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Q2LUT2 (SYE2_SYNAS) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 56. 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:SYNAS_19610
ORF Names:SYN_01399
OrganismSyntrophus aciditrophicus (strain SB) [Complete proteome] [HAMAP]
Taxonomic identifier56780 [NCBI]
Taxonomic lineageBacteriaProteobacteriaDeltaproteobacteriaSyntrophobacteralesSyntrophaceaeSyntrophus

Protein attributes

Sequence length486 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 – 486486Glutamate--tRNA ligase 2 HAMAP-Rule MF_00022
PRO_0000237414

Regions

Motif12 – 2211"HIGH" region HAMAP-Rule MF_00022
Motif252 – 2565"KMSKS" region HAMAP-Rule MF_00022

Sites

Binding site2551ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
Q2LUT2 [UniParc].

Last modified February 21, 2006. Version 1.
Checksum: 713BE8894F195C91

FASTA48655,617
        10         20         30         40         50         60 
MNSTKPRVRF APSPTGELHI GNARTAFFNW LYARHYGGKL ILRIEDTDRQ RSTRAFEARL 

        70         80         90        100        110        120 
IDDLKWLSLD WDEGPDGKGE VGPYRQSERL DLYESFLKNL QKDGRVYPCY CTEDELELER 

       130        140        150        160        170        180 
TSLLSRKMAP RYMGKCRNLT EADRRRLEAQ GRRPTWRFRV SQGPVLFQDL IRGTMKFQGE 

       190        200        210        220        230        240 
AVGDFIIVRS NGTPAYNFAV VIDDHFMEIS TVIRGEDHLS NTAIQLMLYE ALGFEPPEFA 

       250        260        270        280        290        300 
HHSLILGKDR TKLSKRHGSV SVREFREKGI LPEALLNYLA LLGSSIGEGR EVCSLEEIIT 

       310        320        330        340        350        360 
AFSLDRAGKS GAVFDEDKLL WMNSLYIHEE PAIKLIERLR PFIEKAGYDV NKWETPWLDR 

       370        380        390        400        410        420 
MVEAVKPNLT TLADIGSYVK MIVEEPVRID EDAAAVLRET ETQMVLRTLL QLIEEGKFSH 

       430        440        450        460        470        480 
EDFYSQVMTA LRKVTGARGK RLFMPVRAAL TGTTRGPELD KIFVLLGEQS VKERLKKALN 


MQGNFS 

« Hide

References

[1]"The genome of the syntrophic bacterium Syntrophus aciditrophicus: Life dependent on negative change in electrical potential."
Gunsalus R., Rohlin L., Kim U., Krupp R., Bhattacharyya A., Campbell J., Mclerney M., Moutakki H., Rio-Hernandez L.
Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: SB.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000252 Genomic DNA. Translation: ABC77840.1.
RefSeqYP_462008.1. NC_007759.1.

3D structure databases

ProteinModelPortalQ2LUT2.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING56780.SYN_01399.

Proteomic databases

PRIDEQ2LUT2.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABC77840; ABC77840; SYN_01399.
GeneID3882794.
KEGGsat:SYN_01399.
PATRIC23864670. VBISynAci70500_2120.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0008.
HOGENOMHOG000252721.
KOK09698.
OMAFFFANAV.
OrthoDBEOG6DRPF7.

Enzyme and pathway databases

BioCycSACI56780:GHXT-2007-MONOMER.

Family and domain databases

Gene3D1.10.10.350. 1 hit.
1.10.1160.10. 1 hit.
1.10.8.70. 1 hit.
3.40.50.620. 2 hits.
HAMAPMF_00022_B. Glu_tRNA_synth_B.
InterProIPR008925. aa-tRNA-synth_I_codon-bd.
IPR020752. aa-tRNA-synth_I_codon-bd_sub1.
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_SYNAS
AccessionPrimary (citable) accession number: Q2LUT2
Entry history
Integrated into UniProtKB/Swiss-Prot: May 30, 2006
Last sequence update: February 21, 2006
Last modified: February 19, 2014
This is version 56 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