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P45631 (SYE_AZOBR) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 81. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Glutamate--tRNA ligase

EC=6.1.1.17
Alternative name(s):
Glutamyl-tRNA synthetase
Short name=GluRS
Gene names
Name:gltX
OrganismAzospirillum brasilense
Taxonomic identifier192 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRhodospirillalesRhodospirillaceaeAzospirillum

Protein attributes

Sequence length446 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

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. HAMAP-Rule MF_00022

Catalytic activity

ATP + L-glutamate + tRNA(Glu) = AMP + diphosphate + L-glutamyl-tRNA(Glu). HAMAP-Rule MF_00022

Subunit structure

Monomer By similarity. HAMAP-Rule MF_00022

Subcellular location

Cytoplasm By similarity HAMAP-Rule MF_00022.

Sequence similarities

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

Ontologies

Keywords
   Biological processProtein biosynthesis
   Cellular componentCytoplasm
   LigandATP-binding
Nucleotide-binding
   Molecular functionAminoacyl-tRNA synthetase
Ligase
Gene Ontology (GO)
   Biological_processglutamyl-tRNA aminoacylation

Inferred from electronic annotation. Source: UniProtKB-HAMAP

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-HAMAP

glutamate-tRNA ligase activity

Inferred from electronic annotation. Source: UniProtKB-HAMAP

tRNA binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 446446Glutamate--tRNA ligase HAMAP-Rule MF_00022
PRO_0000119496

Regions

Motif9 – 1911"HIGH" region HAMAP-Rule MF_00022
Motif240 – 2445"KMSKS" region HAMAP-Rule MF_00022

Sites

Binding site2431ATP By similarity

Experimental info

Sequence conflict61P → R in AAA61907. Ref.1
Sequence conflict391V → L in AAA61907. Ref.1
Sequence conflict80 – 812AT → RY in AAA61907. Ref.1
Sequence conflict1121S → V in AAA61907. Ref.1
Sequence conflict1371A → S in AAA61907. Ref.1
Sequence conflict1421P → R in AAA61907. Ref.1
Sequence conflict1681S → A in AAA61907. Ref.1
Sequence conflict1771A → R in AAA61907. Ref.1
Sequence conflict2071L → V in AAA61907. Ref.1
Sequence conflict220 – 2234VGGA → LTNSEGGGV Ref.1
Sequence conflict3781T → A in AAA61907. Ref.1
Sequence conflict3821K → E in AAA61907. Ref.1
Sequence conflict423 – 4242GQ → PE in AAA61907. Ref.1
Sequence conflict4381H → E in AAA61907. Ref.1

Sequences

Sequence LengthMass (Da)Tools
P45631 [UniParc].

Last modified December 15, 1998. Version 2.
Checksum: A7CE141B79416572

FASTA44649,179
        10         20         30         40         50         60 
MSVAVPFAPS PTGLLHVGNV RLALVNWLFA RKAGGNFLVR LDDTDEERSK PEYAEGIERD 

        70         80         90        100        110        120 
LTWLGLTWDR FARESDRYGA TDEVAAALKA SGRLYPCYET PEELNLKRAS LSSQGRPPIY 

       130        140        150        160        170        180 
DRAALRLGDA DRARLEAEGR KPHWRFKLEH TPVEWTDLVR GPVHFEGSAL SDPVLIAEDG 

       190        200        210        220        230        240 
RPLYTLTSVV DDADLAITHV IRGEDHLANT AVQIQIFEAV GGAVPVFAHL PLLTDATGQG 

       250        260        270        280        290        300 
LSKRLGSLSV ASLREEEGIE PMALASLLAK LGTSDAIEPR LTLDELVAEF DIAKVSRATP 

       310        320        330        340        350        360 
KFDPEELLRL NARILHLLPF ERVAGELAAS VWMMPTPAFW EAVPNLSRVA EARDWWAVTH 

       370        380        390        400        410        420 
APVARRRTIP LFLAEAATLL PKEPWDLSTW GTWTGAVKAK TGRKGKDLFL PLRRALTGRD 

       430        440 
HGGQLKNLLP LIGRTRAHKR LAGETA 

« Hide

References

[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.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U17699 Genomic DNA. Translation: AAA61907.1.
X99587 Genomic DNA. Translation: CAA67900.1.

3D structure databases

ProteinModelPortalP45631.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

Gene3D1.10.10.350. 1 hit.
1.10.1160.10. 1 hit.
3.40.50.620. 2 hits.
HAMAPMF_00022_B. Glu_tRNA_synth_B.
InterProIPR008925. 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]
PANTHERPTHR10119. PTHR10119. 1 hit.
PfamPF00749. tRNA-synt_1c. 1 hit.
[Graphical view]
PRINTSPR00987. TRNASYNTHGLU.
SUPFAMSSF48163. SSF48163. 1 hit.
TIGRFAMsTIGR00464. gltX_bact. 1 hit.
PROSITEPS00178. AA_TRNA_LIGASE_I. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameSYE_AZOBR
AccessionPrimary (citable) accession number: P45631
Secondary accession number(s): O07044
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: December 15, 1998
Last modified: February 19, 2014
This is version 81 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Aminoacyl-tRNA synthetases

List of aminoacyl-tRNA synthetase entries