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P59691 (SYE_CHLP6) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 63. 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:CPSIT_0206, G5O_0208
OrganismChlamydophila psittaci (strain ATCC VR-125 / 6BC) (Chlamydia psittaci) [Complete proteome] [HAMAP]
Taxonomic identifier331636 [NCBI]
Taxonomic lineageBacteriaChlamydiaeChlamydialesChlamydiaceaeChlamydia/Chlamydophila groupChlamydia

Protein attributes

Sequence length505 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.

Sequence caution

The sequence AAA23122.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

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 – 505505Glutamate--tRNA ligase HAMAP-Rule MF_00022
PRO_0000119540

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
P59691 [UniParc].

Last modified June 28, 2011. Version 2.
Checksum: 9D51E741448A9B22

FASTA50558,540
        10         20         30         40         50         60 
MAWENVRVRV APSPTGDPHV GTAYMALFNE IFAKRFNGKM ILRIEDTDQT RSRDDYEKNI 

        70         80         90        100        110        120 
FSALKWCGIQ WDEGPDIGGP YGPYRQSERT EIYREYAELL LKTDYAYKCF ATPKELEEMR 

       130        140        150        160        170        180 
AVATTLGYRG GYDRRYRYLS PEEIEARTRE GQPYTIRLKV PLTGECVLDD YCKGRVVFPW 

       190        200        210        220        230        240 
ADVDDQVLIK SDGFPTYHFA NVVDDHLMGI THVLRGEEWL SSTPKHLLLY EAFGWEAPTF 

       250        260        270        280        290        300 
LHMPLLLNPD GTKLSKRKNP TSIFYYRDAG YVKEAFMNFL TLMGYSMEGD EEIYSLEKLI 

       310        320        330        340        350        360 
ANFDPRRIGK SGAVFDTRKL DWMNKHYLTH EKSSESLLAK LKDWLINDEF FLKILPLCQS 

       370        380        390        400        410        420 
RITTLAEFIG FTGFFFSVLP EYSKEELLPA TIVEEKAAIL LYSYVKYLEK ADLWVKDQFY 

       430        440        450        460        470        480 
QGSKWLSSAF QVHHKKVVIP LLYVAITGKK QGLPLFDSME LLGKPRTRAR LVHAQNLLGG 

       490        500 
VPKKIQTTID KVLKEEDFEN KIFEF 

« Hide

References

« Hide 'large scale' references
[1]"Full-length de novo sequence of the Chlamydophila psittaci type strain, 6BC."
Voigt A., Schofl G., Heidrich A., Sachse K., Saluz H.P.
J. Bacteriol. 193:2662-2663(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC VR-125 / 6BC.
[2]"Genome sequences of the zoonotic pathogens Chlamydia psittaci 6BC and Cal10."
Grinblat-Huse V., Drabek E.F., Creasy H.H., Daugherty S.C., Jones K.M., Santana-Cruz I., Tallon L.J., Read T.D., Hatch T.P., Bavoil P., Myers G.S.
J. Bacteriol. 193:4039-4040(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC VR-125 / 6BC.
[3]"Identification of an early-stage gene of Chlamydia psittaci 6BC."
Wichlan D.W., Hatch T.P.
J. Bacteriol. 175:2936-2942(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-368.
Strain: ATCC VR-125 / 6BC.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP002549 Genomic DNA. Translation: ADZ18786.1.
CP002586 Genomic DNA. Translation: AEB55211.1.
L13598 Genomic DNA. Translation: AAA23122.1. Different initiation.
PIRA36909.
RefSeqYP_004422038.1. NC_015470.1.
YP_005662884.1. NC_017287.1.

3D structure databases

ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaADZ18786; ADZ18786; CPSIT_0206.
AEB55211; AEB55211; G5O_0208.
GeneID10602476.
12242467.
KEGGchb:G5O_0208.
chp:CPSIT_0206.
PATRIC47105011. VBIChlPsi52874_0193.

Organism-specific databases

CMRSearch...

Phylogenomic databases

KOK01885.
OMAWINGYYL.

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_CHLP6
AccessionPrimary (citable) accession number: P59691
Secondary accession number(s): F0T375, P94662, Q06560
Entry history
Integrated into UniProtKB/Swiss-Prot: May 23, 2003
Last sequence update: June 28, 2011
Last modified: May 14, 2014
This is version 63 of the entry and version 2 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