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Q0I858 (SYE_SYNS3) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 60. 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:sync_2163
OrganismSynechococcus sp. (strain CC9311) [Complete proteome] [HAMAP]
Taxonomic identifier64471 [NCBI]
Taxonomic lineageBacteriaCyanobacteriaOscillatoriophycideaeChroococcalesSynechococcus

Protein attributes

Sequence length476 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 – 476476Glutamate--tRNA ligase HAMAP-Rule MF_00022
PRO_1000001981

Regions

Motif9 – 1911"HIGH" region HAMAP-Rule MF_00022
Motif248 – 2525"KMSKS" region HAMAP-Rule MF_00022

Sites

Binding site2511ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
Q0I858 [UniParc].

Last modified October 3, 2006. Version 1.
Checksum: FF787141DF2902DD

FASTA47653,502
        10         20         30         40         50         60 
MTVRVRLAPS PTGTLHIGTA RTAVFNWLFA RHQNGKFLLR IEDTDKERSK PEFTENILDG 

        70         80         90        100        110        120 
LRWLGLDWDE EPVIQSERIE VHRQAISQLL AQGLAYRCYV SEQELDAMRE AQRASGQPPR 

       130        140        150        160        170        180 
YDNRHRHLTG DQEEAYRAEG REAVIRFRID DEATIAWTDM VRGPMQWRGA DLGGDMVIAR 

       190        200        210        220        230        240 
RAPATTVGDP LYNLVVVVDD AAMAISHVIR GEDHIANTAK QLLLYQALEL NCPTFAHTPL 

       250        260        270        280        290        300 
ILNPEGRKLS KRDGVTSIGD FQEMGYTAEA LANYMTLLGW SVPEGTEERF TLRQAAEVFS 

       310        320        330        340        350        360 
FDRVNKAGAK FDWDKLNWLN AQVLHGWSPA ELLAALEPRW QKQGWVVSDP LWANDLAVLL 

       370        380        390        400        410        420 
GPSLTLIEDG VTQARPFFEE PPLEEDGLKQ LEQEGARPAL QALLSALELN AWDGLDVERA 

       430        440        450        460        470 
QTLLKEAAAS AEVKKGVLMK SLRAALLGRL QGPDLITTWA LLARLGHDRQ RLRRCL 

« Hide

References

[1]"Genome sequence of Synechococcus CC9311: insights into adaptation to a coastal environment."
Palenik B., Ren Q., Dupont C.L., Myers G.S., Heidelberg J.F., Badger J.H., Madupu R., Nelson W.C., Brinkac L.M., Dodson R.J., Durkin A.S., Daugherty S.C., Sullivan S.A., Khouri H., Mohamoud Y., Halpin R., Paulsen I.T.
Proc. Natl. Acad. Sci. U.S.A. 103:13555-13559(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: CC9311.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000435 Genomic DNA. Translation: ABI47571.1.
RefSeqYP_731364.1. NC_008319.1.

3D structure databases

ProteinModelPortalQ0I858.
SMRQ0I858. Positions 2-476.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING64471.sync_2163.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABI47571; ABI47571; sync_2163.
GeneID4259796.
KEGGsyg:sync_2163.
PATRIC23795416. VBISynSp88089_2261.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0008.
HOGENOMHOG000252722.
KOK01885.
OMAVTGQTHG.
OrthoDBEOG6DRPF7.

Enzyme and pathway databases

BioCycSSP64471:GIVP-2163-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_SYNS3
AccessionPrimary (citable) accession number: Q0I858
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: October 3, 2006
Last modified: May 14, 2014
This is version 60 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