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A0L669 (SYE_MAGSM) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 57. 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:Mmc1_0944
OrganismMagnetococcus sp. (strain MC-1) [Complete proteome] [HAMAP]
Taxonomic identifier156889 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaMagnetococcalesMagnetococcaceaeMagnetococcus

Protein attributes

Sequence length472 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 – 472472Glutamate--tRNA ligase HAMAP-Rule MF_00022
PRO_0000330978

Regions

Motif7 – 1711"HIGH" region HAMAP-Rule MF_00022
Motif234 – 2385"KMSKS" region HAMAP-Rule MF_00022

Sites

Metal binding961Zinc By similarity
Metal binding981Zinc By similarity
Metal binding1231Zinc By similarity
Metal binding1251Zinc By similarity
Binding site2371ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
A0L669 [UniParc].

Last modified December 12, 2006. Version 1.
Checksum: 9ECC7FE88D04D39E

FASTA47253,172
        10         20         30         40         50         60 
MRTRFAPSPT GFLHVGGART ALFCHLQARH VGGTTVLRIE DTDRERSNQA LVDAILDGLH 

        70         80         90        100        110        120 
WLGLDPDEGP LFQSDHTQRH TDMALKLLEE GKAYKCYCTK QELDDMRAAQ QARKEKPRYD 

       130        140        150        160        170        180 
GRCRHRSEPP SDQPYVIRFK TPLEGEVVWP DMVQGTIHIA NKELDDLILL RSDGSPTYNL 

       190        200        210        220        230        240 
AVVVDDHDME ITHVIRGEDH TSNTPRQIHL FQALGWDVPS YAHIPLLHGE DGSKLSKRHG 

       250        260        270        280        290        300 
AVSVLQFREE GFLASALNNY LVRMGWSHGE KEEFTMDEMV ALFDVNNVGR SAAIFNTSKL 

       310        320        330        340        350        360 
LWLNGVHIRQ SGPEQLRGEL MWHLQRLGVD NPNPNFIDQI IPGMQERVKT MLEMAQMAMF 

       370        380        390        400        410        420 
YFKAPTEYAE TAVAKHLHAD ILPAYAALLE KLHTVTADEW DNGGLERAFK VVMAETGAKM 

       430        440        450        460        470 
GKIGQPVRIA ISGSDIAPGI YDILQLVGRH ESLRRLEVLL SFFQQRVHGA NG 

« Hide

References

[1]"Complete sequence of Magnetococcus sp. MC-1."
US DOE Joint Genome Institute
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S., Kiss H., Goodwin L.A., Brettin T., Bruce D., Han C., Tapia R., Gilna P. expand/collapse author list , Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Richardson P.
Submitted (SEP-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: MC-1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000471 Genomic DNA. Translation: ABK43462.1.
RefSeqYP_864868.1. NC_008576.1.

3D structure databases

ProteinModelPortalA0L669.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING156889.Mmc1_0944.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABK43462; ABK43462; Mmc1_0944.
GeneID4482743.
KEGGmgm:Mmc1_0944.
PATRIC22428442. VBIMagSp23654_0980.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0008.
HOGENOMHOG000252722.
KOK01885.
OMARANQGKF.
OrthoDBEOG6DRPF7.

Enzyme and pathway databases

BioCycMSP156889:GH36-958-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_MAGSM
AccessionPrimary (citable) accession number: A0L669
Entry history
Integrated into UniProtKB/Swiss-Prot: April 29, 2008
Last sequence update: December 12, 2006
Last modified: February 19, 2014
This is version 57 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