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A8F597 (SYE1_THELT) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 32. 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 1

EC=6.1.1.17
Alternative name(s):
Glutamyl-tRNA synthetase 1
Short name=GluRS 1
Gene names
Name:gltX1
Ordered Locus Names:Tlet_0765
OrganismThermotoga lettingae (strain ATCC BAA-301 / DSM 14385 / TMO) [Complete proteome] [HAMAP]
Taxonomic identifier416591 [NCBI]
Taxonomic lineageBacteriaThermotogaeThermotogalesThermotogaceaeThermotoga

Protein attributes

Sequence length470 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 MF_00022_B

Catalytic activity

ATP + L-glutamate + tRNA(Glu) = AMP + diphosphate + L-glutamyl-tRNA(Glu). HAMAP MF_00022_B

Subunit structure

Monomer By similarity. HAMAP MF_00022_B

Subcellular location

Cytoplasm By similarity HAMAP MF_00022_B.

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: InterPro

   Cellular componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

glutamate-tRNA ligase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 470470Glutamate--tRNA ligase 1 HAMAP MF_00022_B
PRO_0000367788

Regions

Motif8 – 1811"HIGH" region HAMAP MF_00022_B
Motif250 – 2545"KMSKS" region HAMAP MF_00022_B

Sites

Binding site2531ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
A8F597 [UniParc].

Last modified November 13, 2007. Version 1.
Checksum: 9C0343F255E6FF11

FASTA47054,007
        10         20         30         40         50         60 
MVRVRFAPSP TGYLHVGGAR TALFNYLFAK HHGGKFILRI EDTDIARSEG IFEENLMKTL 

        70         80         90        100        110        120 
QWLGLNWDEG PDIGGSFGPY RQSERLNIYE EYAKKLIALD KAYEVFAYPE EIEEIREKLL 

       130        140        150        160        170        180 
SKGLTPHYDR TIFEPFATKE RKREYEEKGL KPAIYFSMPR KAFIHNDLVK GTVQFSEGSV 

       190        200        210        220        230        240 
GDFAILRSNG IPTYNFACVV DDMLMQITHV IRGDDHLPNT VKQLALYEAF SARPPEIGHV 

       250        260        270        280        290        300 
STILGPDGKK LSKRHGATSI EELRERGYLP QAVVNYLALL GWSSPDAKEI MSMQEMIERF 

       310        320        330        340        350        360 
SIDRLSKNPA IFDPAKLSWM NGQYIRSTNE EELEQLLKPL LEKWNFIPRN QDWLRRVIIA 

       370        380        390        400        410        420 
VKDRLHTLED FQHVADFFFV KPEIKTETEY QIKCAMLECA DKLESLDRSD KNSIVEVFRS 

       430        440        450        460        470 
TIKKQKVSAK EFYSTLRYVL TGKHEGPELV DIVFLLGPNE VAARIKSILG 

« Hide

References

[1]"Complete sequence of Thermotoga lettingae TMO."
Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E., Tice H., Pitluck S., Foster B., Bruce D., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Nelson K., Gogarten J.P., Noll K., Richardson P.
Submitted (AUG-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC BAA-301 / DSM 14385 / TMO.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000812 Genomic DNA. Translation: ABV33331.1.
RefSeqYP_001470395.1. NC_009828.1.

3D structure databases

ProteinModelPortalA8F597.
SMRA8F597. Positions 1-470.
ModBaseSearch...

Protein-protein interaction databases

STRINGA8F597.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID5607932.
GenomeReviewsGene locus Tlet_0765 in contig CP000812_GR.
KEGGtle:Tlet_0765.
PATRIC23932073. VBITheLet125395_0797.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHBG628189.
OMALMEITHI.
ProtClustDBPRK01406.

Enzyme and pathway databases

BioCycTLET416591:TLET_0765-MONOMER.

Family and domain databases

HAMAPMF_00022_B. Glu_tRNA_synth_B.
[Tree]
InterProIPR008925. aa-tRNA-synth_I_codon-bd.
IPR020751. aa-tRNA-synth_I_codon-bd_sub2.
IPR001412. aa-tRNA-synth_I_CS.
IPR004527. Glu-tRNA-synth_Ib_bac/mito.
IPR000924. Glu/Gln-tRNA-synth_Ib.
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]
Gene3DG3DSA:1.10.1160.10. Glu/Gln-tRNA-synth_Ic_a-bdl. 1 hit.
G3DSA:3.40.50.620. Rossmann-like_a/b/a_fold. 2 hits.
G3DSA:1.10.10.350. tRNA_synt_bd. 1 hit.
KOK09698.
PANTHERPTHR10119. Glu_tRNA-synt_1c. 1 hit.
PTHR10119:SF1. PTHR10119:SF1. 1 hit.
PfamPF00749. tRNA-synt_1c. 1 hit.
[Graphical view]
PRINTSPR00987. TRNASYNTHGLU.
SUPFAMSSF48163. tRNA-synt_bind. 1 hit.
TIGRFAMsTIGR00464. GltX_bact. 1 hit.
PROSITEPS00178. AA_TRNA_LIGASE_I. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameSYE1_THELT
AccessionPrimary (citable) accession number: A8F597
Entry history
Integrated into UniProtKB/Swiss-Prot: March 24, 2009
Last sequence update: November 13, 2007
Last modified: January 25, 2012
This is version 32 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

Aminoacyl-tRNA synthetases

List of aminoacyl-tRNA synthetase entries

SIMILARITY comments

Index of protein domains and families