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B5YIG1 (SYE_THEYD) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 43. 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:THEYE_A2003
OrganismThermodesulfovibrio yellowstonii (strain ATCC 51303 / DSM 11347 / YP87) [Reference proteome] [HAMAP]
Taxonomic identifier289376 [NCBI]
Taxonomic lineageBacteriaNitrospiraeNitrospiralesNitrospiraceaeThermodesulfovibrio

Protein attributes

Sequence length465 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
Reference 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 – 465465Glutamate--tRNA ligase HAMAP-Rule MF_00022
PRO_0000367785

Regions

Motif8 – 1811"HIGH" region HAMAP-Rule MF_00022
Motif234 – 2385"KMSKS" region HAMAP-Rule MF_00022

Sites

Metal binding971Zinc By similarity
Metal binding991Zinc By similarity
Metal binding1241Zinc By similarity
Metal binding1261Zinc By similarity
Binding site2371ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
B5YIG1 [UniParc].

Last modified November 25, 2008. Version 1.
Checksum: 3BFE8CBCAEEC0E37

FASTA46553,999
        10         20         30         40         50         60 
MVRVRFAPSP TGHLHIGGAR TALFNWLFAR HHNGKFILRI EDTDRSRSTE EYIESIIEAM 

        70         80         90        100        110        120 
KWLGLDWDEG PFRQTDRMEV YKAYAYKLLE EGKAYRCYCT PEELEERRQQ AMKEGKPPRY 

       130        140        150        160        170        180 
DRRCREIKET LNKPFAIRFK MPLEGETVVD DLVKGKVTFK NSEIEDLVIL RSDGTPTYNF 

       190        200        210        220        230        240 
CVVVDDFEMG ITHVIRGEDH LNNTPKQIHI YHALGMNPPE FAHIPMILGT DRARLSKRHG 

       250        260        270        280        290        300 
ATSVLSYRDE GYLSDALVNF LARLGWSYGD KEIFTREELI KYFNLEQVGK ANAVFNAEKL 

       310        320        330        340        350        360 
LWLNSEYIKL TPEEKLFELV KPFLIKEGYL KEGETLDKDW ACRAIKSLKE RCRTLKELAH 

       370        380        390        400        410        420 
AMRYYLLDYV EIEPKAKEKY INAETVPVLR EVTEKLAALE EFTQERIEKI FMDIVNEKGL 

       430        440        450        460 
KLGQVAQPVR VVMTGSTVSP GIYEVLEIAG KEKTLKRLRR VIDAS 

« Hide

References

[1]"The complete genome sequence of Thermodesulfovibrio yellowstonii strain ATCC 51303 / DSM 11347 / YP87."
Dodson R.J., Durkin A.S., Wu M., Eisen J., Sutton G.
Submitted (AUG-2008) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 51303 / DSM 11347 / YP87.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP001147 Genomic DNA. Translation: ACI20684.1.
RefSeqYP_002249792.1. NC_011296.1.

3D structure databases

ProteinModelPortalB5YIG1.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING289376.THEYE_A2003.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACI20684; ACI20684; THEYE_A2003.
GeneID6941512.
KEGGtye:THEYE_A2003.
PATRIC23911033. VBITheYel104483_1957.

Phylogenomic databases

eggNOGCOG0008.
HOGENOMHOG000252720.
KOK01885.
OMAAFRCFCT.
OrthoDBEOG6DRPF7.

Enzyme and pathway databases

BioCycTYEL289376:GH9L-1992-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_THEYD
AccessionPrimary (citable) accession number: B5YIG1
Entry history
Integrated into UniProtKB/Swiss-Prot: March 24, 2009
Last sequence update: November 25, 2008
Last modified: February 19, 2014
This is version 43 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