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Reviewed, UniProtKB/Swiss-Prot A6Q354 (SYE1_NITSB)

Last modified November 3, 2009. Version 17. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Glutamyl-tRNA synthetase 1
    EC=6.1.1.17
Alternative name(s):
    Glutamate--tRNA ligase 1
      Short name=GluRS 1
Gene names
Name: gltX1
Ordered Locus Names: NIS_0801
OrganismNitratiruptor sp. (strain SB155-2) [Complete proteome] [HAMAP]
Taxonomic identifier387092 [NCBI]
Taxonomic lineageBacteriaProteobacteriaEpsilonproteobacteriaNitratiruptor

Protein attributes

Sequence length431 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
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.

Catalytic activity

ATP + L-glutamate + tRNA(Glu) = AMP + diphosphate + L-glutamyl-tRNA(Glu). HAMAP MF_00022

Subunit structure

Monomer By similarity.

Subcellular location

Cytoplasm By similarity.

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: HAMAP

   Cellular componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionATP binding

Inferred from electronic annotation. Source: HAMAP

glutamate-tRNA ligase activity

Inferred from electronic annotation. Source: HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 431431Glutamyl-tRNA synthetase 1 HAMAP MF_00022
PRO_0000367719

Regions

Motif6 – 1611"HIGH" region HAMAP MF_00022
Motif235 – 2395"KMSKS" region HAMAP MF_00022

Sites

Binding site2381ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
A6Q354-1 [UniParc].

Last modified August 21, 2007. Version 1.
Checksum: F340C31FF23E6F72

FASTA43149,845
        10         20         30         40         50         60 
MIRFAPSPTG DMHIGNLRVA IFNYIEAKKR NERFLIRIED TDIERNIEGK DQEILQILDT 

        70         80         90        100        110        120 
FGLQYDDVVY QSKNFSFHQN FAYKLLNEGK AFACFCTPQE LEKEREQAKK EKRAYRYSGK 

       130        140        150        160        170        180 
CENITLDEAS QRGEPFVVRI KKPTGTIEFD DIIKGHLAFE PNEVDSFVIL RADARPTYNF 

       190        200        210        220        230        240 
ACAVDDMLYD ITLVIRGEDH VSNTPKQIHI RNLLGYDKKI EYAHLPIILN EEGKKMSKRD 

       250        260        270        280        290        300 
KASSVKWLLE EGFLPEAIAN YLILLGNKTP KEIFTLDEAI AWFDLKNISK APAKFDIEKL 

       310        320        330        340        350        360 
RFINRAHLQM MSEEELEKAL GVDEGLGALA KIYLEEASTL KELNTKIDLV LHGKRENETF 

       370        380        390        400        410        420 
REEIETLRNL LKSMELPESF DEFKKELMQK SGLKGKKFFK PLRILLTGSE HGPELSELYP 

       430 
AIKNRIKEVI Q 

« Hide

References

[1]"Deep-sea vent epsilon-proteobacterial genomes provide insights into emergence of pathogens."
Nakagawa S., Takaki Y., Shimamura S., Reysenbach A.-L., Takai K., Horikoshi K.
Proc. Natl. Acad. Sci. U.S.A. 104:12146-12150(2007) [PubMed: 17615243] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

AP009178 Genomic DNA. Translation: BAF69913.1.
RefSeqYP_001356270.1.

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

STRINGA6Q354.

Genome annotation databases

GeneID5360157.
GenomeReviewsGene locus NIS_0801 in contig AP009178_GR.
KEGGnis:NIS_0801.

Organism-specific databases

CMRSearch...

Phylogenomic databases

OMAAIFNYIC.

Family and domain databases

HAMAPMF_00022.
[Tree]
InterProIPR008925. aa-tRNA-synth_I_codon-bd.
IPR001412. aa-tRNA-synth_I_CS.
IPR004527. Glu-tRNA-synth_Ic_bac/mito.
IPR000924. Glu/Gln-tRNA-synth_Ic.
IPR020061. Glu/Gln-tRNA-synth_Ic_a-bdl.
IPR020058. Glu/Gln-tRNA-synth_Ic_cat-dom.
IPR020060. Glu/Gln-tRNA-synth_Ic_N.
IPR014729. Rossmann-like_a/b/a_fold.
[Graphical view]
Gene3DG3DSA:1.10.1160.10. Glu/Gln-tRNA-synth_Ic_a-bdl. 1 hit.
G3DSA:3.40.50.620. Rossmann-like_a/b/a_fold. 2 hits.
G3DSA:1.10.10.350. tRNA_synt_bd. 1 hit.
PANTHERPTHR10119. Glu_tRNA-synt_1c. 1 hit.
PfamPF00749. tRNA-synt_1c. 1 hit.
[Graphical view]
PRINTSPR00987. TRNASYNTHGLU.
TIGRFAMsTIGR00464. gltX_bact. 1 hit.
PROSITEPS00178. AA_TRNA_LIGASE_I. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameSYE1_NITSB
AccessionPrimary (citable) accession number: A6Q354
Entry history
Integrated into UniProtKB/Swiss-Prot: March 24, 2009
Last sequence update: August 21, 2007
Last modified: November 3, 2009
This is version 17 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

Relevant documents

Aminoacyl-tRNA synthetases

List of aminoacyl-tRNA synthetase entries

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents