 		1023
 21961011
 1023
 21961011
 		6083
 6083
1fyjA Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound

Reference for Active-site residues
resource references E.C.

Active-site residues
PDB Catalytic residues Cofactor-binding residues Modified residues Main-chain involved in catalysis Comment
1fyjA

References for Catalytic Mechanism
References Sections No. of steps in catalysis

References
[1]
Resource
Comments
Medline ID
PubMed ID 8816763
Journal Proc Natl Acad Sci U S A
Year 1996
Volume 93
Pages 10128-33
Authors Rho SB, Lee KH, Kim JW, Shiba K, Jo YJ, Kim S
Title Interaction between human tRNA synthetases involves repeated sequence elements.
Related PDB
Related UniProtKB
[2]
Resource
Comments
Medline ID
PubMed ID 9556618
Journal J Biol Chem
Year 1998
Volume 273
Pages 11267-73
Authors Rho SB, Lee JS, Jeong EJ, Kim KS, Kim YG, Kim S
Title A multifunctional repeated motif is present in human bifunctional tRNA synthetase.
Related PDB
Related UniProtKB
[3]
Resource
Comments NMR Structures
Medline ID
PubMed ID 11123902
Journal Biochemistry
Year 2000
Volume 39
Pages 15775-82
Authors Jeong EJ, Hwang GS, Kim KH, Kim MJ, Kim S, Kim KS
Title Structural analysis of multifunctional peptide motifs in human bifunctional tRNA synthetase: identification of RNA-binding residues and functional implications for tandem repeats.
Related PDB 1fyj
Related UniProtKB
[4]
Resource
Comments
Medline ID
PubMed ID 10745085
Journal FEBS Lett
Year 2000
Volume 470
Pages 300-4
Authors Berthonneau E, Mirande M
Title A gene fusion event in the evolution of aminoacyl-tRNA synthetases.
Related PDB
Related UniProtKB
[5]
Resource
Comments
Medline ID
PubMed ID 11124041
Journal J Mol Biol
Year 2000
Volume 304
Pages 983-94
Authors Robinson JC, Kerjan P, Mirande M
Title Macromolecular assemblage of aminoacyl-tRNA synthetases: quantitative analysis of protein-protein interactions and mechanism of complex assembly.
Related PDB
Related UniProtKB

Comments
This enzyme is composed of three domains. The N-terminal domain is glutamyl-tRNA synthetase (EC 6.1.1.17), whilst the C-terminal domain is prolyl-tRNA synthetase (EC 6.1.1.15). Three repeats are inserted between the N-terminal and C-terminal domains.
Although PDB structure (1fyj) corresponds to the first one of the three repeats, neither of tRNA synthetase domain structures have not been determined yet.

Created Updated
2004-10-22 2009-02-26