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Q5LWB2 (SYE1_SILPO) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 50. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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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
Synonyms:gltX-1
Ordered Locus Names:SPO0430
OrganismSilicibacter pomeroyi (strain ATCC 700808 / DSM 15171 / DSS-3) [Complete proteome] [HAMAP]
Taxonomic identifier246200 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Alphaproteobacteria › Rhodobacterales › Rhodobacteraceae › Ruegeria

Protein attributes

Sequence length443 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 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 – 443443Glutamate--tRNA ligase 1 HAMAP MF_00022_B
PRO_0000119649

Regions

Motif10 – 2011"HIGH" region HAMAP MF_00022_B
Motif241 – 2455"KMSKS" region HAMAP MF_00022_B

Sites

Binding site2441ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
Q5LWB2 [UniParc].

Last modified February 1, 2005. Version 1.
Checksum: 9E3D61CCD6DE7103

FASTA44348,927
        10         20         30         40         50         60 
MSMTTTRFAP SPTGYIHVGN LRTALMNYLI ARKAGGTFIL RIDDTDPERS KEEYVDAIKQ 

        70         80         90        100        110        120 
DLDWLGLHWD RVERQSERLD RYAEAADKLR AMGRFYEAFE TPTELDLKRK KQLNMGKPPV 

       130        140        150        160        170        180 
YDRAALALSE GEKEALRAER GNGVWRFKLD QERIEWTDGI LGDISIDAAS VSDPVLIRGD 

       190        200        210        220        230        240 
GQVLYTLASV VDDTDMGVTD VVRGSDHVTN TATQIQIMAA LGFEHPRFAH HSLLTGPQGE 

       250        260        270        280        290        300 
ALSKRLGTLA LRDLREQGVQ PMALLSLMAR LGSSDPVELR SDMAELIEGF DVTRFGAAPT 

       310        320        330        340        350        360 
KFDVQDLFPL TGRYLQALPL EAVAKDVAAA GVPEDLAAPF WSMARENITT LNDLAGWWAL 

       370        380        390        400        410        420 
CRDGAEPLIA DEDRAFVTEA MALLPEGPLD ADSWGAWTQA VKEATGRKGK GLFMPLRKAV 

       430        440 
TGMERGPEMA TLLPLMQVIR ARG

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP000031 Genomic DNA. Translation: AAV93748.1.
RefSeqYP_165693.1. NC_003911.11.

3D structure databases

ProteinModelPortalQ5LWB2.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID3192955.
GenomeReviewsGene locus SPO0430 in contig CP000031_GR.
KEGGsil:SPO0430.
NMPDRfig|246200.3.peg.828.
PATRIC23374125. VBIRuePom114501_0439.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHBG628189.
OMADQERIEW.
ProtClustDBPRK12558.

Enzyme and pathway databases

BioCycRPOM246200:SPO_0430-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.
KOK01885.
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_SILPO
AccessionPrimary (citable) accession number: Q5LWB2
Entry history
Integrated into UniProtKB/Swiss-Prot: June 7, 2005
Last sequence update: February 1, 2005
Last modified: January 25, 2012
This is version 50 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

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