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A4XA62 (SYE_SALTO) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 60. 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:Strop_3375
OrganismSalinispora tropica (strain ATCC BAA-916 / DSM 44818 / CNB-440) [Complete proteome] [HAMAP]
Taxonomic identifier369723 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesMicromonosporineaeMicromonosporaceaeSalinispora

Protein attributes

Sequence length465 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 – 465465Glutamate--tRNA ligase HAMAP-Rule MF_00022
PRO_0000367766

Regions

Motif5 – 1511"HIGH" region HAMAP-Rule MF_00022
Motif228 – 2325"KMSKS" region HAMAP-Rule MF_00022

Sites

Metal binding961Zinc By similarity
Metal binding981Zinc By similarity
Metal binding1181Zinc By similarity
Metal binding1201Zinc By similarity
Binding site2311ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
A4XA62 [UniParc].

Last modified May 29, 2007. Version 1.
Checksum: B848B49A1B6D6F44

FASTA46551,263
        10         20         30         40         50         60 
MRFAPSPTGM FHVGGARSAL QNWIFAKQQG GVFVLRVEDT DAARNKPEWT EGILAALEWI 

        70         80         90        100        110        120 
GIARGSYEGP YFQSSYATEH RAAASRLHEG GRAYYCDCTR EVVQARTGSP HTGYDGFCRD 

       130        140        150        160        170        180 
RNLGPGAGRA LRFRTPDEGA TVVVDLIRGE PTFDNRLIED FVIARSDGSP VFLLANVVDD 

       190        200        210        220        230        240 
MTMGITHVIR AEEHLPNTPK QQLLWDALGV KPPVWAHVPV VVNEKRQKLS KRRDKVALEA 

       250        260        270        280        290        300 
YRDEGYLADA MCNYLMLLGW APSGDREIVP WPVIEEEFRL EEVNPSSAFF DEKKLRAFNG 

       310        320        330        340        350        360 
EYIRALPIAE FIAGCQPWLT GTATIAPPPW QPDEFDAEAF AAVAPLAQTR IAVLSEIVPN 

       370        380        390        400        410        420 
VDFLFLDSPL IDEGAWAKAM KEGAGDLLDA VIAAFTALPS WDADSTKSTL EAVGAEHGLK 

       430        440        450        460 
LGKAQAPVRV AVTGRRVGLP LFESLEVLGR ERTLTRLRAA RLRLP 

« Hide

References

[1]"Complete sequence of Salinispora tropica CNB-440."
Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E., Tice H., Pitluck S., Sun H., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Kim E., Jensen P.R., Moore B.S., Udwary D.W., Richardson P.
Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC BAA-916 / DSM 44818 / CNB-440.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000667 Genomic DNA. Translation: ABP55808.1.
RefSeqYP_001160186.1. NC_009380.1.

3D structure databases

ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING369723.Strop_3375.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABP55808; ABP55808; Strop_3375.
GeneID5059842.
KEGGstp:Strop_3375.
PATRIC23445882. VBISalTro43511_3480.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0008.
HOGENOMHOG000252722.
KOK01885.
OMAKRDANIM.
OrthoDBEOG6DRPF7.

Enzyme and pathway databases

BioCycSTRO369723:GI49-3413-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_SALTO
AccessionPrimary (citable) accession number: A4XA62
Entry history
Integrated into UniProtKB/Swiss-Prot: March 24, 2009
Last sequence update: May 29, 2007
Last modified: May 14, 2014
This is version 60 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