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Protein

Glutamate--tRNA ligase

Gene

gltX

Organism
Methanothermobacter thermautotrophicus (strain ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H) (Methanobacterium thermoautotrophicum)
Status
Reviewed-Annotation score: Annotation score: 2 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).UniRule annotation

Catalytic activityi

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

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

Enzyme and pathway databases

BRENDAi6.1.1.17. 7219.

Names & Taxonomyi

Protein namesi
Recommended name:
Glutamate--tRNA ligaseUniRule annotation (EC:6.1.1.17UniRule annotation)
Alternative name(s):
Glutamyl-tRNA synthetaseUniRule annotation
Short name:
GluRSUniRule annotation
Gene namesi
Name:gltXUniRule annotation
Ordered Locus Names:MTH_51
OrganismiMethanothermobacter thermautotrophicus (strain ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H) (Methanobacterium thermoautotrophicum)
Taxonomic identifieri187420 [NCBI]
Taxonomic lineageiArchaeaEuryarchaeotaMethanobacteriaMethanobacterialesMethanobacteriaceaeMethanothermobacter
Proteomesi
  • UP000005223 Componenti: Chromosome

Subcellular locationi

  • Cytoplasm UniRule annotation

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001197211 – 553Glutamate--tRNA ligaseAdd BLAST553

Interactioni

Protein-protein interaction databases

STRINGi187420.MTH51.

Structurei

Secondary structure

1553
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi98 – 101Combined sources4
Beta strandi105 – 108Combined sources4
Helixi111 – 126Combined sources16
Beta strandi130 – 135Combined sources6
Helixi140 – 142Combined sources3
Helixi147 – 158Combined sources12
Beta strandi163 – 167Combined sources5
Helixi168 – 171Combined sources4
Helixi172 – 184Combined sources13
Beta strandi187 – 191Combined sources5
Helixi195 – 203Combined sources9
Helixi209 – 212Combined sources4
Helixi215 – 224Combined sources10
Helixi225 – 227Combined sources3
Beta strandi234 – 237Combined sources4
Helixi246 – 248Combined sources3
Beta strandi252 – 256Combined sources5
Turni262 – 264Combined sources3
Beta strandi270 – 272Combined sources3
Helixi274 – 284Combined sources11
Beta strandi289 – 292Combined sources4
Helixi299 – 310Combined sources12
Beta strandi316 – 319Combined sources4
Helixi333 – 341Combined sources9
Helixi355 – 360Combined sources6
Helixi365 – 375Combined sources11
Helixi386 – 397Combined sources12
Turni398 – 400Combined sources3
Beta strandi402 – 404Combined sources3
Beta strandi406 – 416Combined sources11
Beta strandi422 – 428Combined sources7
Helixi433 – 435Combined sources3
Beta strandi437 – 449Combined sources13
Beta strandi455 – 460Combined sources6
Turni461 – 463Combined sources3
Beta strandi464 – 469Combined sources6
Beta strandi472 – 477Combined sources6
Helixi480 – 486Combined sources7
Beta strandi489 – 491Combined sources3
Helixi496 – 498Combined sources3
Beta strandi500 – 505Combined sources6
Beta strandi511 – 516Combined sources6
Helixi518 – 522Combined sources5
Beta strandi528 – 531Combined sources4
Turni532 – 534Combined sources3
Beta strandi535 – 541Combined sources7
Beta strandi543 – 552Combined sources10

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3AIIX-ray1.65A1-553[»]
ProteinModelPortaliO26157.
SMRiO26157.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi103 – 113"HIGH" regionAdd BLAST11

Sequence similaritiesi

Belongs to the class-I aminoacyl-tRNA synthetase family.UniRule annotation

Phylogenomic databases

eggNOGiarCOG04302. Archaea.
COG0008. LUCA.
KOiK01885.
OMAiKMYRLME.

Family and domain databases

Gene3Di1.10.1160.10. 1 hit.
3.40.50.620. 2 hits.
HAMAPiMF_00022_A. Glu_tRNA_synth_A. 1 hit.
InterProiIPR001412. aa-tRNA-synth_I_CS.
IPR004526. Glu-tRNA-synth_arc/euk.
IPR000924. Glu/Gln-tRNA-synth.
IPR020061. Glu/Gln-tRNA-synth_Ib_a-bdl.
IPR020058. Glu/Gln-tRNA-synth_Ib_cat-dom.
IPR020059. Glu/Gln-tRNA-synth_Ib_codon-bd.
IPR022888. Glu_tRNA_synth_arc.
IPR011035. Ribosomal_L25/Gln-tRNA_synth.
IPR014729. Rossmann-like_a/b/a_fold.
[Graphical view]
PfamiPF00749. tRNA-synt_1c. 1 hit.
PF03950. tRNA-synt_1c_C. 1 hit.
[Graphical view]
PRINTSiPR00987. TRNASYNTHGLU.
SUPFAMiSSF50715. SSF50715. 1 hit.
TIGRFAMsiTIGR00463. gltX_arch. 1 hit.
PROSITEiPS00178. AA_TRNA_LIGASE_I. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

O26157-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MVPVEDLVYR YALLNAVKHR GRANPGAVMG AVMSNEPELR KMAPQVKEAV
60 70 80 90 100
EAAVERVNSL SPEEQQQEME RLGLEITERK QKKRKGLREL AGVKGEVVLR
110 120 130 140 150
FAPNPSGPLH IGHARAAILN HEYARKYDGR LILRIEDTDP RRVDPEAYDM
160 170 180 190 200
IPADLEWLGV EWDETVIQSD RMETYYEYTE KLIERGGAYV CTCRPEEFRE
210 220 230 240 250
LKNRGEACHC RSLGFRENLQ RWREMFEMKE GSAVVRVKTD LNHPNPAIRD
260 270 280 290 300
WVSMRIVEAE HPRTGTRYRV YPMMNFSVAV DDHLLGVTHV LRGKDHLANR
310 320 330 340 350
EKQEYLYRHL GWEPPEFIHY GRLKMDDVAL STSGAREGIL RGEYSGWDDP
360 370 380 390 400
RLGTLRAIAR RGIRPEAIRK LMVEIGVKIA DSTMSWKKIY GLNRSILEEE
410 420 430 440 450
ARRYFFAADP VKLEVVGLPG PVRVERPLHP DHPEIGNRVL ELRGEVYLPG
460 470 480 490 500
DDLGEGPLRL IDAVNVIYSG GELRYHSEGI EEARELGASM IHWVPAESAL
510 520 530 540 550
EAEVIMPDAS RVRGVIEADA SELEVDDVVQ LERFGFARLD SAGPGMVFYY

AHK
Length:553
Mass (Da):63,090
Last modified:January 1, 1998 - v1
Checksum:iC6DB8AE92C2FEE6B
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE000666 Genomic DNA. Translation: AAB84558.1.
PIRiB69167.
RefSeqiWP_010875691.1. NC_000916.1.

Genome annotation databases

EnsemblBacteriaiAAB84558; AAB84558; MTH_51.
GeneIDi1470013.
KEGGimth:MTH_51.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE000666 Genomic DNA. Translation: AAB84558.1.
PIRiB69167.
RefSeqiWP_010875691.1. NC_000916.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3AIIX-ray1.65A1-553[»]
ProteinModelPortaliO26157.
SMRiO26157.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi187420.MTH51.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAB84558; AAB84558; MTH_51.
GeneIDi1470013.
KEGGimth:MTH_51.

Phylogenomic databases

eggNOGiarCOG04302. Archaea.
COG0008. LUCA.
KOiK01885.
OMAiKMYRLME.

Enzyme and pathway databases

BRENDAi6.1.1.17. 7219.

Family and domain databases

Gene3Di1.10.1160.10. 1 hit.
3.40.50.620. 2 hits.
HAMAPiMF_00022_A. Glu_tRNA_synth_A. 1 hit.
InterProiIPR001412. aa-tRNA-synth_I_CS.
IPR004526. Glu-tRNA-synth_arc/euk.
IPR000924. Glu/Gln-tRNA-synth.
IPR020061. Glu/Gln-tRNA-synth_Ib_a-bdl.
IPR020058. Glu/Gln-tRNA-synth_Ib_cat-dom.
IPR020059. Glu/Gln-tRNA-synth_Ib_codon-bd.
IPR022888. Glu_tRNA_synth_arc.
IPR011035. Ribosomal_L25/Gln-tRNA_synth.
IPR014729. Rossmann-like_a/b/a_fold.
[Graphical view]
PfamiPF00749. tRNA-synt_1c. 1 hit.
PF03950. tRNA-synt_1c_C. 1 hit.
[Graphical view]
PRINTSiPR00987. TRNASYNTHGLU.
SUPFAMiSSF50715. SSF50715. 1 hit.
TIGRFAMsiTIGR00463. gltX_arch. 1 hit.
PROSITEiPS00178. AA_TRNA_LIGASE_I. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiSYE_METTH
AccessioniPrimary (citable) accession number: O26157
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: January 1, 1998
Last modified: November 2, 2016
This is version 105 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.