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A4FMP6 (SYE_SACEN) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 54. 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:SACE_6148
OrganismSaccharopolyspora erythraea (strain NRRL 23338) [Complete proteome] [HAMAP]
Taxonomic identifier405948 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesPseudonocardineaePseudonocardiaceaeSaccharopolyspora

Protein attributes

Sequence length503 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 – 503503Glutamate--tRNA ligase HAMAP-Rule MF_00022
PRO_0000330995

Regions

Motif26 – 3611"HIGH" region HAMAP-Rule MF_00022
Motif270 – 2745"KMSKS" region HAMAP-Rule MF_00022

Sites

Binding site2731ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
A4FMP6 [UniParc].

Last modified April 17, 2007. Version 1.
Checksum: 7F0EDA63F55C26BF

FASTA50355,617
        10         20         30         40         50         60 
MSTPEATAEA VSGHEPNRAV RARFCPSPTG TPHVGLVRTA LYNWVFARHN QGKLVFRIED 

        70         80         90        100        110        120 
TDASRDSEES YQALLDALRW LGLDWDEGPE VGGEYGPYRQ SERRDIYADI ARRLLEAGEL 

       130        140        150        160        170        180 
YESFSTPEEV EARHRAAGRD PKLGYDNADR DLTDEQKAAF RAEGRNAVLR LRMPEHDITF 

       190        200        210        220        230        240 
ADLVRGEITF PAGSVPDPVL VRGNGDALYT LTNPVDDALM RITHVLRGED LLSSTPRQIA 

       250        260        270        280        290        300 
LYDALRRIGV TDFTPEFGHL PFVMGEGNKK LSKRDPQSNL FHHRDRGFLP EGLLNYLALL 

       310        320        330        340        350        360 
GWSISEDRDV FTLDEMVEAF EIGRVSSNPA RFDQKKADAI NSAHLRALAP DDFLERVVPY 

       370        380        390        400        410        420 
LVSGGVLPAE PTEEQLATVR AAAPLVQERL IVLSDAVGMM RFLFDGDDFA PDPASAEKAL 

       430        440        450        460        470        480 
GEDARPVLEA AVSALEALPE WTTEAIEAAL KESVVDGLGI KPRKAFAPVR VAVTGRTVSP 

       490        500 
PLYESMELLG REVSLRRLRA PLG 

« Hide

References

[1]"Complete genome sequence of the erythromycin-producing bacterium Saccharopolyspora erythraea NRRL23338."
Oliynyk M., Samborskyy M., Lester J.B., Mironenko T., Scott N., Dickens S., Haydock S.F., Leadlay P.F.
Nat. Biotechnol. 25:447-453(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: NRRL 23338.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AM420293 Genomic DNA. Translation: CAM05321.1.
RefSeqYP_001108246.1. NC_009142.1.

3D structure databases

ProteinModelPortalA4FMP6.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING405948.SACE_6148.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAM05321; CAM05321; SACE_6148.
GeneID4945880.
KEGGsen:SACE_6148.
PATRIC23419672. VBISacEry28377_6123.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0008.
HOGENOMHOG000252720.
KOK01885.
OMAAFRCFCT.
OrthoDBEOG6DRPF7.
ProtClustDBPRK01406.

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.
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.
ProtoNetSearch...

Entry information

Entry nameSYE_SACEN
AccessionPrimary (citable) accession number: A4FMP6
Entry history
Integrated into UniProtKB/Swiss-Prot: April 29, 2008
Last sequence update: April 17, 2007
Last modified: February 19, 2014
This is version 54 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