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Q8DLI5

- SYE_THEEB

UniProt

Q8DLI5 - SYE_THEEB

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Protein

Glutamate--tRNA ligase

Gene

gltX

Organism
Thermosynechococcus elongatus (strain BP-1)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli

Functioni

Non-discriminating glutamyl-tRNA synthetase. 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). Acylates both tRNA(Glu) and tRNA(Gln) with glutamate, but has 13-fold higher efficiency with tRNA(Glu).1 Publication

Catalytic activityi

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

Cofactori

Note: Does not require zinc.

Kineticsi

  1. KM=0.79 µM for tRNA-Glu1 Publication
  2. KM=3.7 µM for tRNA-Gln1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei6 – 61Glutamate1 Publication
Binding sitei192 – 1921Glutamate1 Publication
Binding sitei251 – 2511ATPBy similarity

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

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:tll0506
OrganismiThermosynechococcus elongatus (strain BP-1)
Taxonomic identifieri197221 [NCBI]
Taxonomic lineageiBacteriaCyanobacteriaOscillatoriophycideaeChroococcalesThermosynechococcus
ProteomesiUP000000440: Chromosome

Subcellular locationi

GO - Cellular componenti

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

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 485485Glutamate--tRNA ligasePRO_0000119674Add
BLAST

Interactioni

Subunit structurei

Monomer.By similarity

Protein-protein interaction databases

STRINGi197221.tll0506.

Structurei

Secondary structure

1
485
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi4 – 74Combined sources
Helixi17 – 3216Combined sources
Beta strandi36 – 416Combined sources
Beta strandi45 – 484Combined sources
Helixi51 – 6313Combined sources
Beta strandi69 – 746Combined sources
Helixi75 – 773Combined sources
Helixi79 – 9113Combined sources
Beta strandi94 – 985Combined sources
Helixi102 – 11514Combined sources
Turni124 – 1274Combined sources
Helixi130 – 1389Combined sources
Beta strandi144 – 1474Combined sources
Beta strandi154 – 1596Combined sources
Turni160 – 1623Combined sources
Beta strandi163 – 1686Combined sources
Helixi169 – 1724Combined sources
Beta strandi174 – 1796Combined sources
Helixi192 – 20211Combined sources
Beta strandi206 – 2116Combined sources
Helixi212 – 2165Combined sources
Helixi217 – 22711Combined sources
Beta strandi234 – 2385Combined sources
Beta strandi244 – 2485Combined sources
Helixi258 – 2636Combined sources
Helixi268 – 27710Combined sources
Turni284 – 2863Combined sources
Helixi292 – 2987Combined sources
Helixi313 – 32412Combined sources
Helixi329 – 34214Combined sources
Turni349 – 3524Combined sources
Helixi353 – 36311Combined sources
Helixi364 – 3663Combined sources
Helixi370 – 3723Combined sources
Helixi373 – 3819Combined sources
Beta strandi382 – 3843Combined sources
Helixi389 – 3957Combined sources
Helixi400 – 41011Combined sources
Beta strandi413 – 4153Combined sources
Helixi419 – 43315Combined sources
Helixi437 – 44913Combined sources
Beta strandi450 – 4534Combined sources
Helixi457 – 46610Combined sources
Helixi470 – 48415Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2CFOX-ray2.45A/B2-485[»]
ProteinModelPortaliQ8DLI5.
SMRiQ8DLI5. Positions 2-485.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ8DLI5.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni210 – 2145Glutamate binding

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi9 – 1911"HIGH" regionAdd
BLAST
Motifi248 – 2525"KMSKS" region

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0008.
HOGENOMiHOG000252722.
KOiK01885.
OMAiDSHEHHA.
OrthoDBiEOG6DRPF7.

Family and domain databases

Gene3Di1.10.10.350. 1 hit.
1.10.1160.10. 1 hit.
3.40.50.620. 2 hits.
HAMAPiMF_00022_B. Glu_tRNA_synth_B.
InterProiIPR008925. aa-tRNA-synth_I_codon-bd.
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.

Q8DLI5-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MTVRVRLAPS PTGNLHIGTA RTAVFNWLYA RHRGGKFILR IEDTDRERSR
60 70 80 90 100
PEYTENILEG LQWLGLTWDE GPYFQSDRLD LYRQAIQTLL DKGLAYYCYC
110 120 130 140 150
TPEELEALRA EQKAKGQAPR YDNRHRHLTP EEQAAFEAAG RTPVIRFKIE
160 170 180 190 200
DDRQIEWQDL VRGRVSWQGA DLGGDMVIAR AAPRGEIGYP LYNLVVVVDD
210 220 230 240 250
IAMGITDVIR GEDHIGNTPK QILLYEALGA TPPNFAHTPL ILNSTGQKLS
260 270 280 290 300
KRDGVTSISD FRAMGYLAPA LANYMTLLGW SPPEGVGELF TLDLAAKHFS
310 320 330 340 350
FERINKAGAR FDWDKLNWLN RQYIQQLEPE EFLAELIPLW QGAGYAFDEE
360 370 380 390 400
RDRPWLFDLA QLLQPGLNTL REAIDQGAVF FIPSVTFDSE AMAQLGQPQS
410 420 430 440 450
ATILAYLLEH LPAEPALTVA MGQQLIQQAA KAAGVKKGAT MRTLRAALTG
460 470 480
AVHGPDLMAA WQILHQRGWD EPRLAAALKQ AQTTS
Length:485
Mass (Da):54,362
Last modified:March 1, 2003 - v1
Checksum:iC3547C6415FDDCBA
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BA000039 Genomic DNA. Translation: BAC08058.1.
RefSeqiNP_681296.1. NC_004113.1.
WP_011056357.1. NC_004113.1.

Genome annotation databases

EnsemblBacteriaiBAC08058; BAC08058; BAC08058.
GeneIDi1012165.
KEGGitel:tll0506.
PATRICi23926260. VBITheElo119873_0533.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BA000039 Genomic DNA. Translation: BAC08058.1 .
RefSeqi NP_681296.1. NC_004113.1.
WP_011056357.1. NC_004113.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2CFO X-ray 2.45 A/B 2-485 [» ]
ProteinModelPortali Q8DLI5.
SMRi Q8DLI5. Positions 2-485.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 197221.tll0506.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai BAC08058 ; BAC08058 ; BAC08058 .
GeneIDi 1012165.
KEGGi tel:tll0506.
PATRICi 23926260. VBITheElo119873_0533.

Phylogenomic databases

eggNOGi COG0008.
HOGENOMi HOG000252722.
KOi K01885.
OMAi DSHEHHA.
OrthoDBi EOG6DRPF7.

Miscellaneous databases

EvolutionaryTracei Q8DLI5.

Family and domain databases

Gene3Di 1.10.10.350. 1 hit.
1.10.1160.10. 1 hit.
3.40.50.620. 2 hits.
HAMAPi MF_00022_B. Glu_tRNA_synth_B.
InterProi IPR008925. aa-tRNA-synth_I_codon-bd.
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. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: BP-1.
  2. "Crystal structure of a non-discriminating glutamyl-tRNA synthetase."
    Schulze J.O., Masoumi A., Nickel D., Jahn M., Jahn D., Schubert W.-D., Heinz D.W.
    J. Mol. Biol. 361:888-897(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.45 ANGSTROMS) IN COMPLEX WITH GLUTAMATE, FUNCTION, ABSENCE OF COFACTOR REQUIREMENT, BIOPHYSICOCHEMICAL PROPERTIES.

Entry informationi

Entry nameiSYE_THEEB
AccessioniPrimary (citable) accession number: Q8DLI5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 23, 2003
Last sequence update: March 1, 2003
Last modified: November 26, 2014
This is version 76 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Miscellaneous

This organism lacks a tRNA synthetase for tRNA(Gln). Instead, tRNA(Gln) is first charged with Glu, and then the bound glutamate is converted to glutamine by GatCAB.

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