Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

A4QDQ6 (SYE_CORGB) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 51. 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:cgR_1371
OrganismCorynebacterium glutamicum (strain R) [Complete proteome] [HAMAP]
Taxonomic identifier340322 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesCorynebacterineaeCorynebacteriaceaeCorynebacterium

Protein attributes

Sequence length496 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 – 496496Glutamate--tRNA ligase HAMAP-Rule MF_00022
PRO_1000001892

Regions

Motif13 – 2311"HIGH" region HAMAP-Rule MF_00022
Motif257 – 2615"KMSKS" region HAMAP-Rule MF_00022

Sites

Binding site2601ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
A4QDQ6 [UniParc].

Last modified May 15, 2007. Version 1.
Checksum: 32EA2A7B754E4FBB

FASTA49655,662
        10         20         30         40         50         60 
MACMTDVRVR FCPSPTGTPH VGLVRTALFN WAYARHTGGK LVFRIEDTDA ARDSEESYSA 

        70         80         90        100        110        120 
IIDSLRWLGM DWDEGVEKGG PHEPYRQSQR KDIYQDVLKQ LIDAGEVYPA YSTAEEVEER 

       130        140        150        160        170        180 
HKAAGRDPKL GYDNFDRDLT EEQVAAFEAE GRKPVWRLRM PEQDWKWTDL VRGEVEFKSF 

       190        200        210        220        230        240 
TQPDFVVARS NGEPLYTLVN PVDDALMEVT HVLRGEDLLP STPRQLALYE ALKRIGVAKV 

       250        260        270        280        290        300 
TPAFGHLPFV MGEGNKKLSK RDPQSSLFNH RDNGIIPEGM LNYLALLGWS LSADQDIFGV 

       310        320        330        340        350        360 
DELIANFDVA DVLGNPARFD QKKLEAINAD HIRLLEPKDF EARLRAYMTE YTEFPADYPA 

       370        380        390        400        410        420 
EKFAIAAELV QTRIKVLSEA WDLLKFLVTA DEDLVLNEKA AKKNLKETAV EPLNAGIAAL 

       430        440        450        460        470        480 
EAVEEWTTPN IEAALNKALI EDLGLKPRVA FGALRIGISG EAVSPPLFES MELLGKESTL 

       490 
VRLKATREQT PFVVAE 

« Hide

References

[1]"Comparative analysis of the Corynebacterium glutamicum group and complete genome sequence of strain R."
Yukawa H., Omumasaba C.A., Nonaka H., Kos P., Okai N., Suzuki N., Suda M., Tsuge Y., Watanabe J., Ikeda Y., Vertes A.A., Inui M.
Microbiology 153:1042-1058(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: R.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AP009044 Genomic DNA. Translation: BAF54353.1.
RefSeqYP_001138255.1. NC_009342.1.

3D structure databases

ProteinModelPortalA4QDQ6.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING340322.cgR_1371.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaBAF54353; BAF54353; cgR_1371.
GeneID4993573.
KEGGcgt:cgR_1371.
PATRIC21507294. VBICorGlu58097_1410.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0008.
HOGENOMHOG000252720.
KOK01885.
OMAPAHSYLW.
OrthoDBEOG6DRPF7.
ProtClustDBPRK01406.

Enzyme and pathway databases

BioCycCGLU340322:GJBE-1423-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.
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_CORGB
AccessionPrimary (citable) accession number: A4QDQ6
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: May 15, 2007
Last modified: February 19, 2014
This is version 51 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