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Reviewed, UniProtKB/Swiss-Prot Q5FRG7 (SYE1_GLUOX)

Last modified February 9, 2010. Version 34. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Glutamyl-tRNA synthetase 1
    EC=6.1.1.17
Alternative name(s):
    Glutamate--tRNA ligase 1
      Short name=GluRS 1
Gene names
Name: gltX1
Ordered Locus Names: GOX1268
OrganismGluconobacter oxydans (Gluconobacter suboxydans) [Complete proteome] [HAMAP]
Taxonomic identifier442 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRhodospirillalesAcetobacteraceaeGluconobacter

Protein attributes

Sequence length472 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 MF_00022

Catalytic activity

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

Subunit structure

Monomer By similarity. HAMAP MF_00022

Subcellular location

Cytoplasm HAMAP 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
   Technical termComplete proteome
Gene Ontology (GO)
   Biological processglutamyl-tRNA aminoacylation

Inferred from electronic annotation. Source: HAMAP

   Cellular componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionATP binding

Inferred from electronic annotation. Source: HAMAP

glutamate-tRNA ligase activity

Inferred from electronic annotation. Source: HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 472472Glutamyl-tRNA synthetase 1 HAMAP MF_00022
PRO_0000119569

Regions

Motif9 – 1911"HIGH" region HAMAP MF_00022
Motif238 – 2425"KMSKS" region HAMAP MF_00022

Sites

Binding site2411ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
Q5FRG7-1 [UniParc].

Last modified March 1, 2005. Version 1.
Checksum: 60C7FF557365D4E0

FASTA47252,303
        10         20         30         40         50         60 
MTIRTRFAPS PTGLLHVGNA RAALFNFLFA RHHGGEFLLR IEDTDKERST QKAVDVIFDG 

        70         80         90        100        110        120 
LAWMGIEADA EPVFQSARQD RHTEVALELL AKGQAYKCFC TPEELTAMRE KAMAEKRPPR 

       130        140        150        160        170        180 
YDGTWRDRDP SEAPEGAPYV VRLKAPREGE TVIKDLVQGE VRVANAEMDD LILLRSDGTP 

       190        200        210        220        230        240 
TYLHAVVCDD HDMEITHVMR GDDHLTNTFR QAMIYRAMGW DLPHFAHLPL IHGPDGAKLS 

       250        260        270        280        290        300 
KRHGAQSVVD FREEGYLPEA LCNYLLRLGW GHGDAEVLSR EEQIKLFDLD GVGRSPSRMD 

       310        320        330        340        350        360 
YVKLAHLNGI WMRQADDERL TNDVMERLQG REGVVTDDKT RARILAMMPG LKERAKTLVE 

       370        380        390        400        410        420 
LADNAAFAGF TLPLTFTPKA EKLLGEDGRR VLEGVGKELA ALKDFTPEAI DATLRSYAEK 

       430        440        450        460        470 
HEIKLGSVAQ PLRAAMTGST TSPGIDLTLS ALGQDEVLAR IAAVLASGSA NA 

« Hide

References

[1]"Complete genome sequence of the acetic acid bacterium Gluconobacter oxydans."
Prust C., Hoffmeister M., Liesegang H., Wiezer A., Fricke W.F., Ehrenreich A., Gottschalk G., Deppenmeier U.
Nat. Biotechnol. 23:195-200(2005) [PubMed: 15665824] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 621H.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000009 Genomic DNA. Translation: AAW61029.1.
RefSeqYP_191685.1.

3D structure databases

SMRQ5FRG7. Positions 3-466.
ModBaseSearch...

Genome annotation databases

GeneID3250731.
GenomeReviewsGene locus GOX1268 in contig CP000009_GR.
KEGGgox:GOX1268.
NMPDRfig|290633.1.peg.1230.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHBG628189.
OMAMAHIPLI.

Enzyme and pathway databases

BioCycGOXY290633:GOX1268-MONOMER.
BRENDA6.1.1.17. 3050.

Family and domain databases

HAMAPMF_00022_B. Glu_tRNA_synth_B.
[Tree]
InterProIPR008925. aa-tRNA-synth_I_codon-bd.
IPR020751. aa-tRNA-synth_I_codon-bd_sub2.
IPR001412. aa-tRNA-synth_I_CS.
IPR004527. Glu-tRNA-synth_Ic_bac/mito.
IPR000924. Glu/Gln-tRNA-synth_Ic.
IPR020061. Glu/Gln-tRNA-synth_Ic_a-bdl.
IPR020058. Glu/Gln-tRNA-synth_Ic_cat-dom.
IPR020060. Glu/Gln-tRNA-synth_Ic_N.
IPR014729. Rossmann-like_a/b/a_fold.
[Graphical view]
Gene3DG3DSA:1.10.1160.10. Glu/Gln-tRNA-synth_Ic_a-bdl. 1 hit.
G3DSA:3.40.50.620. Rossmann-like_a/b/a_fold. 1 hit.
G3DSA:1.10.10.350. tRNA_synt_bd. 1 hit.
PANTHERPTHR10119. Glu_tRNA-synt_1c. 1 hit.
PfamPF00749. tRNA-synt_1c. 1 hit.
[Graphical view]
PRINTSPR00987. TRNASYNTHGLU.
TIGRFAMsTIGR00464. gltX_bact. 1 hit.
PROSITEPS00178. AA_TRNA_LIGASE_I. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameSYE1_GLUOX
AccessionPrimary (citable) accession number: Q5FRG7
Entry history
Integrated into UniProtKB/Swiss-Prot: June 7, 2005
Last sequence update: March 1, 2005
Last modified: February 9, 2010
This is version 34 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

Relevant documents

Aminoacyl-tRNA synthetases

List of aminoacyl-tRNA synthetase entries

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents