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Q60BG7 (SYE1_METCA) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 67. 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
Synonyms:gltX-1
Ordered Locus Names:MCA0510
OrganismMethylococcus capsulatus (strain ATCC 33009 / NCIMB 11132 / Bath) [Complete proteome] [HAMAP]
Taxonomic identifier243233 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaMethylococcalesMethylococcaceaeMethylococcus

Protein attributes

Sequence length466 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 – 466466Glutamate--tRNA ligase 1 HAMAP-Rule MF_00022
PRO_0000119597

Regions

Motif10 – 2011"HIGH" region HAMAP-Rule MF_00022
Motif247 – 2515"KMSKS" region HAMAP-Rule MF_00022

Sites

Metal binding1031Zinc By similarity
Metal binding1051Zinc By similarity
Metal binding1301Zinc By similarity
Metal binding1321Zinc By similarity
Binding site2501ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
Q60BG7 [UniParc].

Last modified November 23, 2004. Version 1.
Checksum: ABF0C016F522C4D1

FASTA46652,121
        10         20         30         40         50         60 
MSAIKTRFAP SPTGLIHLGN ARTALFSALG GDVFVLRIED TDLERSRAEF VAELMNDLRW 

        70         80         90        100        110        120 
LGLDWQEGPR GAEPDPDWYQ SRRGEIYATY YRLLEEKGLA YPCFCTPLEL EVSRKVQLGS 

       130        140        150        160        170        180 
GRPPRYSGRC AHLPADEVRR RHEEGLAATL RFRVPKDRVV EFEDEVRGPQ RFAGEDIGDF 

       190        200        210        220        230        240 
IIRRADGSPA FFFCNAIDDA LMGITRVLRG EDHLANTPRQ LMILAALDLP RPRYAHISLI 

       250        260        270        280        290        300 
VGDDGAPLSK RNGSRSIKQL REEGYFPEAV VNMLARLGHH YDSAELLGLP ALRAGFDIRR 

       310        320        330        340        350        360 
LGRSPARFDV SHLDHWQGLA VRGAADDTLW HWLHTETRAV VPDAHRAGFL DLVRSNCLFP 

       370        380        390        400        410        420 
KEADAWARIL FTDELELAAD IAAVAQAAGE AFYLAAIDAA TESPDDFAAF LAGLKRRSGA 

       430        440        450        460 
KGKHLFLPLR AALTGSLDGP ELAKIYQMLD KPRLHRRLAE FTYESE 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE017282 Genomic DNA. Translation: AAU93301.1.
RefSeqYP_113029.1. NC_002977.6.

3D structure databases

ProteinModelPortalQ60BG7.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING243233.MCA0510.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAU93301; AAU93301; MCA0510.
GeneID3103869.
KEGGmca:MCA0510.
PATRIC22604770. VBIMetCap22254_0521.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0008.
HOGENOMHOG000252721.
KOK01885.
OMAAFFFCNA.
OrthoDBEOG6DRPF7.

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_METCA
AccessionPrimary (citable) accession number: Q60BG7
Entry history
Integrated into UniProtKB/Swiss-Prot: June 7, 2005
Last sequence update: November 23, 2004
Last modified: May 14, 2014
This is version 67 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