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A0ZZS4 (SYE_BIFAA) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 58. 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:BAD_0176
OrganismBifidobacterium adolescentis (strain ATCC 15703 / DSM 20083 / NCTC 11814 / E194a) [Complete proteome] [HAMAP]
Taxonomic identifier367928 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeBifidobacterialesBifidobacteriaceaeBifidobacterium

Protein attributes

Sequence length506 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 – 506506Glutamate--tRNA ligase HAMAP-Rule MF_00022
PRO_0000367616

Regions

Motif21 – 3111"HIGH" region HAMAP-Rule MF_00022
Motif265 – 2695"KMSKS" region HAMAP-Rule MF_00022

Sites

Binding site2681ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
A0ZZS4 [UniParc].

Last modified January 23, 2007. Version 1.
Checksum: BB9A2A5B98F23C25

FASTA50656,634
        10         20         30         40         50         60 
MTEVENTRPE LPENVRVRFC PSPTGIPHVG MVRTALFNWA EARHTKGTFV FRIEDTDAQR 

        70         80         90        100        110        120 
DSEESYNQII EALNWLGIDW DEGINVGGPD GPYRQSERGD IYKDVAAKLL EAGYAYESFS 

       130        140        150        160        170        180 
TPEEIEARNV AAGRPKAFGY DGYDRNLTEE QKAAFRAEGR KPALRIRMPD EDVAFDDLIR 

       190        200        210        220        230        240 
GRIEFKAGSV PDYVIVRPNG DPLYTLTNPV DDAMMRINVV LRGEDLLSST PRQIVLYRYL 

       250        260        270        280        290        300 
IELGVAKEMP LFGHMPYVMG QGNKKLSKRD PESNLFLHRD NGFIREGLLN YLALLGWSIA 

       310        320        330        340        350        360 
PDRDVFSMDE MIEKFDVRDV KANPARFDVD KAISINAEHI RMLEPQDFLN RSVPYLHRDG 

       370        380        390        400        410        420 
VVSADSWDAL TDREREVLTA AAPLVQPRVR LLGEVAGMVG SLLSTEGYIE PDADAKKQLK 

       430        440        450        460        470        480 
DSAPAVLDAA IAALDAVAEG DWKTDSLHET LNKALVEDGG YKPRLAFGPV RVAMSGRRVS 

       490        500 
PPLFESMEIV GKDVAMARLK GLREHL 

« Hide

References

[1]"Bifidobacterium adolescentis complete genome sequence."
Suzuki T., Tsuda Y., Kanou N., Inoue T., Kumazaki K., Nagano S., Hirai S., Tanaka K., Watanabe K.
Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 15703 / DSM 20083 / NCTC 11814 / E194a.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AP009256 Genomic DNA. Translation: BAF38957.1.
RefSeqYP_909039.1. NC_008618.1.

3D structure databases

ProteinModelPortalA0ZZS4.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING367928.BAD_0176.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaBAF38957; BAF38957; BAD_0176.
GeneID4556159.
KEGGbad:BAD_0176.
PATRIC21099569. VBIBifAdo27973_0188.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0008.
HOGENOMHOG000252720.
KOK01885.
OMAPEGMLNY.
OrthoDBEOG6DRPF7.

Enzyme and pathway databases

BioCycBADO367928:GHPT-182-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.
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.
ProtoNetSearch...

Entry information

Entry nameSYE_BIFAA
AccessionPrimary (citable) accession number: A0ZZS4
Entry history
Integrated into UniProtKB/Swiss-Prot: March 24, 2009
Last sequence update: January 23, 2007
Last modified: May 14, 2014
This is version 58 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