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Protein

Glutamate--tRNA ligase

Gene

gltX

Organism
Azospirillum brasilense
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Protein inferred from homologyi

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

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei243ATPUniRule annotation1

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 ligaseUniRule annotation (EC:6.1.1.17UniRule annotation)
Alternative name(s):
Glutamyl-tRNA synthetaseUniRule annotation
Short name:
GluRSUniRule annotation
Gene namesi
Name:gltXUniRule annotation
OrganismiAzospirillum brasilense
Taxonomic identifieri192 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaAlphaproteobacteriaRhodospirillalesRhodospirillaceaeAzospirillum

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_00001194961 – 446Glutamate--tRNA ligaseAdd BLAST446

Interactioni

Subunit structurei

Monomer.UniRule annotation

Structurei

3D structure databases

ProteinModelPortaliP45631.
SMRiP45631.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi9 – 19"HIGH" regionAdd BLAST11
Motifi240 – 244"KMSKS" region5

Sequence similaritiesi

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

Family and domain databases

CDDicd00808. GluRS_core. 1 hit.
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. 1 hit.
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.
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.

P45631-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSVAVPFAPS PTGLLHVGNV RLALVNWLFA RKAGGNFLVR LDDTDEERSK
60 70 80 90 100
PEYAEGIERD LTWLGLTWDR FARESDRYGA TDEVAAALKA SGRLYPCYET
110 120 130 140 150
PEELNLKRAS LSSQGRPPIY DRAALRLGDA DRARLEAEGR KPHWRFKLEH
160 170 180 190 200
TPVEWTDLVR GPVHFEGSAL SDPVLIAEDG RPLYTLTSVV DDADLAITHV
210 220 230 240 250
IRGEDHLANT AVQIQIFEAV GGAVPVFAHL PLLTDATGQG LSKRLGSLSV
260 270 280 290 300
ASLREEEGIE PMALASLLAK LGTSDAIEPR LTLDELVAEF DIAKVSRATP
310 320 330 340 350
KFDPEELLRL NARILHLLPF ERVAGELAAS VWMMPTPAFW EAVPNLSRVA
360 370 380 390 400
EARDWWAVTH APVARRRTIP LFLAEAATLL PKEPWDLSTW GTWTGAVKAK
410 420 430 440
TGRKGKDLFL PLRRALTGRD HGGQLKNLLP LIGRTRAHKR LAGETA
Length:446
Mass (Da):49,179
Last modified:December 15, 1998 - v2
Checksum:iA7CE141B79416572
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti6P → R in AAA61907 (Ref. 1) Curated1
Sequence conflicti39V → L in AAA61907 (Ref. 1) Curated1
Sequence conflicti80 – 81AT → RY in AAA61907 (Ref. 1) Curated2
Sequence conflicti112S → V in AAA61907 (Ref. 1) Curated1
Sequence conflicti137A → S in AAA61907 (Ref. 1) Curated1
Sequence conflicti142P → R in AAA61907 (Ref. 1) Curated1
Sequence conflicti168S → A in AAA61907 (Ref. 1) Curated1
Sequence conflicti177A → R in AAA61907 (Ref. 1) Curated1
Sequence conflicti207L → V in AAA61907 (Ref. 1) Curated1
Sequence conflicti220 – 223VGGA → LTNSEGGGV (Ref. 1) Curated4
Sequence conflicti378T → A in AAA61907 (Ref. 1) Curated1
Sequence conflicti382K → E in AAA61907 (Ref. 1) Curated1
Sequence conflicti423 – 424GQ → PE in AAA61907 (Ref. 1) Curated2
Sequence conflicti438H → E in AAA61907 (Ref. 1) Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U17699 Genomic DNA. Translation: AAA61907.1.
X99587 Genomic DNA. Translation: CAA67900.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U17699 Genomic DNA. Translation: AAA61907.1.
X99587 Genomic DNA. Translation: CAA67900.1.

3D structure databases

ProteinModelPortaliP45631.
SMRiP45631.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Family and domain databases

CDDicd00808. GluRS_core. 1 hit.
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. 1 hit.
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.
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 nameiSYE_AZOBR
AccessioniPrimary (citable) accession number: P45631
Secondary accession number(s): O07044
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: December 15, 1998
Last modified: November 30, 2016
This is version 89 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Documents

  1. Aminoacyl-tRNA synthetases
    List of aminoacyl-tRNA synthetase entries
  2. 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.