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Q0AUF7 (SYE2_SYNWW) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 59. 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:Swol_2357
OrganismSyntrophomonas wolfei subsp. wolfei (strain DSM 2245B / Goettingen) [Complete proteome] [HAMAP]
Taxonomic identifier335541 [NCBI]
Taxonomic lineageBacteriaFirmicutesClostridiaClostridialesSyntrophomonadaceaeSyntrophomonas

Protein attributes

Sequence length490 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 – 490490Glutamate--tRNA ligase 2 HAMAP-Rule MF_00022
PRO_0000367780

Regions

Motif17 – 2711"HIGH" region HAMAP-Rule MF_00022
Motif258 – 2625"KMSKS" region HAMAP-Rule MF_00022

Sites

Binding site2611ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
Q0AUF7 [UniParc].

Last modified October 17, 2006. Version 1.
Checksum: 6D70426A4CDAB698

FASTA49055,693
        10         20         30         40         50         60 
MCKGGNKVNK IKVRFAPSPT GPLHIGGARS ALFNYLFASR YNGEMVLRIE DTDLERSRRE 

        70         80         90        100        110        120 
YESEIIDSLK WLGLGWSEGI DTGGPNEPYR QTERLAIYQE YTKKLLEAGQ AYYCFCSEKE 

       130        140        150        160        170        180 
LEVERQDLLD SGQMQKYSGK CRQLSMAERE EKLKQGIKPA IRFKVPAHQL HIVDDLVRGR 

       190        200        210        220        230        240 
VSFDSDDIGD FIIVKSDGIP TYNFAVVIDD VLMGISHVIR AEEHLSNTPR QLMIYDALNF 

       250        260        270        280        290        300 
RRPEFAHISL ILGSDRQKMS KRHGATSLVQ YREMGYLPEA LFNFLALMGW SPEGEEEILS 

       310        320        330        340        350        360 
PAEITAAFSL ERVAKSPAVF DINKLNFINQ QYLKKIGDEE LKEMLKPYLA DSKYLKKIEQ 

       370        380        390        400        410        420 
MGEERYELLV STIRDYLVCL ADVKEQLEVF FGDIDYAGDA REVLAGEGVI PLLQAFKEGI 

       430        440        450        460        470        480 
HKVNKVEEIK QLIKGITKTL KLKPRDVFMP LRCALSGQAH GPDLSSYIAV IGGEEAIRRI 

       490 
DRAIDFIKSQ 

« Hide

References

[1]"The genome of Syntrophomonas wolfei: new insights into syntrophic metabolism and biohydrogen production."
Sieber J.R., Sims D.R., Han C., Kim E., Lykidis A., Lapidus A.L., McDonnald E., Rohlin L., Culley D.E., Gunsalus R., McInerney M.J.
Environ. Microbiol. 12:2289-2301(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: DSM 2245B / Goettingen.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000448 Genomic DNA. Translation: ABI69647.1.
RefSeqYP_755018.1. NC_008346.1.

3D structure databases

ProteinModelPortalQ0AUF7.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING335541.Swol_2357.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABI69647; ABI69647; Swol_2357.
GeneID4283756.
KEGGswo:Swol_2357.
PATRIC23859868. VBISynWol51738_2562.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0008.
HOGENOMHOG000252720.
KOK09698.
OMALMERADI.
OrthoDBEOG6DRPF7.
ProtClustDBCLSK2780822.

Enzyme and pathway databases

BioCycSWOL335541:GHL1-2420-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_SYNWW
AccessionPrimary (citable) accession number: Q0AUF7
Entry history
Integrated into UniProtKB/Swiss-Prot: March 24, 2009
Last sequence update: October 17, 2006
Last modified: February 19, 2014
This is version 59 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