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B4S404 (SYE_PROA2) 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:Paes_1783
OrganismProsthecochloris aestuarii (strain DSM 271 / SK 413) [Complete proteome] [HAMAP]
Taxonomic identifier290512 [NCBI]
Taxonomic lineageBacteriaChlorobiChlorobiaChlorobialesChlorobiaceaeProsthecochloris

Protein attributes

Sequence length503 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 – 503503Glutamate--tRNA ligase HAMAP MF_00022_B
PRO_0000367738

Regions

Motif15 – 2511"HIGH" region HAMAP MF_00022_B
Motif262 – 2665"KMSKS" region HAMAP MF_00022_B

Sites

Binding site2651ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
B4S404 [UniParc].

Last modified September 23, 2008. Version 1.
Checksum: 943B6E8CBFBB4614

FASTA50357,531
        10         20         30         40         50         60 
MQTTLGPRVR TRFAPSPTGY LHVGGLRTAL YNYLYAKKVG GDFIVRIEDT DQARKVEGAD 

        70         80         90        100        110        120 
QSLLKTLEES GIVADESILH GGNFGPYMQS ERLDTYAQYC RQLLDQNNAY YCFSTAEELD 

       130        140        150        160        170        180 
ENRKLQMKQG IQPKYNRKWL PETMGGNMPQ SEIQKKLDEG APYVIRMKVP DYISIMFEDI 

       190        200        210        220        230        240 
VRGPVEFDSA TVDDQVLMKS DGFPTYHFAS VIDDHLMEIT HIIRGEEWLS SMPKHLLLYE 

       250        260        270        280        290        300 
FFGWEAPRFA HLPLLLNPDR SKLSKRQGDV AVEDFIAKGY SPDAILNFVA LLGWNEGEGS 

       310        320        330        340        350        360 
EQEIYSLEEL VQKFSLERVG KAGAVFNIDK LDWIEKQYIK ARPVDQIIQA IKPLLQKELA 

       370        380        390        400        410        420 
EKSTDMDVAR ISSDEYLTQV IDLMRERVNF ENEFITFSNY FYFDPETYDE AAVAKRWQDD 

       430        440        450        460        470        480 
TNEVLAEFIT ELEESDDFSA DNIEAMLKAF VAPKGKKPAF LIHPLRILSS GVGFGPSLYH 

       490        500 
MLEVLGKQTV IRRLKKGIER VTV 

« Hide

References

[1]"Complete sequence of chromosome of Prosthecochloris aestuarii DSM 271."
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., Anderson I., Liu Z., Li T., Zhao F. expand/collapse author list , Overmann J., Bryant D.A., Richardson P.
Submitted (JUN-2008) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: DSM 271 / SK 413.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP001108 Genomic DNA. Translation: ACF46796.1.
RefSeqYP_002016443.1. NC_011059.1.

3D structure databases

ProteinModelPortalB4S404.
ModBaseSearch...

Protein-protein interaction databases

STRINGB4S404.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID6458845.
GenomeReviewsGene locus Paes_1783 in contig CP001108_GR.
KEGGpaa:Paes_1783.
PATRIC23043460. VBIProAes37017_1896.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHBG628189.
OMALMEITHI.
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_PROA2
AccessionPrimary (citable) accession number: B4S404
Entry history
Integrated into UniProtKB/Swiss-Prot: March 24, 2009
Last sequence update: September 23, 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