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O84451 (SYE_CHLTR) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 92. 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:CT_445
OrganismChlamydia trachomatis (strain D/UW-3/Cx) [Reference proteome] [HAMAP]
Taxonomic identifier272561 [NCBI]
Taxonomic lineageBacteriaChlamydiaeChlamydialesChlamydiaceaeChlamydia/Chlamydophila groupChlamydia

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
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

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_0000119542

Regions

Motif12 – 2211"HIGH" region HAMAP-Rule MF_00022
Motif253 – 2575"KMSKS" region HAMAP-Rule MF_00022

Sites

Binding site2561ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
O84451 [UniParc].

Last modified November 1, 1998. Version 1.
Checksum: BF234D36FF10D2B9

FASTA50658,511
        10         20         30         40         50         60 
MTVQNVRVRV APSPTGDPHV GTAYMALFNE VFARKYNGQM ILRIEDTDQT RSRDDYEANI 

        70         80         90        100        110        120 
FSALKWCGIR WDEGPDVGGA YGPYRQSERT EIYKKYAEIL LQTDCAYKCF ATPQELQEMR 

       130        140        150        160        170        180 
AVASTLGYRG GYDRRYRYLS PEEVRQREEQ GQPYTIRLKV PLTGESVFED QCKGCVVFPW 

       190        200        210        220        230        240 
ADVDDQVLVK SDGFPTYHFA NVVDDHLMGI THVLRGEEWL SSTPKHLLLY EAFGWEPPQF 

       250        260        270        280        290        300 
FHMPLLLNPD GSKLSKRKNP TSIFYYRDAG YKKEAFMNFL TLMGYSMEGD EEIYSMQRLI 

       310        320        330        340        350        360 
EAFDPKRIGR SGAVFDIRKL DWMNKHYLNH EGSPESLLQE LKGWLWNDEF LLKILPLCQS 

       370        380        390        400        410        420 
RITTLADFVG LTSFFFTAIP QYSKEELLPS SLKQEQAAVM LYSLVKYLEK KDLWEKDFFY 

       430        440        450        460        470        480 
QGSKWLAEAF QVHHKKAVIP LLYVAITGAK QGLPLFDSME LLGKARTRAR LTYAQNLLGG 

       490        500 
VSKKVQQQVD KALQDQPLED IRFLDF 

« Hide

References

[1]"Genome sequence of an obligate intracellular pathogen of humans: Chlamydia trachomatis."
Stephens R.S., Kalman S., Lammel C.J., Fan J., Marathe R., Aravind L., Mitchell W.P., Olinger L., Tatusov R.L., Zhao Q., Koonin E.V., Davis R.W.
Science 282:754-759(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: D/UW-3/Cx.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE001273 Genomic DNA. Translation: AAC68044.1.
PIRF71513.
RefSeqNP_219958.1. NC_000117.1.

3D structure databases

ProteinModelPortalO84451.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING272561.CT445.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAC68044; AAC68044; CT_445.
GeneID884218.
KEGGctr:CT_445.
PATRIC20380457. VBIChlTra43535_0481.

Phylogenomic databases

eggNOGCOG0008.
KOK01885.
OMATKHSNVM.
OrthoDBEOG6DRPF7.

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_CHLTR
AccessionPrimary (citable) accession number: O84451
Entry history
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: November 1, 1998
Last modified: May 14, 2014
This is version 92 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