Skip Header

Contribute Send feedback
Read comments (?) or add your own

Q5YRX6 (SYE_NOCFA) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 52. 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:NFA_42160
OrganismNocardia farcinica (strain IFM 10152) [Complete proteome] [HAMAP]
Taxonomic identifier247156 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesCorynebacterineaeNocardiaceaeNocardia

Protein attributes

Sequence length489 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_B

Catalytic activity

ATP + L-glutamate + tRNA(Glu) = AMP + diphosphate + L-glutamyl-tRNA(Glu). HAMAP MF_00022_B

Subunit structure

Monomer By similarity. HAMAP MF_00022_B

Subcellular location

Cytoplasm HAMAP MF_00022_B.

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: InterPro

   Cellular componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

glutamate-tRNA ligase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 489489Glutamate--tRNA ligase HAMAP MF_00022_B
PRO_0000119615

Regions

Motif10 – 2011"HIGH" region HAMAP MF_00022_B
Motif254 – 2585"KMSKS" region HAMAP MF_00022_B

Sites

Binding site2571ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
Q5YRX6 [UniParc].

Last modified November 23, 2004. Version 1.
Checksum: 1D9403992B960FBD

FASTA48954,251
        10         20         30         40         50         60 
MTEVRVRFCP SPTGTPHVGL IRTALFNWAY ARHTGGTFVF RIEDTDAARD SEESYHAILD 

        70         80         90        100        110        120 
ALRWLGLTWD EGPEVGGPYG PYRQSQRREL YLDVVRRLLE AGEAYESFST PEEVEARHRA 

       130        140        150        160        170        180 
AGRDPKLGYD NYDRDLTPEA IEAYRAAGRP AVVRLRMPDE DLTWTDLVRG ETTFKAGTVP 

       190        200        210        220        230        240 
DFALTRGNGD PLYTLVNPVD DASMKITHVL RGEDLLSSTP RQLALYAALR RIGVADFTPE 

       250        260        270        280        290        300 
FGHLPFVMGQ GNKKLSKRDP ESNLFAHRDR GFIPEGLLNY LALLGWSLAD DRDVFSMSEM 

       310        320        330        340        350        360 
VAAFDISKVN SNPARFDQKK ADALNAEHIR LLEPGDFAHR LRQFLTEHGH IGADVDEKVF 

       370        380        390        400        410        420 
AAAAELVQTR IVVLGDAWDL LRFLFAPADE FTVDEAAAAK NLGADAVPVL EAAIAALEPL 

       430        440        450        460        470        480 
PGWATPVIED ALKTALIDDL GLKPRKAFAP VRVAVTGSHI SPPLYESLEL LGRELTLARL 


RSGLEWARQ 

« Hide

References

[1]"The complete genomic sequence of Nocardia farcinica IFM 10152."
Ishikawa J., Yamashita A., Mikami Y., Hoshino Y., Kurita H., Hotta K., Shiba T., Hattori M.
Proc. Natl. Acad. Sci. U.S.A. 101:14925-14930(2004) [PubMed: 15466710] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: IFM 10152.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AP006618 Genomic DNA. Translation: BAD59065.1.
RefSeqYP_120429.1. NC_006361.1.

3D structure databases

ProteinModelPortalQ5YRX6.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID3109603.
GenomeReviewsGene locus NFA_42160 in contig AP006618_GR.
KEGGnfa:nfa42160.
NMPDRfig|247156.1.peg.4065.
PATRIC22737976. VBINocFar94200_4215.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHBG628189.
OMAMAHIPLI.
ProtClustDBPRK01406.

Enzyme and pathway databases

BioCycNFAR247156:NFA42160-MONOMER.

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.
IPR004527. Glu-tRNA-synth_Ib_bac/mito.
IPR000924. Glu/Gln-tRNA-synth_Ib.
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]
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. 2 hits.
G3DSA:1.10.10.350. tRNA_synt_bd. 1 hit.
KOK01885.
PANTHERPTHR10119. Glu_tRNA-synt_1c. 1 hit.
PTHR10119:SF1. PTHR10119:SF1. 1 hit.
PfamPF00749. tRNA-synt_1c. 1 hit.
[Graphical view]
PRINTSPR00987. TRNASYNTHGLU.
SUPFAMSSF48163. tRNA-synt_bind. 1 hit.
TIGRFAMsTIGR00464. GltX_bact. 1 hit.
PROSITEPS00178. AA_TRNA_LIGASE_I. False negative.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameSYE_NOCFA
AccessionPrimary (citable) accession number: Q5YRX6
Entry history
Integrated into UniProtKB/Swiss-Prot: June 7, 2005
Last sequence update: November 23, 2004
Last modified: January 25, 2012
This is version 52 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

Aminoacyl-tRNA synthetases

List of aminoacyl-tRNA synthetase entries

SIMILARITY comments

Index of protein domains and families