EzCatDB: M00150
Related links:    PDB-formatted query search system Fasta-formatted query search system Fasta-formatted query search system

DB codeM00150
CATH domainDomain 1-.-.-.-
Domain 21.10.287.10 : Helix Hairpins
Domain 31.10.287.10 : Helix Hairpins
Domain 41.10.287.10 : Helix Hairpins
Domain 5-.-.-.-
E.C.6.1.1.17,6.1.1.15


Enzyme Name
UniProtKBKEGG

P07814
Protein nameBifunctional aminoacyl-tRNA synthetaseglutamate---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)

SynonymsProliferation-inducing gene 32 protein
IncludesGlutamyl-tRNA synthetase
   EC 6.1.1.17
Glutamate--tRNA ligase
Prolyl-tRNA synthetase
   EC 6.1.1.15
Proline--tRNA ligase
RefSeqNP_004437.2 (Protein)
NM_004446.2 (DNA/RNA sequence)
PfamPF03129 (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 pathways
MAP codePathwaysE.C.
MAP00251Glutamate metabolism6.1.1.17
MAP00330Arginine and proline metabolism6.1.1.15
MAP00860Porphyrin and chlorophyll metabolism6.1.1.17
MAP00970Aminoacyl-tRNA biosynthesis6.1.1.17,6.1.1.15

UniProtKB:Accession NumberP07814
Entry nameSYEP_HUMAN
ActivityATP + L-glutamate + tRNA(Glu) = AMP + diphosphate + L-glutamyl-tRNA(Glu).,ATP + L-proline + tRNA(Pro) = AMP + diphosphate + L-prolyl-tRNA(Pro).
SubunitComponent 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.
Subcellular location
Cofactor

Compound table: links to PDB-related databases & PoSSuM

SubstratesProducts
KEGG-idC00002C00025C01640C01641C00148C01649C00013C00020C02987C06112C02702
E.C.6.1.1.17,6.1.1.156.1.1.176.1.1.176.1.1.176.1.1.156.1.1.156.1.1.17,6.1.1.156.1.1.17,6.1.1.156.1.1.176.1.1.176.1.1.15
CompoundATPL-GlutamatetRNA(Gln)tRNA(Glu)L-ProlinetRNA(Pro)PyrophosphateAMPL-Glutamyl-tRNA(Glu)L-Glutamyl-tRNA(Gln)L-Prolyl-tRNA(Pro)
Typeamine group,nucleotideamino acids,carboxyl groupnucleic acidsnucleic acidsamino acidsnucleic acidsphosphate group/phosphate ionamine group,nucleotideamino acids,carboxyl group,nucleic acidsamino acids,carboxyl group,nucleic acidsamino acids,nucleic acids
ChEBI15422
16015


17203
60039

29888
16027



PubChem5957
88747398
44272391
33032


6971047
145742

21961011
1023
6083



                   
1fyjAUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound

Active-site residues
pdb
        
1fyjA


references
[1]
PubMed ID8816763
JournalProc Natl Acad Sci U S A
Year1996
Volume93
Pages10128-33
AuthorsRho SB, Lee KH, Kim JW, Shiba K, Jo YJ, Kim S
TitleInteraction between human tRNA synthetases involves repeated sequence elements.
[2]
PubMed ID9556618
JournalJ Biol Chem
Year1998
Volume273
Pages11267-73
AuthorsRho SB, Lee JS, Jeong EJ, Kim KS, Kim YG, Kim S
TitleA multifunctional repeated motif is present in human bifunctional tRNA synthetase.
[3]
CommentsNMR Structures
PubMed ID11123902
JournalBiochemistry
Year2000
Volume39
Pages15775-82
AuthorsJeong EJ, Hwang GS, Kim KH, Kim MJ, Kim S, Kim KS
TitleStructural analysis of multifunctional peptide motifs in human bifunctional tRNA synthetase: identification of RNA-binding residues and functional implications for tandem repeats.
Related PDB1fyj
[4]
PubMed ID10745085
JournalFEBS Lett
Year2000
Volume470
Pages300-4
AuthorsBerthonneau E, Mirande M
TitleA gene fusion event in the evolution of aminoacyl-tRNA synthetases.
[5]
PubMed ID11124041
JournalJ Mol Biol
Year2000
Volume304
Pages983-94
AuthorsRobinson JC, Kerjan P, Mirande M
TitleMacromolecular assemblage of aminoacyl-tRNA synthetases: quantitative analysis of protein-protein interactions and mechanism of complex assembly.

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.

createdupdated
2004-10-222009-02-26


Copyright: Nozomi Nagano, JST & CBRC-AIST
Funded by PRESTO/Japan Science and Technology Corporation (JST) (December 2001 - November 2004)
Funded by Grant-in-Aid for Publication of Scientific Research Results/Japan Society for the Promotion of Science (JSPS) (April 2005 - March 2006)
Funded by Grant-in-Aid for Scientific Research (B)/Japan Society for the Promotion of Science (JSPS) (April 2005 - March 2008)
Funded by BIRD/Japan Science and Technology Corporation (JST) (September 2005 - September 2008)
Funded by BIRD/Japan Science and Technology Corporation (JST) (October 2007 - September 2010)
Funded by Grant-in-Aid for Publication of Scientific Research Results/Japan Society for the Promotion of Science (JSPS) (April 2011 - March 2012)
Funded by Grant-in-Aid for Publication of Scientific Research Results/Japan Society for the Promotion of Science (JSPS) (April 2012 - March 2013)
Supported by the commission for the Development of Artificial Gene Synthesis Technology for Creating Innovative Biomaterial from the Ministry of Economy, Trade and Industry (METI) (October 2012 - )
© Biotechnology Research Institute for Drug Discovery, AIST, 2015-2016 All Rights Reserved.
© Computational Biology Research Center, AIST, 2004-2016 All Rights Reserved.