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A8F960 (SYE_BACP2) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 49. 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:BPUM_0077
OrganismBacillus pumilus (strain SAFR-032) [Complete proteome] [HAMAP]
Taxonomic identifier315750 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus

Protein attributes

Sequence length483 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

Cofactor

Binds 1 zinc ion per subunit By similarity. 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.

Ontologies

Keywords
   Biological processProtein biosynthesis
   Cellular componentCytoplasm
   LigandATP-binding
Metal-binding
Nucleotide-binding
Zinc
   Molecular functionAminoacyl-tRNA synthetase
Ligase
   Technical termComplete 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

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

tRNA binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 483483Glutamate--tRNA ligase HAMAP-Rule MF_00022
PRO_1000057191

Regions

Motif11 – 2111"HIGH" region HAMAP-Rule MF_00022
Motif252 – 2565"KMSKS" region HAMAP-Rule MF_00022

Sites

Metal binding1081Zinc By similarity
Metal binding1101Zinc By similarity
Metal binding1351Zinc By similarity
Metal binding1371Zinc By similarity
Binding site2551ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
A8F960 [UniParc].

Last modified November 13, 2007. Version 1.
Checksum: A26ED8A92D61532A

FASTA48355,586
        10         20         30         40         50         60 
MGNEVRVRYA PSPTGHLHIG NARTALFNYL FARSQGGKFI IRIEDTDQKR NVEGGEESQL 

        70         80         90        100        110        120 
RHLQWLGIDW DESIDKDGGY GPYRQSERND IYKKYYDELL EKDLAYKCYC TAEELEEERE 

       130        140        150        160        170        180 
AQIARSEMPR YSGKCSHLSK EEEDKLIAEG REPSIRFRVP KGEIIKFDDM VKGEISFETD 

       190        200        210        220        230        240 
GIGDFVIVKK DGTPTYNFAV AVDDHLMKMT HILRGEDHIS NTPKQIMIFN AFGWDVPLFG 

       250        260        270        280        290        300 
HMTLIVNENR KKLSKRDESI IQFIEQYKNL GYLPEALFNF IALLGWSPVG EEELFTKEQF 

       310        320        330        340        350        360 
IDIFDVNRLS KSPALFDMHK LKWVNNQYVK ALDLDQVVAL TLPHLQKAGK VSEQLSDEKN 

       370        380        390        400        410        420 
TWVRKLIALY HEQLSYGAEI VELTELFFKE QIEYNQEAKE VLAEEQVPEV MASFAGQLER 

       430        440        450        460        470        480 
LESFTPDEIK AAIKAVQKET GHKGKKLFMP IRVAVTGQTH GPELPQSIEL LGKETVLNRI 


KQI 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000813 Genomic DNA. Translation: ABV60777.1.
RefSeqYP_001485337.1. NC_009848.1.

3D structure databases

ProteinModelPortalA8F960.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING315750.BPUM_0077.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABV60777; ABV60777; BPUM_0077.
GeneID5619295.
KEGGbpu:BPUM_0077.
PATRIC18963873. VBIBacPum16546_0081.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0008.
HOGENOMHOG000252720.
KOK09698.
OMAVTGQTHG.
OrthoDBEOG6DRPF7.

Enzyme and pathway databases

BioCycBPUM315750:GH6N-85-MONOMER.

Family and domain databases

Gene3D1.10.10.350. 1 hit.
1.10.1160.10. 1 hit.
3.40.50.620. 2 hits.
HAMAPMF_00022_B. Glu_tRNA_synth_B.
InterProIPR008925. aa-tRNA-synth_I_codon-bd.
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_BACP2
AccessionPrimary (citable) accession number: A8F960
Entry history
Integrated into UniProtKB/Swiss-Prot: February 5, 2008
Last sequence update: November 13, 2007
Last modified: May 14, 2014
This is version 49 of the entry and version 1 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