Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
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)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei243 – 2431ATPUniRule 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

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)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 446446Glutamate--tRNA ligasePRO_0000119496Add
BLAST

Interactioni

Subunit structurei

Monomer.UniRule annotation

Protein-protein interaction databases

STRINGi1064539.AZOBR_40356.

Structurei

3D structure databases

ProteinModelPortaliP45631.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi9 – 1911"HIGH" regionAdd
BLAST
Motifi240 – 2445"KMSKS" region

Sequence similaritiesi

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

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.

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)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti6 – 61P → R in AAA61907 (Ref. 1) Curated
Sequence conflicti39 – 391V → L in AAA61907 (Ref. 1) Curated
Sequence conflicti80 – 812AT → RY in AAA61907 (Ref. 1) Curated
Sequence conflicti112 – 1121S → V in AAA61907 (Ref. 1) Curated
Sequence conflicti137 – 1371A → S in AAA61907 (Ref. 1) Curated
Sequence conflicti142 – 1421P → R in AAA61907 (Ref. 1) Curated
Sequence conflicti168 – 1681S → A in AAA61907 (Ref. 1) Curated
Sequence conflicti177 – 1771A → R in AAA61907 (Ref. 1) Curated
Sequence conflicti207 – 2071L → V in AAA61907 (Ref. 1) Curated
Sequence conflicti220 – 2234VGGA → LTNSEGGGV (Ref. 1) Curated
Sequence conflicti378 – 3781T → A in AAA61907 (Ref. 1) Curated
Sequence conflicti382 – 3821K → E in AAA61907 (Ref. 1) Curated
Sequence conflicti423 – 4242GQ → PE in AAA61907 (Ref. 1) Curated
Sequence conflicti438 – 4381H → E in AAA61907 (Ref. 1) Curated

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.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi1064539.AZOBR_40356.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

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]
ProtoNetiSearch...

Publicationsi

  1. Costacurta A., Keijers V., Vanderleyden J.
    Submitted (NOV-1994) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: Sp245.
  2. "Identification and isolation of the indole-3-pyruvate decarboxylase gene from Azospirillum brasilense Sp7: sequencing and functional analysis of the gene locus."
    Zimmer W., Wesche M., Timmermans L.
    Curr. Microbiol. 36:327-331(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 29145 / Sp7 / DSM 1690 / IMET 11303.

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: June 24, 2015
This is version 85 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

External Data

Dasty 3

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 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.