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Q73R87 (SYE_TREDE) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 69. 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:TDE_0204
OrganismTreponema denticola (strain ATCC 35405 / CIP 103919 / DSM 14222) [Complete proteome] [HAMAP]
Taxonomic identifier243275 [NCBI]
Taxonomic lineageBacteriaSpirochaetesSpirochaetalesSpirochaetaceaeTreponema

Protein attributes

Sequence length506 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 – 506506Glutamate--tRNA ligase HAMAP-Rule MF_00022
PRO_0000119686

Regions

Motif9 – 1911"HIGH" region HAMAP-Rule MF_00022
Motif251 – 2555"KMSKS" region HAMAP-Rule MF_00022

Sites

Binding site2541ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
Q73R87 [UniParc].

Last modified July 5, 2004. Version 1.
Checksum: 9E3D62E7D58393F2

FASTA50658,234
        10         20         30         40         50         60 
MQVKVRYAPS PTGFQHIGGV RTALFNYLFA RSKGGKFVLR IEDTDRTRYS EEYEQNLYDT 

        70         80         90        100        110        120 
LEWLGLEWDE GGPKGGPCAP YIQSQRFDIY RKYAQELVDK GFAYYCFCDS ERLDRIRKIQ 

       130        140        150        160        170        180 
TMNKMPPGYD RACRNLTDEE IKAKMDEGIP YVIRLKVPLE GSTKFTDALL GDIEWKNEDI 

       190        200        210        220        230        240 
NPDQILLKSD GFPTYHLANI VDDHLMGITH VMRAQEWLPS TPMHVIMYKA FGWEPPQFCH 

       250        260        270        280        290        300 
LPMVMGNDGQ KLSKRHGATS CNEFRNKGYL KEAIINYVAM LGCSYEDGRD MYSLSDLEKL 

       310        320        330        340        350        360 
FDIKHLNKAP AVFDYKKLEW FNGQYMREKT DEELFALTWP YIANSGLFGK INEEELKKAG 

       370        380        390        400        410        420 
CRFENQTYLK PTQEQKEILM KVMPLVKERL HLLSEITEMV RFLFEEPAVP PAEEIIPKKL 

       430        440        450        460        470        480 
DAETTKKVLQ KAIEVMPKIL GLDDHAGGEV FRAEADAMGI KMGDFMMPVR MTVTGSRISP 

       490        500 
PLVGSIQILG IEKAIKRIEK AIAERF 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE017226 Genomic DNA. Translation: AAS10701.1.
RefSeqNP_970820.1. NC_002967.9.

3D structure databases

ProteinModelPortalQ73R87.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING243275.TDE0204.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAS10701; AAS10701; TDE_0204.
GeneID2739810.
KEGGtde:TDE0204.
PATRIC20522658. VBITreDen445_0198.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0008.
KOK01885.
OMAAFRCFCT.
OrthoDBEOG6DRPF7.
ProtClustDBPRK01406.

Enzyme and pathway databases

BioCycTDEN243275:GJ7G-205-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.
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.
ProtoNetSearch...

Entry information

Entry nameSYE_TREDE
AccessionPrimary (citable) accession number: Q73R87
Entry history
Integrated into UniProtKB/Swiss-Prot: June 7, 2005
Last sequence update: July 5, 2004
Last modified: February 19, 2014
This is version 69 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