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B2IKL1 (SYE1_BEII9) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 36. 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:Bind_1410
OrganismBeijerinckia indica subsp. indica (strain ATCC 9039 / DSM 1715 / NCIB 8712) [Complete proteome] [HAMAP]
Taxonomic identifier395963 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRhizobialesBeijerinckiaceaeBeijerinckia

Protein attributes

Sequence length473 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 – 473473Glutamate--tRNA ligase 1 HAMAP-Rule MF_00022
PRO_0000367614

Regions

Motif11 – 2111"HIGH" region HAMAP-Rule MF_00022
Motif240 – 2445"KMSKS" region HAMAP-Rule MF_00022

Sites

Binding site2431ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
B2IKL1 [UniParc].

Last modified June 10, 2008. Version 1.
Checksum: 6EF7B7FC083A1B62

FASTA47352,471
        10         20         30         40         50         60 
MPDEVVTRFA PSPTGFLHIG GARTALFNWL FARHAGGRML LRIEDTDRER STDAAIAAIL 

        70         80         90        100        110        120 
DGLSWLGLHW DGDVIYQFQR VARHRDVALS LLEAGQAYYC YATPQELEEM REQARKEGRP 

       130        140        150        160        170        180 
PRYDGRWRDR AENDAPSGVK PVIRLKAPRD GETTLDDKVQ GKVTWANKDL DDLVLLRSDG 

       190        200        210        220        230        240 
TPTYMLAVVV DDHDMGVTQI IRGDDHLTNA ARQMQIYQAL GWSVPIMAHI PLIHGADGAK 

       250        260        270        280        290        300 
LSKRHGALGV DAYRGMGYLP EALRNYLVRL GWSQGDKEFF STEEMIEAFD LAHVGRSPAR 

       310        320        330        340        350        360 
FDFAKLENMN GHYLRHADDR HLVDMLSTTL PFLPKGLELA PKFTDERKAQ LLAAMPGLKE 

       370        380        390        400        410        420 
RAKTLVELLD GANFLFAERP LELDAKAQAL LDASSRAHIA ALVPLFEAAP EWKASALEAI 

       430        440        450        460        470 
VRAYVAETGV KLGQVAQPLR AALTGRATSP GIFDVLEVLG RDEGLARLRD QAG 

« Hide

References

[1]"Complete sequence of chromosome of Beijerinckia indica subsp. indica ATCC 9039."
US DOE Joint Genome Institute
Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E., Tice H., Bruce D., Goodwin L., Pitluck S., LaButti K., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Dunfield P.F., Dedysh S.N. expand/collapse author list , Liesack W., Saw J.H., Alam M., Chen Y., Murrell J.C., Richardson P.
Submitted (MAR-2008) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 9039 / DSM 1715 / NCIB 8712.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP001016 Genomic DNA. Translation: ACB95050.1.
RefSeqYP_001832539.1. NC_010581.1.

3D structure databases

ProteinModelPortalB2IKL1.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING395963.Bind_1410.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACB95050; ACB95050; Bind_1410.
GeneID6201052.
KEGGbid:Bind_1410.
PATRIC21085635. VBIBeiInd21058_1758.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0008.
HOGENOMHOG000252722.
KOK01885.
OMARANQGKF.
OrthoDBEOG6DRPF7.
ProtClustDBPRK01406.

Enzyme and pathway databases

BioCycBIND395963:GJA7-1430-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_BEII9
AccessionPrimary (citable) accession number: B2IKL1
Entry history
Integrated into UniProtKB/Swiss-Prot: March 24, 2009
Last sequence update: June 10, 2008
Last modified: February 19, 2014
This is version 36 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