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B2V5J1 (SYE_SULSY) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 44. 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:SYO3AOP1_1325
OrganismSulfurihydrogenibium sp. (strain YO3AOP1) [Complete proteome] [HAMAP]
Taxonomic identifier436114 [NCBI]
Taxonomic lineageBacteriaAquificaeAquificalesHydrogenothermaceaeSulfurihydrogenibium

Protein attributes

Sequence length478 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 – 478478Glutamate--tRNA ligase HAMAP-Rule MF_00022
PRO_0000367776

Regions

Motif8 – 1811"HIGH" region HAMAP-Rule MF_00022
Motif248 – 2525"KMSKS" region HAMAP-Rule MF_00022

Sites

Binding site2511ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
B2V5J1 [UniParc].

Last modified July 1, 2008. Version 1.
Checksum: 9DE44E847E45BD25

FASTA47855,797
        10         20         30         40         50         60 
MKRVRFAPSP TGYLHLGNAR TALFNYLFSR HENATFILRI EDTDLERSKK EYEEMLMEDL 

        70         80         90        100        110        120 
KWMGIEWDEG PDAGGPHGPY RQSERLEIYM KYVDKLLKSG DAYYCYCTEE ELEQEREKAI 

       130        140        150        160        170        180 
AEGRPYRYSG KCRNLTPEER AFYEGKSIKP VIRFKVPDKT VVFEDIIRGH VEIDTKEFGD 

       190        200        210        220        230        240 
FVIVRQDGMP VYNFVVVIDD ALMGITHVIR GEDHLSNTPK QIVIYEALGF AIPQFAHLPI 

       250        260        270        280        290        300 
ILGEDRTKLS KRHGAVSVRA LKDDGFISEA VFNYLSLLGW HPKEEKEILS KEEIIKQFRI 

       310        320        330        340        350        360 
EDVNKSPAIF DRTKLRWMNG VYIREILDLD DLTKRAIPFF EGFGYKADYE FYKKVMSAIR 

       370        380        390        400        410        420 
DSIETLMEIK ERAKVFFVDE FPYTEEIVNE VKSDENVYKV VEIFYNKIKN LSAITKEDFK 

       430        440        450        460        470 
NITKEIQKEY GYKGKALFHP IRIALTGEPS GVGLDLLVEV IGIERVKFRL ERFLEYFG 

« Hide

References

[1]"Complete and draft genome sequences of six members of the Aquificales."
Reysenbach A.-L., Hamamura N., Podar M., Griffiths E., Ferreira S., Hochstein R., Heidelberg J., Johnson J., Mead D., Pohorille A., Sarmiento M., Schweighofer K., Seshadri R., Voytek M.A.
J. Bacteriol. 191:1992-1993(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: YO3AOP1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP001080 Genomic DNA. Translation: ACD66935.1.
RefSeqYP_001931489.1. NC_010730.1.

3D structure databases

ProteinModelPortalB2V5J1.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING436114.SYO3AOP1_1325.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACD66935; ACD66935; SYO3AOP1_1325.
GeneID6332677.
KEGGsul:SYO3AOP1_1325.
PATRIC23767513. VBISulSp94719_1382.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0008.
HOGENOMHOG000252720.
KOK01885.
OMAAFRCFCT.
OrthoDBEOG6DRPF7.
ProtClustDBPRK01406.

Enzyme and pathway databases

BioCycSSP436114:GI6I-1373-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 nameSYE_SULSY
AccessionPrimary (citable) accession number: B2V5J1
Entry history
Integrated into UniProtKB/Swiss-Prot: March 24, 2009
Last sequence update: July 1, 2008
Last modified: February 19, 2014
This is version 44 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