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P27000

- SYE_THET8

UniProt

P27000 - SYE_THET8

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Protein

Glutamate--tRNA ligase

Gene
gltX, TTHA0438
Organism
Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)
Status
Reviewed - 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).UniRule annotation

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 – 2475ATPUniRule annotation

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.

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: 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 ligaseUniRule annotationPRO_0000119683Add
BLAST

Interactioni

Subunit structurei

Monomer.

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

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
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.

Miscellaneous databases

EvolutionaryTraceiP27000.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni5 – 73Glutamate bindingUniRule annotation
Regioni187 – 1915Glutamate bindingUniRule annotation
Regioni432 – 44716Interaction with tRNAUniRule annotationAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi8 – 1811"HIGH" regionUniRule annotationAdd
BLAST
Motifi243 – 2475"KMSKS" regionUniRule annotation

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0008.
HOGENOMiHOG000252720.
KOiK01885.
OMAiVTGQTHG.
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

MVVTRIAPSP TGDPHVGTAY IALFNYAWAR RNGGRFIVRI EDTDRARYVP    50
GAEERILAAL KWLGLSYDEG PDVGGPHGPY RQSERLPLYQ KYAEELLKRG 100
WAYRAFETPE ELEQIRKEKG GYDGRARNIP PEEAEERARR GEPHVIRLKV 150
PRPGTTEVKD ELRGVVVYDN QEIPDVVLLK SDGYPTYHLA NVVDDHLMGV 200
TDVIRAEEWL VSTPIHVLLY RAFGWEAPRF YHMPLLRNPD KTKISKRKSH 250
TSLDWYKAEG FLPEALRNYL CLMGFSMPDG REIFTLEEFI QAFTWERVSL 300
GGPVFDLEKL RWMNGKYIRE VLSLEEVAER VKPFLREAGL SWESEAYLRR 350
AVELMRPRFD TLKEFPEKAR YLFTEDYPVS EKAQRKLEEG LPLLKELYPR 400
LRAQEEWTEA ALEALLRGFA AEKGVKLGQV AQPLRAALTG SLETPGLFEI 450
LALLGKERAL RRLERALA 468
Length:468
Mass (Da):53,910
Last modified:March 29, 2005 - v2
Checksum:i920E7F3363AF19E9
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti74 – 774GGPH → AAPT in CAA45854. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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:
EMBL
GenBank
DDBJ
Links Updated
X64557 Genomic DNA. Translation: CAA45854.1 .
AP008226 Genomic DNA. Translation: BAD70261.1 .
RefSeqi WP_011227935.1. NC_006461.1.
YP_143704.1. NC_006461.1.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1G59 X-ray 2.40 A/C 1-468 [» ]
1GLN X-ray 2.50 A 1-468 [» ]
1J09 X-ray 1.80 A 1-468 [» ]
1N75 X-ray 1.90 A 1-468 [» ]
1N77 X-ray 2.40 A/B 1-468 [» ]
1N78 X-ray 2.10 A/B 1-468 [» ]
2CUZ X-ray 1.98 A 1-468 [» ]
2CV0 X-ray 2.40 A/B 1-468 [» ]
2CV1 X-ray 2.41 A/B 1-468 [» ]
2CV2 X-ray 2.69 A/B 1-468 [» ]
2DXI X-ray 2.20 A/B 1-468 [» ]
ProteinModelPortali P27000.
SMRi P27000. Positions 1-468.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

DIPi DIP-29168N.
STRINGi 300852.TTHA0438.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai BAD70261 ; BAD70261 ; BAD70261 .
GeneIDi 3168748.
KEGGi ttj:TTHA0438.
PATRICi 23955847. VBITheThe93045_0438.

Phylogenomic databases

eggNOGi COG0008.
HOGENOMi HOG000252720.
KOi K01885.
OMAi VTGQTHG.
OrthoDBi EOG6DRPF7.
PhylomeDBi P27000.

Enzyme and pathway databases

BioCyci TTHE300852:GH8R-459-MONOMER.

Miscellaneous databases

EvolutionaryTracei P27000.

Family and domain databases

Gene3Di 1.10.10.350. 1 hit.
1.10.1160.10. 1 hit.
1.10.8.70. 1 hit.
3.40.50.620. 2 hits.
HAMAPi MF_00022_B. Glu_tRNA_synth_B.
InterProi IPR008925. 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 ]
PANTHERi PTHR10119. PTHR10119. 1 hit.
Pfami PF00749. tRNA-synt_1c. 1 hit.
[Graphical view ]
PRINTSi PR00987. TRNASYNTHGLU.
SUPFAMi SSF48163. SSF48163. 1 hit.
TIGRFAMsi TIGR00464. gltX_bact. 1 hit.
PROSITEi PS00178. AA_TRNA_LIGASE_I. 1 hit.
[Graphical view ]
ProtoNeti Search...

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(1992) [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 (NOV-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(1995) [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(2001) [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(2003) [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(2006) [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: August 1, 1992
Last sequence update: March 29, 2005
Last modified: September 3, 2014
This is version 110 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

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