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P31970 (SYE_SYNP2) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 95. 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:SYNPCC7002_A1394
OrganismSynechococcus sp. (strain ATCC 27264 / PCC 7002 / PR-6) (Agmenellum quadruplicatum) [Complete proteome] [HAMAP]
Taxonomic identifier32049 [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

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 – 481481Glutamate--tRNA ligase HAMAP-Rule MF_00022
PRO_0000119675

Regions

Motif9 – 1911"HIGH" region HAMAP-Rule MF_00022
Motif249 – 2535"KMSKS" region HAMAP-Rule MF_00022

Sites

Binding site2521ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
P31970 [UniParc].

Last modified June 10, 2008. Version 4.
Checksum: 71E6FB7E30925E49

FASTA48154,135
        10         20         30         40         50         60 
MTVRVRIAPS PTGNLHIGTA RTAVFNWLFA HHHGGTFVLR VEDTDLERSK PEYTENIKTG 

        70         80         90        100        110        120 
LQWLGLHWDE GPFFQTQRLD QYKAAIQTLL DQGLAYRCYC TPAELEAMRE QQKANNQAPR 

       130        140        150        160        170        180 
YDNRHRNLTE AQRAEFEAQG RKPVIRFKID DAQQIVWQDL IRGTMTWKGS DLGGDMVIAR 

       190        200        210        220        230        240 
TPEGDESFGQ PLYNLAVVVD DIDMQISHVI RGEDHIANTA KQILLYEALG AAVPQFAHTP 

       250        260        270        280        290        300 
LILNQEGRKL SKRDGVTSID DFRQMGFLPQ AIANYMSLLG WTPTDSTQEI FTLEEAAKEF 

       310        320        330        340        350        360 
SLERVNKAGA KFDWDKLDWI NAQYLHQMPI PALTDLLIPY LQAAGYGDYL GDRPWLESLV 

       370        380        390        400        410        420 
ALVAPSLTRL ADVTQETRLL FGDSITLDEK ATAQLQTEGV KVILQEILQN IQASTNFTPD 

       430        440        450        460        470        480 
EAKALINQAT KAHGVKKGVV MKSMRAGLMG ELQGPDLMQS WVLLHQKGWD IERLNQAIAS 


I 

« Hide

References

« Hide 'large scale' references
[1]"Complete sequence of Synechococcus sp. PCC 7002."
Li T., Zhao J., Zhao C., Liu Z., Zhao F., Marquardt J., Nomura C.T., Persson S., Detter J.C., Richardson P.M., Lanz C., Schuster S.C., Wang J., Li S., Huang X., Cai T., Yu Z., Luo J., Zhao J., Bryant D.A.
Submitted (FEB-2008) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 27264 / PCC 7002 / PR-6.
[2]"Cloning and characterization of the psaE gene of the cyanobacterium Synechococcus sp. PCC 7002: characterization of a psaE mutant and overproduction of the protein in Escherichia coli."
Zhao J., Snyder W., Muhlenhoff U., Rhiel E., Bryant D.A.
Mol. Microbiol. 9:183-194(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-160.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000951 Genomic DNA. Translation: ACA99390.1.
M99379 Genomic DNA. Translation: AAA27356.1.
RefSeqYP_001734646.1. NC_010475.1.

3D structure databases

ProteinModelPortalP31970.
SMRP31970. Positions 2-478.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING32049.SYNPCC7002_A1394.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACA99390; ACA99390; SYNPCC7002_A1394.
GeneID6055293.
KEGGsyp:SYNPCC7002_A1394.
PATRIC23817378. VBISynSp37135_1638.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0008.
HOGENOMHOG000252722.
KOK01885.
OMADIDMQIS.
OrthoDBEOG6DRPF7.

Enzyme and pathway databases

BioCycSSP32049:GKF7-1395-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_SYNP2
AccessionPrimary (citable) accession number: P31970
Secondary accession number(s): B1XMA4
Entry history
Integrated into UniProtKB/Swiss-Prot: July 1, 1993
Last sequence update: June 10, 2008
Last modified: May 14, 2014
This is version 95 of the entry and version 4 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