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Q2JKY3 (SYE_SYNJB) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 56. 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:CYB_1680
OrganismSynechococcus sp. (strain JA-2-3B'a(2-13)) (Cyanobacteria bacterium Yellowstone B-Prime) [Complete proteome] [HAMAP]
Taxonomic identifier321332 [NCBI]
Taxonomic lineageBacteriaCyanobacteriaOscillatoriophycideaeChroococcalesSynechococcus

Protein attributes

Sequence length479 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 – 479479Glutamate--tRNA ligase HAMAP-Rule MF_00022
PRO_0000237411

Regions

Motif9 – 1911"HIGH" region HAMAP-Rule MF_00022
Motif243 – 2475"KMSKS" region HAMAP-Rule MF_00022

Sites

Binding site2461ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
Q2JKY3 [UniParc].

Last modified March 7, 2006. Version 1.
Checksum: 6291942B0C9A6D7B

FASTA47953,767
        10         20         30         40         50         60 
MSVCVRIAPS PTGNLHIGTA RTAVFNWLYA RRHGGRFILR IEDTDRDRSL PRYTRNILAG 

        70         80         90        100        110        120 
LAWLGLDWDE GPVYQSKRIE RYQAVVQQLL DRGLAYRCYV SEAELEEMRA AQKAAGKAPR 

       130        140        150        160        170        180 
YDNRHRFLTE AQRRAYEAEG RQPVIRFKIE EPLEVSWVDL IRGPITWNTQ DLGGDMVIAR 

       190        200        210        220        230        240 
ADGCPLYNLA VVVDDIDMGI THVIRGEDHI GNTPKQILLY RALGHEPPQF AHSPLILNPE 

       250        260        270        280        290        300 
GKKLSKRDGA TSVAEFQQLG FLPEALKNYL ALLSWSPPDG EELFSLEKAA ALFDFDRVNR 

       310        320        330        340        350        360 
AAARFDWDKL NWINSQYIKR LSPPELVERL TPFWQAAGFD LSEVPDPTWL EDVARLIADG 

       370        380        390        400        410        420 
IDRLAEAPPL SRFLFQEPLS YTLPALEQLR LPGVAEAMAA MATTLAAAEL PQVSADSLKP 

       430        440        450        460        470 
LVDQVAKGQN MKKGLLMKSL RAALTGDLQG PDLLESFALL QRRGWALGRL EAVQKLVPC 

« Hide

References

[1]"Population level functional diversity in a microbial community revealed by comparative genomic and metagenomic analyses."
Bhaya D., Grossman A.R., Steunou A.-S., Khuri N., Cohan F.M., Hamamura N., Melendrez M.C., Bateson M.M., Ward D.M., Heidelberg J.F.
ISME J. 1:703-713(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: JA-2-3B'a(2-13).

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000240 Genomic DNA. Translation: ABD02639.1.
RefSeqYP_477902.1. NC_007776.1.

3D structure databases

ProteinModelPortalQ2JKY3.
SMRQ2JKY3. Positions 2-474.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING321332.CYB_1680.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABD02639; ABD02639; CYB_1680.
GeneID3901895.
KEGGcyb:CYB_1680.
PATRIC23805688. VBISynSp29577_1686.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0008.
HOGENOMHOG000252722.
KOK01885.
OMALMLFGRD.
OrthoDBEOG6DRPF7.
ProtClustDBPRK01406.

Enzyme and pathway databases

BioCycSSP321332:GH1B-1680-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_SYNJB
AccessionPrimary (citable) accession number: Q2JKY3
Entry history
Integrated into UniProtKB/Swiss-Prot: May 30, 2006
Last sequence update: March 7, 2006
Last modified: February 19, 2014
This is version 56 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