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Q8L1E5 (SYE_SYNE7) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 74. 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:Synpcc7942_2393
OrganismSynechococcus elongatus (strain PCC 7942) (Anacystis nidulans R2) [Complete proteome] [HAMAP]
Taxonomic identifier1140 [NCBI]
Taxonomic lineageBacteriaCyanobacteriaOscillatoriophycideaeChroococcalesSynechococcus

Protein attributes

Sequence length481 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

Cofactor

Binds 1 zinc ion per subunit By similarity. 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
Metal-binding
Nucleotide-binding
Zinc
   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

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

tRNA binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 481481Glutamate--tRNA ligase HAMAP-Rule MF_00022
PRO_0000119677

Regions

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

Sites

Metal binding981Zinc By similarity
Metal binding1001Zinc By similarity
Metal binding1251Zinc By similarity
Metal binding1271Zinc By similarity
Binding site2511ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
Q8L1E5 [UniParc].

Last modified October 1, 2002. Version 1.
Checksum: 82AC99209A06D033

FASTA48153,200
        10         20         30         40         50         60 
MSVRVRIAPS PTGNLHIGTA RTAVFNWLFA RRHQGQFILR IEDTDLERSR SEYTDNILTG 

        70         80         90        100        110        120 
LQWLGLNWDE GPFYQTQRLD LYKAAVQQLL DSGKAYRCYC TEAELEALRE SQRARNEAPR 

       130        140        150        160        170        180 
YDNRHRDLTP EQEAAFQAEG REAVIRFRID DDREIAWTDL VRDRVVWKGS DLGGDMVIAR 

       190        200        210        220        230        240 
RSPAGTIGQP LYNLAVVVDD IDMTISHVIR GEDHIANTAK QILLYEALGA AVPEFAHTPL 

       250        260        270        280        290        300 
ILNKEGRKLS KRDGVTSISD FQNLGYLPEA IANYMTLLGW SPVEGMDERF SLAEAATVFD 

       310        320        330        340        350        360 
FDRVNKAGAK FDWDKLNWLN SQVIKEKSAS ELVALLQPFW SKAGVDTAAY PAAWLEELAT 

       370        380        390        400        410        420 
LLGPSLVTLT DIVGQSQLFF SQGIELQEDA IAQLGQAGSK AVLQQILEAL PSEALTLEVA 

       430        440        450        460        470        480 
KGLIDQAVKA AGVKKGIGMR SLRAALMGSM QGPDLLTSWV LLHQAGQAQP RLQAAIAAAQ 


G 

« Hide

References

« Hide 'large scale' references
[1]"Expression of the glutamyl-tRNA synthetase gene from the cyanobacterium Synechococcus sp PCC 7942 depends on nitrogen availability and the global regulator NtcA."
Luque I., Contreras A., Zabulon G., Herrero A., Houmard J.
Mol. Microbiol. 46:1157-1167(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"Complete sequence of chromosome 1 of Synechococcus elongatus PCC 7942."
US DOE Joint Genome Institute
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T., Hammon N., Israni S., Pitluck S., Schmutz J., Larimer F., Land M., Kyrpides N., Lykidis A., Richardson P.
Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: PCC 7942.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AJ440366 Genomic DNA. Translation: CAD29422.1.
CP000100 Genomic DNA. Translation: ABB58423.1.
RefSeqYP_401410.1. NC_007604.1.

3D structure databases

ProteinModelPortalQ8L1E5.
SMRQ8L1E5. Positions 2-480.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING1140.Synpcc7942_2393.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABB58423; ABB58423; Synpcc7942_2393.
GeneID3774677.
KEGGsyf:Synpcc7942_2393.
PATRIC23790343. VBISynElo51371_2686.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0008.
HOGENOMHOG000252722.
KOK01885.
OrthoDBEOG6DRPF7.

Enzyme and pathway databases

BioCycSYNEL:SYNPCC7942_2393-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_SYNE7
AccessionPrimary (citable) accession number: Q8L1E5
Secondary accession number(s): Q31KJ6
Entry history
Integrated into UniProtKB/Swiss-Prot: August 22, 2003
Last sequence update: October 1, 2002
Last modified: May 14, 2014
This is version 74 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