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Q9PJU7 (SYE_CHLMU) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 89. 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:TC_0730
OrganismChlamydia muridarum (strain MoPn / Nigg) [Complete proteome] [HAMAP]
Taxonomic identifier243161 [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
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_0000119538

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
Q9PJU7 [UniParc].

Last modified October 1, 2000. Version 1.
Checksum: 692A300EA5267DC5

FASTA50658,981
        10         20         30         40         50         60 
MTFQNVRVRV APSPTGDPHV GTAYMALFNE VFARKFNGKM ILRIEDTDQT RSRDDYEKNI 

        70         80         90        100        110        120 
FSALKWCGIR WDEGPDIGGP YGPYRQSERT EIYKKYAEIL LQTDYAYKCF ATPQELQEMR 

       130        140        150        160        170        180 
AVASTLGYRG GYDRRYRYLS AEEVRQREEQ GQPYTIRLKV PLTGESVFED QCKGRVVFPW 

       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 EGSPESLLKE LKDWLWNDEF LLKILPLCQT 

       370        380        390        400        410        420 
RITTLADFIR LTSFFFMAIP EYSKEDLLPS SLGHQQAAVM LYSLVKYLEK KDLWEKDFFY 

       430        440        450        460        470        480 
QGSKWLAEAF QVHHKKAVIP LLYVTITGEK QGLPLFDSME LLGKARTRAR LTHAQNLLGG 

       490        500 
VPKKLQQQID KALQDQPLEE IRFLDF 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE002160 Genomic DNA. Translation: AAF39540.1.
PIRF81671.
RefSeqNP_297104.1. NC_002620.2.

3D structure databases

ProteinModelPortalQ9PJU7.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING243161.TC0730.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAF39540; AAF39540; TC_0730.
GeneID1246093.
KEGGcmu:TC_0730.
PATRIC20372934. VBIChlMur19118_0777.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0008.
KOK01885.
OMAWINGYYL.
OrthoDBEOG6DRPF7.

Enzyme and pathway databases

BioCycCMUR243161:GHYU-755-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.
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_CHLMU
AccessionPrimary (citable) accession number: Q9PJU7
Entry history
Integrated into UniProtKB/Swiss-Prot: April 27, 2001
Last sequence update: October 1, 2000
Last modified: May 14, 2014
This is version 89 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