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B3EFG9 (SYE_CHLL2) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 27. 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:Clim_0359
OrganismChlorobium limicola (strain DSM 245 / NBRC 103803) [Complete proteome] [HAMAP]
Taxonomic identifier290315 [NCBI]
Taxonomic lineageBacteriaChlorobiChlorobiaChlorobialesChlorobiaceaeChlorobium/Pelodictyon groupChlorobium

Protein attributes

Sequence length502 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 MF_00022_B

Catalytic activity

ATP + L-glutamate + tRNA(Glu) = AMP + diphosphate + L-glutamyl-tRNA(Glu). HAMAP MF_00022_B

Subunit structure

Monomer By similarity. HAMAP MF_00022_B

Subcellular location

Cytoplasm By similarity HAMAP MF_00022_B.

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: InterPro

   Cellular componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

glutamate-tRNA ligase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 502502Glutamate--tRNA ligase HAMAP MF_00022_B
PRO_1000090062

Regions

Motif12 – 2211"HIGH" region HAMAP MF_00022_B
Motif259 – 2635"KMSKS" region HAMAP MF_00022_B

Sites

Binding site2621ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
B3EFG9 [UniParc].

Last modified July 22, 2008. Version 1.
Checksum: 0A2305BCE4FF8D40

FASTA50257,778
        10         20         30         40         50         60 
MVAQRVRTRF APSPTGYLHV GGLRTALYNY LFAKKMKGDF IIRIEDTDQS RKVEDAQQNL 

        70         80         90        100        110        120 
IKTLEWAGIV ADESPVHGGS FGPYVQSERL HIYREYCDRL LEDKHAYYCF STSEELEENR 

       130        140        150        160        170        180 
QLQLKQGLQP KYNRKWLPEE MGGAMPSSNI RKKMAEGSPY VVRMKVPDYI SVWFEDMIRG 

       190        200        210        220        230        240 
PVEFDSSTID DQVLMKSDGF PTYHFASVID DHLMEFTHII RGEEWLPSMP KHLLLYEFFG 

       250        260        270        280        290        300 
WEPPKFAHLP LLLNPDRSKL SKRQGDVAVE DYIRKGYSCD AIVNFVAMLG WNEGEGTEQE 

       310        320        330        340        350        360 
VYALQELIDK FSLERVGKAG AVFNVEKLNW LEKQYIKHRP AADIINTIRP VLASELAKRE 

       370        380        390        400        410        420 
TLLSVDVITG DHYLEQVIEL MRERVGFEHE FVTFSSYFFF EPESYEEEAV KKRWIPETND 

       430        440        450        460        470        480 
LLREFTAELE VLEPFTAETI ESALKAFVAP KGLKAAVLIH PLRILASGVS FGPSLYHMLE 

       490        500 
VLGREAVLRR ITKGIEQISV AE 

« Hide

References

[1]"Complete sequence of Chlorobium limicola DSM 245."
US DOE Joint Genome Institute
Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H., Bruce D., Goodwin L., Pitluck S., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Ovchinnikova G., Zhao F., Li T., Liu Z. expand/collapse author list , Overmann J., Bryant D.A., Richardson P.
Submitted (MAY-2008) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: DSM 245 / NBRC 103803.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP001097 Genomic DNA. Translation: ACD89452.1.
RefSeqYP_001942431.1. NC_010803.1.

3D structure databases

ProteinModelPortalB3EFG9.
ModBaseSearch...

Protein-protein interaction databases

STRINGB3EFG9.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID6354353.
GenomeReviewsGene locus Clim_0359 in contig CP001097_GR.
KEGGcli:Clim_0359.
PATRIC21372671. VBIChlLim118737_0385.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHBG628189.
OMAMAHIPLI.
ProtClustDBPRK01406.

Family and domain databases

HAMAPMF_00022_B. Glu_tRNA_synth_B.
[Tree]
InterProIPR008925. aa-tRNA-synth_I_codon-bd.
IPR020751. aa-tRNA-synth_I_codon-bd_sub2.
IPR001412. aa-tRNA-synth_I_CS.
IPR004527. Glu-tRNA-synth_Ib_bac/mito.
IPR000924. Glu/Gln-tRNA-synth_Ib.
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]
Gene3DG3DSA:1.10.1160.10. Glu/Gln-tRNA-synth_Ic_a-bdl. 1 hit.
G3DSA:3.40.50.620. Rossmann-like_a/b/a_fold. 2 hits.
G3DSA:1.10.10.350. tRNA_synt_bd. 1 hit.
KOK01885.
PANTHERPTHR10119. Glu_tRNA-synt_1c. 1 hit.
PTHR10119:SF1. PTHR10119:SF1. 1 hit.
PfamPF00749. tRNA-synt_1c. 1 hit.
[Graphical view]
PRINTSPR00987. TRNASYNTHGLU.
SUPFAMSSF48163. tRNA-synt_bind. 1 hit.
TIGRFAMsTIGR00464. GltX_bact. 1 hit.
PROSITEPS00178. AA_TRNA_LIGASE_I. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameSYE_CHLL2
AccessionPrimary (citable) accession number: B3EFG9
Entry history
Integrated into UniProtKB/Swiss-Prot: March 24, 2009
Last sequence update: July 22, 2008
Last modified: January 25, 2012
This is version 27 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

Aminoacyl-tRNA synthetases

List of aminoacyl-tRNA synthetase entries

SIMILARITY comments

Index of protein domains and families