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Q2W7Y6 (SYE1_MAGSA) 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 1

EC=6.1.1.17
Alternative name(s):
Glutamyl-tRNA synthetase 1
Short name=GluRS 1
Gene names
Name:gltX1
Ordered Locus Names:amb1235
OrganismMagnetospirillum magneticum (strain AMB-1 / ATCC 700264) [Complete proteome] [HAMAP]
Taxonomic identifier342108 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRhodospirillalesRhodospirillaceaeMagnetospirillum

Protein attributes

Sequence length444 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 – 444444Glutamate--tRNA ligase 1 HAMAP-Rule MF_00022
PRO_0000237368

Regions

Motif10 – 2011"HIGH" region HAMAP-Rule MF_00022
Motif241 – 2455"KMSKS" region HAMAP-Rule MF_00022

Sites

Binding site2441ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
Q2W7Y6 [UniParc].

Last modified January 10, 2006. Version 1.
Checksum: 9A252B67868D01F6

FASTA44449,181
        10         20         30         40         50         60 
MTSPVVRFAP SPTGLLHVGN ARVALLNRLF AKAHGGSFIL RLDDTDLERS RPEFAEAILD 

        70         80         90        100        110        120 
DLRWLGLDWD RLERQSARLD AYAAAAERLK VSGRVYACYE TPDELELRRK VQLGRGLPPV 

       130        140        150        160        170        180 
YDRAALKLAP DEIARLEAEG RRPHWRFKLE LEDVRWDDCV RGPSHYHGGN LSDPVLIRGD 

       190        200        210        220        230        240 
GSFLYTLPSV VDDIEFGVTH IIRGEDHVTN TAPQIQLFQA LGAVPPAFAH LPLLTGATGE 

       250        260        270        280        290        300 
GLSKRLGSGS LKDLRATGIH PMALNSLLAK LGSSDAIDIR HTLAELEAEF AWDKFGRGTP 

       310        320        330        340        350        360 
KFDSAELERL DARLMHTASF AEVRDRLGID GADEEFWLAV RPNLNHLAEA EAWWAICRQD 

       370        380        390        400        410        420 
LTPVIEDGEF TRAAAALLPD GAWDHATWGA WTETVKQATG RKGKALFHPL RLALTGRENG 

       430        440 
PELKTLLPLI GHDRARARLM GEIA 

« Hide

References

[1]"Complete genome sequence of the facultative anaerobic magnetotactic bacterium Magnetospirillum sp. strain AMB-1."
Matsunaga T., Okamura Y., Fukuda Y., Wahyudi A.T., Murase Y., Takeyama H.
DNA Res. 12:157-166(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: AMB-1 / ATCC 700264.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AP007255 Genomic DNA. Translation: BAE50039.1.
RefSeqYP_420598.1. NC_007626.1.

3D structure databases

ProteinModelPortalQ2W7Y6.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING342108.amb1235.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaBAE50039; BAE50039; amb1235.
GeneID3803454.
KEGGmag:amb1235.
PATRIC22436731. VBIMagMag129836_1221.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0008.
HOGENOMHOG000252721.
KOK01885.
OMARIALFNW.
OrthoDBEOG6DRPF7.

Enzyme and pathway databases

BioCycMMAG342108:GJNU-1251-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 nameSYE1_MAGSA
AccessionPrimary (citable) accession number: Q2W7Y6
Entry history
Integrated into UniProtKB/Swiss-Prot: May 30, 2006
Last sequence update: January 10, 2006
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