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A6LEA1 (SYE_PARD8) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 37. 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:BDI_2289
OrganismParabacteroides distasonis (strain ATCC 8503 / DSM 20701 / NCTC 11152) [Complete proteome] [HAMAP]
Taxonomic identifier435591 [NCBI]
Taxonomic lineageBacteriaBacteroidetesBacteroidiaBacteroidalesPorphyromonadaceaeParabacteroides

Protein attributes

Sequence length505 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 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 – 505505Glutamate--tRNA ligase HAMAP MF_00022_B
PRO_1000001928

Regions

Motif12 – 2211"HIGH" region HAMAP MF_00022_B
Motif260 – 2645"KMSKS" region HAMAP MF_00022_B

Sites

Binding site2631ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
A6LEA1 [UniParc].

Last modified July 24, 2007. Version 1.
Checksum: 064BE993584ADCDF

FASTA50557,731
        10         20         30         40         50         60 
MTQRKVRVRF APSPTGALHI GGVRTALYNY LFAKQNGGDM ILRIEDTDSQ RFVPGAEDYI 

        70         80         90        100        110        120 
IEALTWLGIK FDEGVSFGGN YGPYRQSERR EIYKKYVDQL LNDGHAYIAF DTPAELEEKR 

       130        140        150        160        170        180 
KEIANFQYDA STRSQMRNSL TLSQEEVQSL IESGHQYVVR AKIEPNEDIH VNDLIRGEVV 

       190        200        210        220        230        240 
INSSILDDKV LYKSADQLPT YHLANIVDDH LMEVTHVIRG EEWLPSAPLH VLLYRFFGWE 

       250        260        270        280        290        300 
DTMPSFAHLS LLLKPEGNGK LSKRDGDRLG FPVFPLEWHD PKTGDVSSGY RESGYFPEAV 

       310        320        330        340        350        360 
VNFLALLGWN PGNDQEVMSM DDLIRLFDLS RCSKSGAKFD YEKGRWFNHH YLLEKSNAEI 

       370        380        390        400        410        420 
ADLFLPIVES HGIQTTHAYV EKVVGMMKGR VNFVSELWDL CSFFFIAPTE YDEKTRKKRW 

       430        440        450        460        470        480 
KEDSAVQLGE FIEQLRAREP FDVEGTENEC KAWIESKGYH LGNIMNAARL ALVGEGKGPG 

       490        500 
IFDITEALGK EESIRRIQRA IEILK 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000140 Genomic DNA. Translation: ABR44015.1.
RefSeqYP_001303637.1. NC_009615.1.

3D structure databases

ProteinModelPortalA6LEA1.
ModBaseSearch...

Protein-protein interaction databases

STRINGA6LEA1.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID5307438.
GenomeReviewsGene locus BDI_2289 in contig CP000140_GR.
KEGGpdi:BDI_2289.
PATRIC22847788. VBIParDis29947_2270.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0008.
HOGENOMHBG628189.
OMAWENVRVR.
ProtClustDBPRK01406.

Enzyme and pathway databases

BioCycPDIS435591:BDI_2289-MONOMER.

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_PARD8
AccessionPrimary (citable) accession number: A6LEA1
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: July 24, 2007
Last modified: January 25, 2012
This is version 37 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