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A8LCV4 (SYE_FRASN) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 47. 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:Franean1_1684
OrganismFrankia sp. (strain EAN1pec) [Complete proteome] [HAMAP]
Taxonomic identifier298653 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesFrankineaeFrankiaceaeFrankia

Protein attributes

Sequence length500 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

Cofactor

Binds 1 zinc ion per subunit By similarity. 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
Metal-binding
Nucleotide-binding
Zinc
   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

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

tRNA binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 500500Glutamate--tRNA ligase HAMAP-Rule MF_00022
PRO_0000367675

Regions

Motif12 – 2211"HIGH" region HAMAP-Rule MF_00022
Motif235 – 2395"KMSKS" region HAMAP-Rule MF_00022

Sites

Metal binding1031Zinc By similarity
Metal binding1051Zinc By similarity
Metal binding1251Zinc By similarity
Metal binding1271Zinc By similarity
Binding site2381ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
A8LCV4 [UniParc].

Last modified December 4, 2007. Version 1.
Checksum: F2A1947B86FCD570

FASTA50053,900
        10         20         30         40         50         60 
MSTGRVRVRF APSPTGIFHV GGARSALFNW LVAKGAGGDF VLRVEDTDAS RNRPEWTEGI 

        70         80         90        100        110        120 
ISALDWLGIS PGGYEGPVFQ SERAGRHAEA AAGLFAAGRA YYCGCTRDEL AARTGNAQHG 

       130        140        150        160        170        180 
YDGFCRERGL GPGPGRALRF RTPDEGTTVV LDVIRGTPEF PNDTIEDFVI ARADGSAVFL 

       190        200        210        220        230        240 
LANVVDDLDM GITHVVRGEE HLSNTPKQQL LWAALGTPPP VWAHVPVIVN EKRQKLSKRR 

       250        260        270        280        290        300 
DKVALESYRA EGYLAAAMCN YLMLLGWAPP GDEEIVPFET IEASFRLEDV KPSPAFFDEK 

       310        320        330        340        350        360 
KLRAFNGEYI RALSVDEFVA ACEPWLVPAA DVPAAVDAPA AAGTGDGAAG VTTAVPAPPW 

       370        380        390        400        410        420 
SPERFSAEVF AAVAPLAQSR VAVLSEIVPM VDFLFLPEAP TDEAAWAKTM KGPALDLLTE 

       430        440        450        460        470        480 
AAEAYEKVAW DHDVLRETLI EVGERHGLKL GKAQAPVRVA VTGRTVGLPL FESLEILGRE 

       490        500 
ETLRRLRAAV ERLDTAANPA 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000820 Genomic DNA. Translation: ABW11122.1.
RefSeqYP_001506028.1. NC_009921.1.

3D structure databases

ProteinModelPortalA8LCV4.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING298653.Franean1_1684.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABW11122; ABW11122; Franean1_1684.
GeneID5670086.
KEGGfre:Franean1_1684.
PATRIC21936234. VBIFraSp51419_1730.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0008.
HOGENOMHOG000252722.
KOK01885.
OMAHCLRASI.
OrthoDBEOG6DRPF7.

Enzyme and pathway databases

BioCycFSP298653:GHPI-1700-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_FRASN
AccessionPrimary (citable) accession number: A8LCV4
Entry history
Integrated into UniProtKB/Swiss-Prot: March 24, 2009
Last sequence update: December 4, 2007
Last modified: May 14, 2014
This is version 47 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