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Q0BTZ0 (SYE1_GRABC) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 44. 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:GbCGDNIH1_0814
OrganismGranulibacter bethesdensis (strain ATCC BAA-1260 / CGDNIH1) [Complete proteome] [HAMAP]
Taxonomic identifier391165 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRhodospirillalesAcetobacteraceaeGranulibacter

Protein attributes

Sequence length473 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 – 473473Glutamate--tRNA ligase 1 HAMAP MF_00022_B
PRO_0000330973

Regions

Motif23 – 3311"HIGH" region HAMAP MF_00022_B
Motif252 – 2565"KMSKS" region HAMAP MF_00022_B

Sites

Binding site2551ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
Q0BTZ0 [UniParc].

Last modified October 17, 2006. Version 1.
Checksum: 5081EECA24D166E8

FASTA47352,327
        10         20         30         40         50         60 
MHSLTTHKHV RGGDMTIRTR FAPSPTGLLH VGGARTALFN YLFARHHGGE YLLRIEDTDR 

        70         80         90        100        110        120 
ARSTPEAVQV ILDGLDWLGL SPDQEPVFQS TRETRHTEVA HSLLERGMAY RCFLSPEELQ 

       130        140        150        160        170        180 
AQRDQAAADK RPLRINSPWR DRDLSEAPSG IAPVIRLRVP QEGETVVDDL VQGPVRVANA 

       190        200        210        220        230        240 
ELDDMIILRS DGTPTYLHAV VVDDHDMAIT HVIRGDDHLT NTFRQVQIFK ALGWDLPRFA 

       250        260        270        280        290        300 
HIPLIHGADG AKLSKRHGAV SVLEFEREGF LPEALCNYLL RLGWGHGDAE ILSRDEQVAL 

       310        320        330        340        350        360 
FDLDGVGRAA SRMDYAKLTH LNGVYLREAD DQRLTTDLCR RLDLSPDSDA SSRIRRLMPK 

       370        380        390        400        410        420 
LKERARTLVD LAESARFVIE RPSGPKDAKA AALLSDEARG WLRALLPQLQ ATDFSAAAVD 

       430        440        450        460        470 
QALRAFAEEH GLKLGQIAQP LRVALTGGTT SPPIDATLEA LGASEVTSRI EAV 

« Hide

References

[1]"Genome sequence analysis of the emerging human pathogenic acetic acid bacterium Granulibacter bethesdensis."
Greenberg D.E., Porcella S.F., Zelazny A.M., Virtaneva K., Sturdevant D.E., Kupko J.J. III, Barbian K.D., Babar A., Dorward D.W., Holland S.M.
J. Bacteriol. 189:8727-8736(2007) [PubMed: 17827295] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC BAA-1260 / CGDNIH1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000394 Genomic DNA. Translation: ABI61712.1.
RefSeqYP_744635.1. NC_008343.1.

3D structure databases

ProteinModelPortalQ0BTZ0.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ0BTZ0.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID4275090.
GenomeReviewsGene locus GbCGDNIH1_0814 in contig CP000394_GR.
KEGGgbe:GbCGDNIH1_0814.
NMPDRfig|391165.8.peg.819.
PATRIC22077735. VBIGraBet83793_0850.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0008.
HOGENOMHBG628189.
OMAMAHIPLI.
PhylomeDBQ0BTZ0.
ProtClustDBPRK01406.

Enzyme and pathway databases

BioCycGBET391165:GBCGDNIH1_0814-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_GRABC
AccessionPrimary (citable) accession number: Q0BTZ0
Entry history
Integrated into UniProtKB/Swiss-Prot: April 29, 2008
Last sequence update: October 17, 2006
Last modified: January 25, 2012
This is version 44 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