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A8LZ53 (SYE_SALAI) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 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

EC=6.1.1.17
Alternative name(s):
Glutamyl-tRNA synthetase
Short name=GluRS
Gene names
Name:gltX
Ordered Locus Names:Sare_3615
OrganismSalinispora arenicola (strain CNS-205) [Complete proteome] [HAMAP]
Taxonomic identifier391037 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesMicromonosporineaeMicromonosporaceaeSalinispora

Protein attributes

Sequence length469 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

Cofactor

Binds 1 zinc ion per subunit By similarity. 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
Metal-binding
Nucleotide-binding
Zinc
   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

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

tRNA binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 469469Glutamate--tRNA ligase HAMAP-Rule MF_00022
PRO_0000330996

Regions

Motif9 – 1911"HIGH" region HAMAP-Rule MF_00022
Motif232 – 2365"KMSKS" region HAMAP-Rule MF_00022

Sites

Metal binding1001Zinc By similarity
Metal binding1021Zinc By similarity
Metal binding1221Zinc By similarity
Metal binding1241Zinc By similarity
Binding site2351ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
A8LZ53 [UniParc].

Last modified December 4, 2007. Version 1.
Checksum: 516D6C73C536F3D7

FASTA46951,750
        10         20         30         40         50         60 
MTVRVRFAPS PTGMFHVGGA RSALQNWIFA KQRGGVFVLR VEDTDAARNK PEWTEGILSA 

        70         80         90        100        110        120 
LEWIGIARGS YEGPYFQSSY AAEHRTAASR LHEGGRAYYC DCTREAVQAR TGSPHSGYDG 

       130        140        150        160        170        180 
FCRDRDLGPG AGRALRFRTP DEGATVVVDL IRGEPTFENR LIEDFVIARS DGSPVFLLAN 

       190        200        210        220        230        240 
VVDDMTMGIT HVIRAEEHLP NTPKQQLLWE ALGVKPPVWA HVPVVVNEKR QKLSKRRDKV 

       250        260        270        280        290        300 
ALEAYRDEGY LADAMRNYLM LLGWAPSGDR EIVPWPVIEE EFRLEQVNPS SAFFDEKKLR 

       310        320        330        340        350        360 
AFNGEYIRAL PVAEFVAACQ PWLTGTATIA PPPWQPDEFD ADTFAAVAPL AQTRIAVLSE 

       370        380        390        400        410        420 
IVANVDFLFL DSPLIDEGAW AKAMKEGAGD LLDAAITAFT AIPSWDAEST KSALEAVGAE 

       430        440        450        460 
HGLKLGKAQA PVRVAVTGRR VGLPLFESLE VLGRERTLTR LRAARVRLP 

« Hide

References

[1]"Complete sequence of Salinispora arenicola CNS-205."
US DOE Joint Genome Institute
Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E., Tice H., Pitluck S., Foster B., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Ivanova N., Jensen P.R., Moore B.S., Penn K. expand/collapse author list , Jenkins C., Udwary D., Xiang L., Gontang E., Richardson P.
Submitted (OCT-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: CNS-205.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000850 Genomic DNA. Translation: ABV99413.1.
RefSeqYP_001538404.1. NC_009953.1.

3D structure databases

ProteinModelPortalA8LZ53.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING391037.Sare_3615.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABV99413; ABV99413; Sare_3615.
GeneID5706641.
KEGGsaq:Sare_3615.
PATRIC23435767. VBISalAre38676_3643.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0008.
HOGENOMHOG000252722.
KOK01885.
OMACDCTREA.
OrthoDBEOG6DRPF7.
ProtClustDBPRK01406.

Enzyme and pathway databases

BioCycSARE391037:GH66-3654-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 nameSYE_SALAI
AccessionPrimary (citable) accession number: A8LZ53
Entry history
Integrated into UniProtKB/Swiss-Prot: April 29, 2008
Last sequence update: December 4, 2007
Last modified: February 19, 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