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B1H0J3 (SYE_UNCTG) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 41. 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

EC=6.1.1.17
Alternative name(s):
Glutamyl-tRNA synthetase
Short name=GluRS
Gene names
Name:gltX
Ordered Locus Names:TGRD_542
OrganismUncultured termite group 1 bacterium phylotype Rs-D17 [Complete proteome] [HAMAP]
Taxonomic identifier471821 [NCBI]
Taxonomic lineageBacteriaElusimicrobiaenvironmental samples

Protein attributes

Sequence length494 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 – 494494Glutamate--tRNA ligase HAMAP-Rule MF_00022
PRO_1000090118

Regions

Motif10 – 2011"HIGH" region HAMAP-Rule MF_00022
Motif254 – 2585"KMSKS" region HAMAP-Rule MF_00022

Sites

Metal binding1101Zinc By similarity
Metal binding1121Zinc By similarity
Metal binding1371Zinc By similarity
Metal binding1391Zinc By similarity
Binding site2571ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
B1H0J3 [UniParc].

Last modified April 29, 2008. Version 1.
Checksum: E1A64E5136CA754A

FASTA49456,547
        10         20         30         40         50         60 
MSGIRVRFAP SPTGDLHIGG VRTALFNWLF AKNKGGKFIL RIEDTDETRS TGESAKVILD 

        70         80         90        100        110        120 
AMKWLELEWN EGPGNENLKY SPYSQMKRKE RGIYRKYADE LVAKELAYPC YCTPEEIDVM 

       130        140        150        160        170        180 
RKKAKADKLP PKYDGKCRHL TPGQRKQKEI EGKKAVVRFK MFGSGTTVLN DIIRGRVKFD 

       190        200        210        220        230        240 
NSLLDDFVIM KASGVPAYNF ACVVDDYLME ITHVLRGDDH ISNAPRQMHI YNALGWEMPE 

       250        260        270        280        290        300 
FAHMSMILGA GGARLSKRHG HTSVLEYRKE GYLREALINY LALLGWSTED SQQIFTIEEL 

       310        320        330        340        350        360 
KQKFSVERCG ISPSIFDPAK LLWLNGEKIR SKTPQQVYEL FIDWLKYTGN EKLTETWDVE 

       370        380        390        400        410        420 
LLKKALILEH DKIKLLKDIP SLVDFFFTKN VDYKEEAVKK TLLSEKSKDI AKLVLIESAA 

       430        440        450        460        470        480 
RLPNQLDFSA ISLEQYARNL AAEKNIKTGQ VFHPIRVAIS GRMQGPGLFQ MMEVMGKEDV 

       490 
VRRINVAINK FFQK 

« Hide

References

[1]"Complete genome of the uncultured termite group 1 bacteria in a single host protist cell."
Hongoh Y., Sharma V.K., Prakash T., Noda S., Taylor T.D., Kudo T., Sakaki Y., Toyoda A., Hattori M., Ohkuma M.
Proc. Natl. Acad. Sci. U.S.A. 105:5555-5560(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AP009510 Genomic DNA. Translation: BAG14025.1.
RefSeqYP_001956486.1. NC_020419.1.

3D structure databases

ProteinModelPortalB1H0J3.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING471821.TGRD_542.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID6373192.
KEGGrsd:TGRD_542.
PATRIC38571400. VBIUncTer52152_0883.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0008.
HOGENOMHOG000252722.
KOK01885.
OMAAFRCFCT.
OrthoDBEOG6DRPF7.

Enzyme and pathway databases

BioCycUTER471821:GJAD-580-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 nameSYE_UNCTG
AccessionPrimary (citable) accession number: B1H0J3
Entry history
Integrated into UniProtKB/Swiss-Prot: March 24, 2009
Last sequence update: April 29, 2008
Last modified: February 19, 2014
This is version 41 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