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Protein

Glutamate--tRNA ligase 1

Gene

gltX1

Organism
Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099)
Status
Reviewed-Annotation score: Annotation score: 3 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).By similarity

Catalytic activityi

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

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei253ATPBy similarity1

GO - Molecular functioni

GO - Biological processi

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 1 (EC:6.1.1.17)
Alternative name(s):
Glutamyl-tRNA synthetase 1
Short name:
GluRS 1
Gene namesi
Name:gltX1
Ordered Locus Names:TM_1351
OrganismiThermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099)
Taxonomic identifieri243274 [NCBI]
Taxonomic lineageiBacteriaThermotogaeThermotogalesThermotogaceaeThermotoga
Proteomesi
  • UP000008183 Componenti: Chromosome

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001196801 – 469Glutamate--tRNA ligase 1Add BLAST469

Proteomic databases

PRIDEiQ9X172.

Interactioni

Subunit structurei

Monomer.By similarity

Protein-protein interaction databases

STRINGi243274.TM1351.

Structurei

Secondary structure

1469
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi3 – 6Combined sources4
Helixi16 – 32Combined sources17
Beta strandi35 – 38Combined sources4
Helixi48 – 50Combined sources3
Helixi51 – 63Combined sources13
Beta strandi68 – 70Combined sources3
Turni71 – 73Combined sources3
Helixi82 – 85Combined sources4
Helixi86 – 98Combined sources13
Beta strandi101 – 105Combined sources5
Turni110 – 112Combined sources3
Helixi113 – 121Combined sources9
Helixi130 – 133Combined sources4
Turni134 – 136Combined sources3
Helixi139 – 147Combined sources9
Beta strandi153 – 156Combined sources4
Beta strandi163 – 167Combined sources5
Turni168 – 170Combined sources3
Beta strandi171 – 175Combined sources5
Beta strandi182 – 186Combined sources5
Helixi194 – 204Combined sources11
Beta strandi208 – 213Combined sources6
Helixi214 – 216Combined sources3
Helixi217 – 229Combined sources13
Beta strandi236 – 240Combined sources5
Beta strandi248 – 250Combined sources3
Helixi253 – 255Combined sources3
Helixi260 – 266Combined sources7
Helixi270 – 278Combined sources9
Beta strandi280 – 282Combined sources3
Helixi293 – 299Combined sources7
Helixi302 – 304Combined sources3
Helixi314 – 327Combined sources14
Helixi330 – 343Combined sources14
Helixi351 – 361Combined sources11
Turni362 – 364Combined sources3
Helixi368 – 370Combined sources3
Helixi371 – 374Combined sources4
Helixi376 – 378Combined sources3
Helixi389 – 391Combined sources3
Helixi392 – 401Combined sources10
Turni402 – 404Combined sources3
Helixi409 – 423Combined sources15
Helixi427 – 438Combined sources12
Beta strandi440 – 442Combined sources3
Helixi447 – 453Combined sources7
Helixi456 – 466Combined sources11

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2O5RX-ray2.34A1-469[»]
ProteinModelPortaliQ9X172.
SMRiQ9X172.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9X172.

Family & Domainsi

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi8 – 18"HIGH" regionAdd BLAST11
Motifi250 – 254"KMSKS" region5

Sequence similaritiesi

Phylogenomic databases

eggNOGiENOG4105C20. Bacteria.
COG0008. LUCA.
InParanoidiQ9X172.
KOiK09698.
OMAiTQMANKE.

Family and domain databases

CDDicd00808. GluRS_core. 1 hit.
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. 1 hit.
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.
IPR033910. GluRS_core.
IPR014729. Rossmann-like_a/b/a_fold.
[Graphical view]
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.

Q9X172-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MVRVRFAPSP TGFLHVGGAR TALFNFLFAR KEKGKFILRI EDTDLERSER
60 70 80 90 100
EYEEKLMESL RWLGLLWDEG PDVGGDHGPY RQSERVEIYR EHAERLVKEG
110 120 130 140 150
KAYYVYAYPE EIEEMREKLL SEGKAPHYSQ EMFEKFDTPE RRREYEEKGL
160 170 180 190 200
RPAVFFKMPR KDYVLNDVVK GEVVFKTGAI GDFVIMRSNG LPTYNFACVV
210 220 230 240 250
DDMLMEITHV IRGDDHLSNT LRQLALYEAF EKAPPVFAHV STILGPDGKK
260 270 280 290 300
LSKRHGATSV EAFRDMGYLP EALVNYLALL GWSHPEGKEL LTLEELISSF
310 320 330 340 350
SLDRLSPNPA IFDPQKLKWM NGYYLRNMPI EKLAELAKPF FEKAGIKIID
360 370 380 390 400
EEYFKKVLEI TKERVEVLSE FPEESRFFFE DPAPVEIPEE MKEVFSQLKE
410 420 430 440 450
ELQNVRWTME EITPVFKKVL KQHGVKPKEF YMTLRRVLTG REEGPELVNI
460
IPLLGKEIFL RRIERSLGG
Length:469
Mass (Da):54,607
Last modified:November 1, 1999 - v1
Checksum:iF27D3AB4FE070BD8
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE000512 Genomic DNA. Translation: AAD36422.1.
PIRiG72264.
RefSeqiNP_229152.1. NC_000853.1.
WP_004081547.1. NZ_CP011107.1.

Genome annotation databases

EnsemblBacteriaiAAD36422; AAD36422; TM_1351.
GeneIDi898129.
KEGGitma:TM1351.
PATRICi23937640. VBITheMar51294_1363.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE000512 Genomic DNA. Translation: AAD36422.1.
PIRiG72264.
RefSeqiNP_229152.1. NC_000853.1.
WP_004081547.1. NZ_CP011107.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2O5RX-ray2.34A1-469[»]
ProteinModelPortaliQ9X172.
SMRiQ9X172.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi243274.TM1351.

Proteomic databases

PRIDEiQ9X172.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAD36422; AAD36422; TM_1351.
GeneIDi898129.
KEGGitma:TM1351.
PATRICi23937640. VBITheMar51294_1363.

Phylogenomic databases

eggNOGiENOG4105C20. Bacteria.
COG0008. LUCA.
InParanoidiQ9X172.
KOiK09698.
OMAiTQMANKE.

Miscellaneous databases

EvolutionaryTraceiQ9X172.

Family and domain databases

CDDicd00808. GluRS_core. 1 hit.
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. 1 hit.
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.
IPR033910. GluRS_core.
IPR014729. Rossmann-like_a/b/a_fold.
[Graphical view]
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...

Entry informationi

Entry nameiSYE1_THEMA
AccessioniPrimary (citable) accession number: Q9X172
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: November 1, 1999
Last modified: November 30, 2016
This is version 120 of the entry and version 1 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

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 one 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.