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Q2YQ56 (SYE1_BRUA2) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 40. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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
Synonyms:gltX-1
Ordered Locus Names:BAB1_1034
OrganismBrucella abortus (strain 2308) [Complete proteome] [HAMAP]
Taxonomic identifier359391 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRhizobialesBrucellaceaeBrucella

Protein attributes

Sequence length457 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 – 457457Glutamate--tRNA ligase 1 HAMAP MF_00022_B
PRO_0000237345

Regions

Motif9 – 1911"HIGH" region HAMAP MF_00022_B
Motif250 – 2545"KMSKS" region HAMAP MF_00022_B

Sites

Binding site2531ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
Q2YQ56 [UniParc].

Last modified February 7, 2006. Version 1.
Checksum: CB61D0FD9A6C460D

FASTA45750,828
        10         20         30         40         50         60 
MTVTVRFAPS PTGYIHIGNT RTALSNWLYA SKNNGKFILR YDDTDVERSK DEYAQAIAVD 

        70         80         90        100        110        120 
LDWLGVRPDR VEYQSKRFDI YAKAVEKLKT AGLLYACYET ADELERRRKF RLARRLPPVY 

       130        140        150        160        170        180 
GREALKLTDA EKAALEAEGR KPHWRFLLPN FESDPFATQR TEVHWDDLVR GPQTVDLASM 

       190        200        210        220        230        240 
SDPILVREDG TYLYTLPSVV DDIDMGVTHI IRGDDHVTNT GVQISIFKAL GATPPVFGHH 

       250        260        270        280        290        300 
NLLTTISGEG LSKRTGALSV GSLREAGYEP MAVASLAILI GTSESVTAAP DMAALAEHFD 

       310        320        330        340        350        360 
LASISKSSAK FDPSELDALN RSLLHEMPFE KAKPRLEALG ICGAKAESFW LAVRGNLDRF 

       370        380        390        400        410        420 
SDVSHWWQVV SGDLPEAPDL SGEDRDFVRH AFDLLPPEPW NGQTWKSWTE AVKSATGRKG 

       430        440        450 
KNLFMPLRLA LTGQAHGPEL ADLLVLVGLE RTKSRRP 

« Hide

References

[1]"Whole-genome analyses of speciation events in pathogenic Brucellae."
Chain P.S., Comerci D.J., Tolmasky M.E., Larimer F.W., Malfatti S.A., Vergez L.M., Aguero F., Land M.L., Ugalde R.A., Garcia E.
Infect. Immun. 73:8353-8361(2005) [PubMed: 16299333] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 2308.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AM040264 Genomic DNA. Translation: CAJ10990.1.
RefSeqYP_414440.1. NC_007618.1.

3D structure databases

ProteinModelPortalQ2YQ56.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ2YQ56.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID3788733.
GenomeReviewsGene locus BAB1_1034 in contig AM040264_GR.
KEGGbmf:BAB1_1034.
PATRIC17845014. VBIBruMel86222_1079.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0008.
HOGENOMHBG628189.
OMADQERIEW.
ProtClustDBPRK12558.

Enzyme and pathway databases

BioCycBMEL359391:BAB1_1034-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_BRUA2
AccessionPrimary (citable) accession number: Q2YQ56
Entry history
Integrated into UniProtKB/Swiss-Prot: May 30, 2006
Last sequence update: February 7, 2006
Last modified: January 25, 2012
This is version 40 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

Brucella abortus strain 2308

Brucella abortus (strain 2308): entries and gene names

SIMILARITY comments

Index of protein domains and families