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Q9F724 (SYE_CHLTE) 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:CT0299
OrganismChlorobium tepidum (strain ATCC 49652 / DSM 12025 / TLS) [Reference proteome] [HAMAP]
Taxonomic identifier194439 [NCBI]
Taxonomic lineageBacteriaChlorobiChlorobiaChlorobialesChlorobiaceaeChlorobaculum

Protein attributes

Sequence length503 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 AAG12192.1 differs from that shown. Reason: Frameshift at position 317.

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 – 503503Glutamate--tRNA ligase HAMAP-Rule MF_00022
PRO_0000119541

Regions

Motif12 – 2211"HIGH" region HAMAP-Rule MF_00022
Motif259 – 2635"KMSKS" region HAMAP-Rule MF_00022

Sites

Binding site2621ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
Q9F724 [UniParc].

Last modified August 30, 2002. Version 2.
Checksum: 8A265B64E72F4D80

FASTA50357,810
        10         20         30         40         50         60 
MAGQKVRTRF APSPTGYLHV GGLRTALYNY LFAKRMNGDF VIRIEDTDQS RKVEDAEKKL 

        70         80         90        100        110        120 
ISTLEWAGII ADESPMHGGN YGPYVQSQRL SIYRDYCTRL LEDKNAYYCF STPEELEENR 

       130        140        150        160        170        180 
QLQLKQGLQP KYNRKWLPED MGGNMPESEI KKKLDEGAPY VVRMKVPDYV SVWFEDMIRG 

       190        200        210        220        230        240 
PIEFDSATID DQVLMKSDGF PTYHFASVID DHLMEFTHII RGEEWLPSMP KHLLLYEFFG 

       250        260        270        280        290        300 
WEPPKFAHLP LLLNPDRSKL SKRQGDVAVE DYMRKGYSSE AIVNFVALLG WNEGEGSEQE 

       310        320        330        340        350        360 
VFSMEELISK FSLERVGKAG AVFNVEKLSW LEKQYIKTRP VEKIVGNIKP VLQAKLAEFS 

       370        380        390        400        410        420 
PEMSVERITS DDYLAKVVEL MRERVNFEHE FVTFSSYFFF EPESYEEEAV AKRWTPNVPP 

       430        440        450        460        470        480 
LLQEFADLLE ANDDFTAENI EAQLKAFVAP KGLKPAVLIH PIRIAVSGVS FGPSLYHMLE 

       490        500 
VLGKEAVLRR IRRAIERIEV PAA 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE006470 Genomic DNA. Translation: AAM71545.1.
AF287480 Genomic DNA. Translation: AAG12192.1. Frameshift.
RefSeqNP_661203.1. NC_002932.3.

3D structure databases

ProteinModelPortalQ9F724.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING194439.CT0299.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAM71545; AAM71545; CT0299.
GeneID1007958.
KEGGcte:CT0299.
PATRIC21398713. VBIChlTep116050_0290.

Phylogenomic databases

eggNOGCOG0008.
HOGENOMHOG000252720.
KOK01885.
OMAVTGQTHG.
OrthoDBEOG6DRPF7.

Enzyme and pathway databases

BioCycCTEP194439:GHN0-315-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_CHLTE
AccessionPrimary (citable) accession number: Q9F724
Entry history
Integrated into UniProtKB/Swiss-Prot: April 27, 2001
Last sequence update: August 30, 2002
Last modified: May 14, 2014
This is version 92 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