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Q2LQN4 (SYE1_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 1

EC=6.1.1.17
Alternative name(s):
Glutamyl-tRNA synthetase 1
Short name=GluRS 1
Gene names
Name:gltX1
Ordered Locus Names:SYNAS_01920
ORF Names:SYN_02557
OrganismSyntrophus aciditrophicus (strain SB) [Complete proteome] [HAMAP]
Taxonomic identifier56780 [NCBI]
Taxonomic lineageBacteriaProteobacteriaDeltaproteobacteriaSyntrophobacteralesSyntrophaceaeSyntrophus

Protein attributes

Sequence length472 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

Cofactor

Binds 1 zinc ion per subunit By similarity. 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
Metal-binding
Nucleotide-binding
Zinc
   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

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

tRNA binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 472472Glutamate--tRNA ligase 1 HAMAP-Rule MF_00022
PRO_0000237413

Regions

Motif13 – 2311"HIGH" region HAMAP-Rule MF_00022
Motif239 – 2435"KMSKS" region HAMAP-Rule MF_00022

Sites

Metal binding1021Zinc By similarity
Metal binding1041Zinc By similarity
Metal binding1291Zinc By similarity
Metal binding1311Zinc By similarity
Binding site2421ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
Q2LQN4 [UniParc].

Last modified February 21, 2006. Version 1.
Checksum: 4A1ED73395B51DE3

FASTA47253,248
        10         20         30         40         50         60 
MQKLKEIRTR FAPSPTGYLH IGGARTALFS WLYARHHQGK FVLRIEDTDQ LRSTEESTRA 

        70         80         90        100        110        120 
ILDAMTWLGL NWDEGPVFQA ERVDIHRAMI RKLVDEDKAY YCTCTPDELE EKRKRALAEG 

       130        140        150        160        170        180 
RKPKYDGTCR EKKLPPSPGT VVRFRCPQTG ITVVDDLIKG KISFNNEELD DLIIQRSDGY 

       190        200        210        220        230        240 
PTYNFAVVVD DAQMGISHVI RGDDHVNNTP RQILLYQALG YDIPHFGHVP MILGADKARL 

       250        260        270        280        290        300 
SKRHGATSVM AYKDMGYLPE ALVNYLVRLG WSHGDQEIFS LDELIALFGL ESIGKSAAVF 

       310        320        330        340        350        360 
NPEKLLWLNQ HYIKTYPEDR LLEVLQPFWK QLGIEAPDPD YGRSIVRDLR ARAKTLVDMA 

       370        380        390        400        410        420 
ESSTFYFNDE PAIDADAAKK FLTPEIAGHL EAIAEALATL GDYSKEGIEI FLRSLVEARA 

       430        440        450        460        470 
IKLKTIAQPL RIALTGKTVS PGLDDIMLTL GKERVIARIQ RTVAYIRSGM AS 

« 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: ABC76071.1.
RefSeqYP_460239.1. NC_007759.1.

3D structure databases

ProteinModelPortalQ2LQN4.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING56780.SYN_02557.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABC76071; ABC76071; SYN_02557.
GeneID3884491.
KEGGsat:SYN_02557.
PATRIC23860759. VBISynAci70500_0208.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0008.
HOGENOMHOG000252722.
KOK01885.
OMARANQGKF.
OrthoDBEOG6DRPF7.

Enzyme and pathway databases

BioCycSACI56780:GHXT-195-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 nameSYE1_SYNAS
AccessionPrimary (citable) accession number: Q2LQN4
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