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Q47GG0 (SYE_DECAR) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 59. 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
Ordered Locus Names:Daro_1321
OrganismDechloromonas aromatica (strain RCB) [Complete proteome] [HAMAP]
Taxonomic identifier159087 [NCBI]
Taxonomic lineageBacteriaProteobacteriaBetaproteobacteriaRhodocyclalesRhodocyclaceaeDechloromonas

Protein attributes

Sequence length464 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
   Technical termComplete proteome
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 – 464464Glutamate--tRNA ligase HAMAP-Rule MF_00022
PRO_0000237356

Regions

Motif10 – 2011"HIGH" region HAMAP-Rule MF_00022
Motif242 – 2465"KMSKS" region HAMAP-Rule MF_00022

Sites

Binding site2451ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
Q47GG0 [UniParc].

Last modified September 13, 2005. Version 1.
Checksum: 6CD879AB04626526

FASTA46451,555
        10         20         30         40         50         60 
MKPVRTRFAP SPTGYLHIGG ARTALFSWAY ARRHGGDFIL RIEDTDVARS TPEAVQAILD 

        70         80         90        100        110        120 
GMQWLGLEHD EGPFYQMQRM DRYKEVIQQM LANGSAYYCY TTREELDALR AEQEAKKEKP 

       130        140        150        160        170        180 
RYDGRWRPEA GKALPVPPTD VPPVIRFKNP QGGVVAWDDQ VKGRIEFANT ELDDLIIARA 

       190        200        210        220        230        240 
DGTPTYNFCV CVDDWDMGIT HVIRGDDHVN NTPRQINILK ALGAEVPTYA HLSMILGDDG 

       250        260        270        280        290        300 
AKLSKRHGAV SVMQYDEEGF LTEAVINYLA RLGWSHGDDE VFSRQQFVEW FDLDHITASA 

       310        320        330        340        350        360 
AQFNTEKLLW LNQHYMKQLP PAELAAKVQA RLTARGVDTA NGPDLEKAVV LYVDRSNTLN 

       370        380        390        400        410        420 
VLADAVEVFY AHVTPNPELL AQHLADDARP ALAEFAAGIA TVTWEAPAIN ALIKETVTKH 

       430        440        450        460 
GLKMPKLAMP LRVILTGQAQ TPAVDAVIAL IGRDKVAATL AAYL 

« Hide

References

[1]"Metabolic analysis of the soil microbe Dechloromonas aromatica str. RCB: indications of a surprisingly complex life-style and cryptic anaerobic pathways for aromatic degradation."
Salinero K.K., Keller K., Feil W.S., Feil H., Trong S., Di Bartolo G., Lapidus A.
BMC Genomics 10:351-351(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: RCB.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000089 Genomic DNA. Translation: AAZ46071.1.
RefSeqYP_284541.1. NC_007298.1.

3D structure databases

ProteinModelPortalQ47GG0.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING159087.Daro_1321.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAZ46071; AAZ46071; Daro_1321.
GeneID3569190.
KEGGdar:Daro_1321.
PATRIC21601296. VBIDecAro89105_1316.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0008.
HOGENOMHOG000252722.
KOK01885.
OMARANQGKF.
OrthoDBEOG6DRPF7.
ProtClustDBPRK01406.

Enzyme and pathway databases

BioCycDARO159087:GI5B-1371-MONOMER.

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_DECAR
AccessionPrimary (citable) accession number: Q47GG0
Entry history
Integrated into UniProtKB/Swiss-Prot: May 30, 2006
Last sequence update: September 13, 2005
Last modified: February 19, 2014
This is version 59 of the entry and version 1 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