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A6Q5I8 (SYE2_NITSB) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 45. 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 2

EC=6.1.1.17
Alternative name(s):
Glutamyl-tRNA synthetase 2
Short name=GluRS 2
Gene names
Name:gltX2
Ordered Locus Names:NIS_1641
OrganismNitratiruptor sp. (strain SB155-2) [Complete proteome] [HAMAP]
Taxonomic identifier387092 [NCBI]
Taxonomic lineageBacteriaProteobacteriaEpsilonproteobacteriaNitratiruptor

Protein attributes

Sequence length462 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 – 462462Glutamate--tRNA ligase 2 HAMAP-Rule MF_00022
PRO_0000367720

Regions

Motif8 – 1811"HIGH" region HAMAP-Rule MF_00022
Motif236 – 2405"KMSKS" region HAMAP-Rule MF_00022

Sites

Binding site2391ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
A6Q5I8 [UniParc].

Last modified August 21, 2007. Version 1.
Checksum: 6F6D96388E8DCFCB

FASTA46252,783
        10         20         30         40         50         60 
MIVTRFAPSP TGYLHIGGLR TALFNWLWAR KNGGKFILRI EDTDLARNSE EATKAILEAF 

        70         80         90        100        110        120 
DWVGLDYDGD VAYQSKRFDI YKRYIQKLLD EGKAYYCYMS KEELDRLREE QMKRGERPRY 

       130        140        150        160        170        180 
DRRYRDFTGT PPQGVQPVVR IKAPLEGDIV FEDGIKGIVT IKAEELDDFI IARSDGTPTY 

       190        200        210        220        230        240 
NFVVAIDDAL MGVTDVIRGD DHLYNTPKQI IVYEALGLPI PRFYHVPMIL NEQGKKLSKR 

       250        260        270        280        290        300 
DGAMDVMEYK KMGYLPEALL NFLVRLGWSH GDQEIFSLQE MKELFDPKDI NKSASAYNLS 

       310        320        330        340        350        360 
KLQWLNAHYI KNTPNEKLVK LLEEFGLFLS DHDKKEILLD ALKERAKTLQ ELADMAKEIL 

       370        380        390        400        410        420 
EAPKNYDEKG VKKALKGEWK AILELFLQKL KASDAHLPSD FHAIIEAVVE EKEIGFGKIG 

       430        440        450        460 
QPLRLALLGK MAGPDLSDVM AIIGKEETIA RVEKLIKEKG NS 

« 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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: SB155-2.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AP009178 Genomic DNA. Translation: BAF70747.1.
RefSeqYP_001357104.1. NC_009662.1.

3D structure databases

ProteinModelPortalA6Q5I8.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING387092.NIS_1641.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaBAF70747; BAF70747; NIS_1641.
GeneID5360353.
KEGGnis:NIS_1641.
PATRIC22685442. VBINitSp82229_1718.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0008.
HOGENOMHOG000252722.
KOK01885.
OMACDCTREA.
OrthoDBEOG6DRPF7.
ProtClustDBPRK01406.

Enzyme and pathway databases

BioCycNSP387092:GHA5-1686-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 nameSYE2_NITSB
AccessionPrimary (citable) accession number: A6Q5I8
Entry history
Integrated into UniProtKB/Swiss-Prot: March 24, 2009
Last sequence update: August 21, 2007
Last modified: February 19, 2014
This is version 45 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