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B1VG41 (SYE_CORU7) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 44. 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:cu0770
OrganismCorynebacterium urealyticum (strain ATCC 43042 / DSM 7109) [Complete proteome] [HAMAP]
Taxonomic identifier504474 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesCorynebacterineaeCorynebacteriaceaeCorynebacterium

Protein attributes

Sequence length499 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 – 499499Glutamate--tRNA ligase HAMAP-Rule MF_00022
PRO_0000367654

Regions

Motif10 – 2011"HIGH" region HAMAP-Rule MF_00022
Motif255 – 2595"KMSKS" region HAMAP-Rule MF_00022

Sites

Binding site2581ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
B1VG41 [UniParc].

Last modified May 20, 2008. Version 1.
Checksum: CA251E47611E82ED

FASTA49956,518
        10         20         30         40         50         60 
MSEVRVRFCP SPTGTPHVGM VRTALFNWAY ARHTGGKLIF RIEDTDAQRD TEESYQAIID 

        70         80         90        100        110        120 
SLKWLGLDWD EGIETGGPHE PYRQSQRMDI YAEVLEKLKA AGEVYPAYST PEEVEERHKA 

       130        140        150        160        170        180 
AGRDPKLGYD NYDRDLTEEQ IAAFEAEGRK PVWRLKMDHD RRYTWTDLVR GEMDVDGKTM 

       190        200        210        220        230        240 
PDFVVARSNG QPLYTLVNPL DDALMGITHV LRGEDLLPST PRQIALYEAL IRIGVAKEVP 

       250        260        270        280        290        300 
TFAHLPFVTG EGNRKLSKRD PESNLFNHRD AGVIPEGMLN YLSLLGWSLS ADEDIFTMAQ 

       310        320        330        340        350        360 
LIENFDIADV KPNPARFDHK KMEAINADHI RMLDLADFTQ RLRTYLEEFK GWPADYPADK 

       370        380        390        400        410        420 
FAFAAELVQT RIKVLGDADG LLRFLLTKDE DLELEPKAAR KNLKEAAKEP LEAAIEELEA 

       430        440        450        460        470        480 
IAEEDFRTEP IEQALSTRLI EQMELKPRVA YGALRVAICG QAVSPPLFES MELLGKDSTL 

       490 
VRLRAGLEQT PFQAEQPAN 

« Hide

References

[1]"The lifestyle of Corynebacterium urealyticum derived from its complete genome sequence established by pyrosequencing."
Tauch A., Trost E., Tilker A., Ludewig U., Schneiker S., Goesmann A., Arnold W., Bekel T., Brinkrolf K., Brune I., Goetker S., Kalinowski J., Kamp P.-B., Lobo F.P., Viehoever P., Weisshaar B., Soriano F., Droege M., Puehler A.
J. Biotechnol. 136:11-21(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 43042 / DSM 7109.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AM942444 Genomic DNA. Translation: CAQ04730.1.
RefSeqYP_001800164.1. NC_010545.1.

3D structure databases

ProteinModelPortalB1VG41.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING504474.cur_0770.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAQ04730; CAQ04730; cu0770.
GeneID6185762.
KEGGcur:cur_0770.
PATRIC21521260. VBICorUre58120_0769.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0008.
KOK01885.
OMAPAHSYLW.
OrthoDBEOG6DRPF7.
ProtClustDBPRK01406.

Enzyme and pathway databases

BioCycCURE504474:GJ8Y-783-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_CORU7
AccessionPrimary (citable) accession number: B1VG41
Entry history
Integrated into UniProtKB/Swiss-Prot: March 24, 2009
Last sequence update: May 20, 2008
Last modified: February 19, 2014
This is version 44 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