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A8LMK2 (SYE1_DINSH) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 47. 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 1

EC=6.1.1.17
Alternative name(s):
Glutamyl-tRNA synthetase 1
Short name=GluRS 1
Gene names
Name:gltX1
Ordered Locus Names:Dshi_1805
OrganismDinoroseobacter shibae (strain DSM 16493 / NCIMB 14021 / DFL 12) [Complete proteome] [HAMAP]
Taxonomic identifier398580 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRhodobacteralesRhodobacteraceaeDinoroseobacter

Protein attributes

Sequence length471 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 – 471471Glutamate--tRNA ligase 1 HAMAP-Rule MF_00022
PRO_0000330969

Regions

Motif15 – 2511"HIGH" region HAMAP-Rule MF_00022
Motif243 – 2475"KMSKS" region HAMAP-Rule MF_00022

Sites

Binding site2461ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
A8LMK2 [UniParc].

Last modified December 4, 2007. Version 1.
Checksum: 4543B982AC18652E

FASTA47150,893
        10         20         30         40         50         60 
MSPTDASPVV TRFAPSPTGY LHIGGARTAL FNWLYARGRG GKFLLRIEDT DKARSTAEAT 

        70         80         90        100        110        120 
EAIFAGLRWL GLDWDGDAVS QAEGAARHAQ VARALQEAGK AYKCFTTQDE IAAFREAARA 

       130        140        150        160        170        180 
EGRSTLFRSP WRDADPASHP DAPYVIRIKA PQEGTTVIAD QVQGDVRIRN DQLDDMILLR 

       190        200        210        220        230        240 
SDGSPVYMLA VVVDDHDMGV THVIRGDDHL NNAARQMMIY DAMGWDMPVF AHIPLIHGPD 

       250        260        270        280        290        300 
GKKLSKRHGA LGVEEYQAMG YPAQAMRNYL ARLGWSHGDD EFFGDAQAQA WFDLDGIGKS 

       310        320        330        340        350        360 
PARLDLKKLD NLSGQHLGVM ADEAIVAGAQ GYLAATGAPP LTEAQETGLS RAMYCLKDRA 

       370        380        390        400        410        420 
KKFPDLLEKA HFILASRPID PDPKAAKSLD TVSRGILAEL TPQLQNASWT RDTLEGVVGG 

       430        440        450        460        470 
LAEAHGLGLG KLAAPLRAAL AGRSATPSVF DMMLVLGRDE TLARLSDATS A 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000830 Genomic DNA. Translation: ABV93547.1.
RefSeqYP_001533148.1. NC_009952.1.

3D structure databases

ProteinModelPortalA8LMK2.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING398580.Dshi_1805.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABV93547; ABV93547; Dshi_1805.
GeneID5712793.
KEGGdsh:Dshi_1805.
PATRIC21816261. VBIDinShi9476_1876.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0008.
HOGENOMHOG000252722.
KOK01885.
OMAAFEGPYF.
OrthoDBEOG6DRPF7.

Enzyme and pathway databases

BioCycDSHI398580:GKEL-1832-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 nameSYE1_DINSH
AccessionPrimary (citable) accession number: A8LMK2
Entry history
Integrated into UniProtKB/Swiss-Prot: April 29, 2008
Last sequence update: December 4, 2007
Last modified: May 14, 2014
This is version 47 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