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Protein

Glutamate--tRNA ligase

Gene

gltX

Organism
Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the attachment of glutamate to tRNA(Glu) in a two-step reaction: glutamate is first activated by ATP to form Glu-AMP and then transferred to the acceptor end of tRNA(Glu).2 Publications

Catalytic activityi

ATP + L-glutamate + tRNA(Glu) = AMP + diphosphate + L-glutamyl-tRNA(Glu).

Enzyme regulationi

In the absence of bound tRNA, ATP is bound in a non-productive mode, and the enzyme cannot activate amino acids.1 Publication

Kineticsi

  1. KM=4.7 µM for tRNA-Glu1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei15 – 151ATP
Binding sitei41 – 411Glutamate
Binding sitei205 – 2051Glutamate
Binding sitei208 – 2081ATP
Binding sitei236 – 2361ATP; via amide nitrogen and carbonyl oxygen
Sitei354 – 3541Interaction with tRNA; via carbonyl oxygen
Sitei358 – 3581Essential for discrimination between tRNA(Glu) and tRNA(Gln)

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi243 – 2475ATP

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-HAMAP
  2. glutamate-tRNA ligase activity Source: UniProtKB-HAMAP
  3. tRNA binding Source: InterPro

GO - Biological processi

  1. glutamyl-tRNA aminoacylation Source: UniProtKB-HAMAP
Complete GO annotation...

Keywords - Molecular functioni

Aminoacyl-tRNA synthetase, Ligase

Keywords - Biological processi

Protein biosynthesis

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciTTHE300852:GH8R-459-MONOMER.
BRENDAi6.1.1.17. 2305.

Names & Taxonomyi

Protein namesi
Recommended name:
Glutamate--tRNA ligase (EC:6.1.1.17)
Alternative name(s):
Glutamyl-tRNA synthetase
Short name:
GluRS
Gene namesi
Name:gltX
Ordered Locus Names:TTHA0438
OrganismiThermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)
Taxonomic identifieri300852 [NCBI]
Taxonomic lineageiBacteriaDeinococcus-ThermusDeinococciThermalesThermaceaeThermus
ProteomesiUP000000532 Componenti: Chromosome

Subcellular locationi

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi358 – 3581R → Q: Reduces affinity for tRNA and abolishes the ability to discriminate between tRNA(Glu) and tRNA(Gln). 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 468468Glutamate--tRNA ligasePRO_0000119683Add
BLAST

Interactioni

Subunit structurei

Monomer.1 Publication

Protein-protein interaction databases

DIPiDIP-29168N.
STRINGi300852.TTHA0438.

Structurei

Secondary structure

1
468
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi3 – 64Combined sources
Beta strandi11 – 133Combined sources
Helixi16 – 3116Combined sources
Beta strandi35 – 384Combined sources
Turni45 – 473Combined sources
Helixi52 – 6211Combined sources
Beta strandi68 – 703Combined sources
Turni71 – 733Combined sources
Beta strandi76 – 783Combined sources
Helixi82 – 843Combined sources
Helixi86 – 9813Combined sources
Beta strandi101 – 1055Combined sources
Helixi109 – 11911Combined sources
Helixi125 – 1284Combined sources
Helixi131 – 1399Combined sources
Beta strandi145 – 1484Combined sources
Beta strandi155 – 1606Combined sources
Turni161 – 1633Combined sources
Beta strandi164 – 1696Combined sources
Helixi170 – 1723Combined sources
Beta strandi177 – 1793Combined sources
Helixi187 – 19711Combined sources
Beta strandi202 – 2065Combined sources
Helixi207 – 2126Combined sources
Helixi213 – 22311Combined sources
Beta strandi229 – 2335Combined sources
Beta strandi241 – 2433Combined sources
Turni246 – 2483Combined sources
Helixi253 – 2586Combined sources
Helixi263 – 27311Combined sources
Helixi286 – 2927Combined sources
Helixi295 – 2973Combined sources
Helixi307 – 32014Combined sources
Helixi324 – 33714Combined sources
Helixi345 – 35511Combined sources
Helixi356 – 3583Combined sources
Helixi364 – 3685Combined sources
Helixi370 – 3723Combined sources
Helixi381 – 40323Combined sources
Helixi409 – 42315Combined sources
Helixi427 – 43913Combined sources
Helixi447 – 4537Combined sources
Helixi456 – 46712Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1G59X-ray2.40A/C1-468[»]
1GLNX-ray2.50A1-468[»]
1J09X-ray1.80A1-468[»]
1N75X-ray1.90A1-468[»]
1N77X-ray2.40A/B1-468[»]
1N78X-ray2.10A/B1-468[»]
2CUZX-ray1.98A1-468[»]
2CV0X-ray2.40A/B1-468[»]
2CV1X-ray2.41A/B1-468[»]
2CV2X-ray2.69A/B1-468[»]
2DXIX-ray2.20A/B1-468[»]
ProteinModelPortaliP27000.
SMRiP27000. Positions 1-468.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP27000.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni5 – 73Glutamate binding
Regioni187 – 1915Glutamate binding
Regioni432 – 44716Interaction with tRNAAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi8 – 1811"HIGH" regionAdd
BLAST
Motifi243 – 2475"KMSKS" region

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0008.
HOGENOMiHOG000252720.
KOiK01885.
OMAiAFRCFCT.
OrthoDBiEOG6DRPF7.
PhylomeDBiP27000.

Family and domain databases

Gene3Di1.10.10.350. 1 hit.
1.10.1160.10. 1 hit.
1.10.8.70. 1 hit.
3.40.50.620. 2 hits.
HAMAPiMF_00022_B. Glu_tRNA_synth_B.
InterProiIPR008925. aa-tRNA-synth_I_codon-bd.
IPR020752. aa-tRNA-synth_I_codon-bd_sub1.
IPR020751. aa-tRNA-synth_I_codon-bd_sub2.
IPR001412. aa-tRNA-synth_I_CS.
IPR004527. Glu-tRNA-ligase_bac/mito.
IPR000924. Glu/Gln-tRNA-synth.
IPR020061. Glu/Gln-tRNA-synth_Ib_a-bdl.
IPR020058. Glu/Gln-tRNA-synth_Ib_cat-dom.
IPR014729. Rossmann-like_a/b/a_fold.
[Graphical view]
PANTHERiPTHR10119. PTHR10119. 1 hit.
PfamiPF00749. tRNA-synt_1c. 1 hit.
[Graphical view]
PRINTSiPR00987. TRNASYNTHGLU.
SUPFAMiSSF48163. SSF48163. 1 hit.
TIGRFAMsiTIGR00464. gltX_bact. 1 hit.
PROSITEiPS00178. AA_TRNA_LIGASE_I. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P27000-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MVVTRIAPSP TGDPHVGTAY IALFNYAWAR RNGGRFIVRI EDTDRARYVP
60 70 80 90 100
GAEERILAAL KWLGLSYDEG PDVGGPHGPY RQSERLPLYQ KYAEELLKRG
110 120 130 140 150
WAYRAFETPE ELEQIRKEKG GYDGRARNIP PEEAEERARR GEPHVIRLKV
160 170 180 190 200
PRPGTTEVKD ELRGVVVYDN QEIPDVVLLK SDGYPTYHLA NVVDDHLMGV
210 220 230 240 250
TDVIRAEEWL VSTPIHVLLY RAFGWEAPRF YHMPLLRNPD KTKISKRKSH
260 270 280 290 300
TSLDWYKAEG FLPEALRNYL CLMGFSMPDG REIFTLEEFI QAFTWERVSL
310 320 330 340 350
GGPVFDLEKL RWMNGKYIRE VLSLEEVAER VKPFLREAGL SWESEAYLRR
360 370 380 390 400
AVELMRPRFD TLKEFPEKAR YLFTEDYPVS EKAQRKLEEG LPLLKELYPR
410 420 430 440 450
LRAQEEWTEA ALEALLRGFA AEKGVKLGQV AQPLRAALTG SLETPGLFEI
460
LALLGKERAL RRLERALA
Length:468
Mass (Da):53,910
Last modified:March 28, 2005 - v2
Checksum:i920E7F3363AF19E9
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti74 – 774GGPH → AAPT in CAA45854 (PubMed:1541262).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X64557 Genomic DNA. Translation: CAA45854.1.
AP008226 Genomic DNA. Translation: BAD70261.1.
RefSeqiWP_011227935.1. NC_006461.1.
YP_143704.1. NC_006461.1.

Genome annotation databases

EnsemblBacteriaiBAD70261; BAD70261; BAD70261.
GeneIDi3168748.
KEGGittj:TTHA0438.
PATRICi23955847. VBITheThe93045_0438.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X64557 Genomic DNA. Translation: CAA45854.1.
AP008226 Genomic DNA. Translation: BAD70261.1.
RefSeqiWP_011227935.1. NC_006461.1.
YP_143704.1. NC_006461.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1G59X-ray2.40A/C1-468[»]
1GLNX-ray2.50A1-468[»]
1J09X-ray1.80A1-468[»]
1N75X-ray1.90A1-468[»]
1N77X-ray2.40A/B1-468[»]
1N78X-ray2.10A/B1-468[»]
2CUZX-ray1.98A1-468[»]
2CV0X-ray2.40A/B1-468[»]
2CV1X-ray2.41A/B1-468[»]
2CV2X-ray2.69A/B1-468[»]
2DXIX-ray2.20A/B1-468[»]
ProteinModelPortaliP27000.
SMRiP27000. Positions 1-468.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-29168N.
STRINGi300852.TTHA0438.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiBAD70261; BAD70261; BAD70261.
GeneIDi3168748.
KEGGittj:TTHA0438.
PATRICi23955847. VBITheThe93045_0438.

Phylogenomic databases

eggNOGiCOG0008.
HOGENOMiHOG000252720.
KOiK01885.
OMAiAFRCFCT.
OrthoDBiEOG6DRPF7.
PhylomeDBiP27000.

Enzyme and pathway databases

BioCyciTTHE300852:GH8R-459-MONOMER.
BRENDAi6.1.1.17. 2305.

Miscellaneous databases

EvolutionaryTraceiP27000.

Family and domain databases

Gene3Di1.10.10.350. 1 hit.
1.10.1160.10. 1 hit.
1.10.8.70. 1 hit.
3.40.50.620. 2 hits.
HAMAPiMF_00022_B. Glu_tRNA_synth_B.
InterProiIPR008925. aa-tRNA-synth_I_codon-bd.
IPR020752. aa-tRNA-synth_I_codon-bd_sub1.
IPR020751. aa-tRNA-synth_I_codon-bd_sub2.
IPR001412. aa-tRNA-synth_I_CS.
IPR004527. Glu-tRNA-ligase_bac/mito.
IPR000924. Glu/Gln-tRNA-synth.
IPR020061. Glu/Gln-tRNA-synth_Ib_a-bdl.
IPR020058. Glu/Gln-tRNA-synth_Ib_cat-dom.
IPR014729. Rossmann-like_a/b/a_fold.
[Graphical view]
PANTHERiPTHR10119. PTHR10119. 1 hit.
PfamiPF00749. tRNA-synt_1c. 1 hit.
[Graphical view]
PRINTSiPR00987. TRNASYNTHGLU.
SUPFAMiSSF48163. SSF48163. 1 hit.
TIGRFAMsiTIGR00464. gltX_bact. 1 hit.
PROSITEiPS00178. AA_TRNA_LIGASE_I. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Glutamyl-tRNA synthetase from Thermus thermophilus HB8. Molecular cloning of the gltX gene and crystallization of the overproduced protein."
    Nureki O., Suzuki K., Hara-Yokoyama M., Kohno T., Matsuzawa H., Ohta T., Shimizu T., Morikawa K., Miyazawa T., Yokoyama S.
    Eur. J. Biochem. 204:465-472(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "Complete genome sequence of Thermus thermophilus HB8."
    Masui R., Kurokawa K., Nakagawa N., Tokunaga F., Koyama Y., Shibata T., Oshima T., Yokoyama S., Yasunaga T., Kuramitsu S.
    Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: HB8 / ATCC 27634 / DSM 579.
  3. "Architectures of class-defining and specific domains of glutamyl-tRNA synthetase."
    Nureki O., Vassylyev D.G., Katayanagi K., Shimizu T., Sekine S., Kigawa T., Miyazawa T., Yokoyama S., Morikawa K.
    Science 267:1958-1965(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).
  4. "Structural basis for anticodon recognition by discriminating glutamyl-tRNA synthetase."
    Sekine S., Nureki O., Shimada A., Vassylyev D.G., Yokoyama S.
    Nat. Struct. Biol. 8:203-206(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) IN COMPLEX WITH TRNA-GLU, FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF ARG-358.
  5. "ATP binding by glutamyl-tRNA synthetase is switched to the productive mode by tRNA binding."
    Sekine S., Nureki O., Dubois D.Y., Bernier S., Chenevert R., Lapointe J., Vassylyev D.G., Yokoyama S.
    EMBO J. 22:676-688(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) IN COMPLEXES WITH ATP; GLUTAMATE AND TRNA.
  6. "Structural bases of transfer RNA-dependent amino acid recognition and activation by glutamyl-tRNA synthetase."
    Sekine S., Shichiri M., Bernier S., Chenevert R., Lapointe J., Yokoyama S.
    Structure 14:1791-1799(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) IN COMPLEXES WITH ATP; GLUTAMATE AND TRNA, FUNCTION, ENZYME REGULATION.

Entry informationi

Entry nameiSYE_THET8
AccessioniPrimary (citable) accession number: P27000
Secondary accession number(s): Q5SL55
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 31, 1992
Last sequence update: March 28, 2005
Last modified: March 31, 2015
This is version 116 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Aminoacyl-tRNA synthetases
    List of aminoacyl-tRNA synthetase entries
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.