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ECOLI:SYE

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Species (Taxon ID) Escherichia coli (strain K12). (83333)
Gene Name(s) gltX
Protein Name(s) Glutamate--tRNA ligase

Glutamyl-tRNA synthetase GluRS

External Links
UniProt P04805
EMBL X63976
M13687
U00096
AP009048
X55737
PIR A25956
RefSeq NP_416899.1
YP_490639.1
ProteinModelPortal P04805
SMR P04805
DIP DIP-9810N
IntAct P04805
MINT MINT-1296746
STRING 511145.b2400
BindingDB P04805
PaxDb P04805
PRIDE P04805
EnsemblBacteria AAC75457
BAA16272
GeneID 12930199
946906
KEGG ecj:Y75_p2364
eco:b2400
PATRIC 32120177
EchoBASE EB0402
EcoGene EG10407
eggNOG COG0008
HOGENOM HOG000252722
InParanoid P04805
KO K01885
OMA IEAFKWV
OrthoDB EOG6DRPF7
PhylomeDB P04805
BioCyc EcoCyc:GLURS-MONOMER
ECOL316407:JW2395-MONOMER
MetaCyc:GLURS-MONOMER
SABIO-RK P04805
PRO PR:P04805
Proteomes UP000000318
UP000000625
Genevestigator P04805
GO GO:0005737
GO:0005524
GO:0004818
GO:0000049
GO:0008270
GO:0006424
Gene3D 1.10.10.350
1.10.1160.10
3.40.50.620
HAMAP MF_00022_B
InterPro IPR008925
IPR020751
IPR001412
IPR004527
IPR000924
IPR020061
IPR020058
IPR014729
PANTHER PTHR10119
Pfam PF00749
PRINTS PR00987
SUPFAM SSF48163
TIGRFAMs TIGR00464
PROSITE PS00178

Annotations

Qualifier GO ID GO term name Reference ECO ID ECO term name with/from Aspect Extension Notes Status

NOT

GO:0004818

glutamate-tRNA ligase activity

PMID:6280993[1]

ECO:0000314

F

Table 4 and Fig. 4 shows that GluRS can bind both ATP and its tRNA substrate independently, but binding of glutamate requires the presence of tRNAGlu.

complete
CACAO 4651

involved_in

GO:0006424

glutamyl-tRNA aminoacylation

PMID:21873635[2]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

EcoGene:EG10407
PANTHER:PTN000012469
UniProtKB:Q5JPH6
UniProtKB:Q8IDD3

P

Seeded From UniProt

complete

part_of

GO:0005829

cytosol

PMID:21873635[2]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

EcoGene:EG10407
PANTHER:PTN000804412

C

Seeded From UniProt

complete

enables

GO:0004818

glutamate-tRNA ligase activity

PMID:21873635[2]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

EcoGene:EG10407
PANTHER:PTN000012469
UniProtKB:Q5JPH6
UniProtKB:Q8IDD3

F

Seeded From UniProt

complete

enables

GO:0008270

zinc ion binding

PMID:8218204[3]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

involved_in

GO:0006424

glutamyl-tRNA aminoacylation

PMID:4942764[4]

ECO:0000315

mutant phenotype evidence used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:0006424

glutamyl-tRNA aminoacylation

PMID:4577134[5]

ECO:0000315

mutant phenotype evidence used in manual assertion

P

Seeded From UniProt

complete

part_of

GO:0005829

cytosol

PMID:18304323[6]

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

part_of

GO:0005829

cytosol

PMID:15911532[7]

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

enables

GO:0004818

glutamate-tRNA ligase activity

PMID:786370[8]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

enables

GO:0000049

tRNA binding

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR008925

F

Seeded From UniProt

complete

enables

GO:0000166

nucleotide binding

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR000924
InterPro:IPR001412
InterPro:IPR004527

F

Seeded From UniProt

complete

enables

GO:0004812

aminoacyl-tRNA ligase activity

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR000924
InterPro:IPR001412
InterPro:IPR020058

F

Seeded From UniProt

complete

enables

GO:0004818

glutamate-tRNA ligase activity

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR004527

F

Seeded From UniProt

complete

enables

GO:0005524

ATP binding

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR000924
InterPro:IPR001412
InterPro:IPR004527
InterPro:IPR020058

F

Seeded From UniProt

complete

involved_in

GO:0006418

tRNA aminoacylation for protein translation

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR001412

P

Seeded From UniProt

complete

involved_in

GO:0006424

glutamyl-tRNA aminoacylation

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR004527
InterPro:IPR033910

P

Seeded From UniProt

complete

enables

GO:0008270

zinc ion binding

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR033910

F

Seeded From UniProt

complete

involved_in

GO:0043039

tRNA aminoacylation

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR000924
InterPro:IPR020058

P

Seeded From UniProt

complete

enables

GO:0004818

glutamate-tRNA ligase activity

GO_REF:0000003

ECO:0000501

evidence used in automatic assertion

EC:6.1.1.17

F

Seeded From UniProt

complete

enables

GO:0008270

zinc ion binding

GO_REF:0000104

ECO:0000256

match to sequence model evidence used in automatic assertion

UniRule:UR000075658

F

Seeded From UniProt

complete

part_of

GO:0005737

cytoplasm

GO_REF:0000104

ECO:0000256

match to sequence model evidence used in automatic assertion

UniRule:UR000075658

C

Seeded From UniProt

complete

enables

GO:0005524

ATP binding

GO_REF:0000104

ECO:0000256

match to sequence model evidence used in automatic assertion

UniRule:UR000075658

F

Seeded From UniProt

complete

enables

GO:0004818

glutamate-tRNA ligase activity

GO_REF:0000104

ECO:0000256

match to sequence model evidence used in automatic assertion

UniRule:UR000075658

F

Seeded From UniProt

complete

involved_in

GO:0006424

glutamyl-tRNA aminoacylation

GO_REF:0000104

ECO:0000256

match to sequence model evidence used in automatic assertion

UniRule:UR000075658

P

Seeded From UniProt

complete

enables

GO:0016874

ligase activity

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0436

F

Seeded From UniProt

complete

enables

GO:0046872

metal ion binding

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0479

F

Seeded From UniProt

complete

part_of

GO:0005737

cytoplasm

GO_REF:0000037
GO_REF:0000039

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0963
UniProtKB-SubCell:SL-0086

C

Seeded From UniProt

complete

enables

GO:0004812

aminoacyl-tRNA ligase activity

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0030

F

Seeded From UniProt

complete

enables

GO:0000166

nucleotide binding

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0547

F

Seeded From UniProt

complete

involved_in

GO:0006412

translation

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0648

P

Seeded From UniProt

complete

enables

GO:0005524

ATP binding

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0067

F

Seeded From UniProt

complete

edit table

Notes

References

See Help:References for how to manage references in GONUTS.

  1. ↑ Kern, D & Lapointe, J (1980) The catalytic mechanism of glutamyl-tRNA synthetase of Escherichia coli. Evidence for a two-step aminoacylation pathway, and study of the reactivity of the intermediate complex. Eur. J. Biochem. 106 137-50 PubMed GONUTS page
  2. ↑ 2.0 2.1 2.2 Gaudet, P et al. (2011) Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium. Brief. Bioinformatics 12 449-62 PubMed GONUTS page
  3. ↑ Liu, J et al. (1993) The glutamyl-tRNA synthetase of Escherichia coli contains one atom of zinc essential for its native conformation and its catalytic activity. Biochemistry 32 11390-6 PubMed GONUTS page
  4. ↑ Russell, RR & Pittard, AJ (1971) Mutants of Escherichia coli unable to make protein at 42 C. J. Bacteriol. 108 790-8 PubMed GONUTS page
  5. ↑ Kaplan, S et al. (1973) Synthesis of stable RNA in stringent Escherichia coli cells in the absence of charged transfer RNA. Proc. Natl. Acad. Sci. U.S.A. 70 689-92 PubMed GONUTS page
  6. ↑ Ishihama, Y et al. (2008) Protein abundance profiling of the Escherichia coli cytosol. BMC Genomics 9 102 PubMed GONUTS page
  7. ↑ Lopez-Campistrous, A et al. (2005) Localization, annotation, and comparison of the Escherichia coli K-12 proteome under two states of growth. Mol. Cell Proteomics 4 1205-9 PubMed GONUTS page
  8. ↑ Willick, GE & Kay, CM (1976) Circular dichroism study of the interaction of glutamyl-tRNA synthetase with tRNAGlu2. Biochemistry 15 4347-52 PubMed GONUTS page
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