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B2V5H4 (SYE_CLOBA) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 43. 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:CLH_2322
OrganismClostridium botulinum (strain Alaska E43 / Type E3) [Complete proteome] [HAMAP]
Taxonomic identifier508767 [NCBI]
Taxonomic lineageBacteriaFirmicutesClostridiaClostridialesClostridiaceaeClostridium

Protein attributes

Sequence length485 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 – 485485Glutamate--tRNA ligase HAMAP-Rule MF_00022
PRO_0000367648

Regions

Motif12 – 2211"HIGH" region HAMAP-Rule MF_00022
Motif253 – 2575"KMSKS" region HAMAP-Rule MF_00022

Sites

Metal binding1091Zinc By similarity
Metal binding1111Zinc By similarity
Metal binding1361Zinc By similarity
Metal binding1381Zinc By similarity
Binding site2561ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
B2V5H4 [UniParc].

Last modified July 1, 2008. Version 1.
Checksum: 65A3A8694DE15970

FASTA48555,581
        10         20         30         40         50         60 
MASKKIRTRF APSPTGYMHV GNLRTALYAY LIAKHEAGDF ILRIEDTDQE RLVDGAVDII 

        70         80         90        100        110        120 
YNTLKLTGLN HDEGPDVGGN VGPYVQSERK AIYLEYAKNL VEKGEAYYCF CSKDRLDMLK 

       130        140        150        160        170        180 
ENAEALKRPF KYDKHCLHLT KEEIEANLAK GLPYVIRQNN PTTGSTTFDD VIYGKITVDN 

       190        200        210        220        230        240 
SELEDMILIK SDGLPTYNFA NVVDDHLMGI THIVRGNEYL SSSPKYNRLY EAFGWDIPVY 

       250        260        270        280        290        300 
VHCPPIMKDT HNKLSKRNGD ASFEDLMKKG YLKDAVLNYI ALLGWNPGTN EEIFNLEELT 

       310        320        330        340        350        360 
QKFDFKDISK SPAIFDDAKL KWMNGEYIRK LSLDEFHELA VPEYKKVLKK DFDLKFISEL 

       370        380        390        400        410        420 
LHTRCELLSD LAEQIDFLEE LPEYSTDLYV HKKMKSTVES SLENLQKVLP IIEEIDEANW 

       430        440        450        460        470        480 
NKDYIHEKVF ELIKSLEIKN GQMLWPIRTA LSGKSFTPGG AFELAILLGK EESISRLKKG 


IELLK 

« Hide

References

[1]"Complete genome sequence of Clostridium botulinum E3 str. Alaska E43."
Brinkac L.M., Brown J.L., Bruce D., Detter C., Munk C., Smith L.A., Smith T.J., Sutton G., Brettin T.S.
Submitted (MAY-2008) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Alaska E43 / Type E3.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP001078 Genomic DNA. Translation: ACD52707.1.
RefSeqYP_001921703.1. NC_010723.1.

3D structure databases

ProteinModelPortalB2V5H4.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING508767.CLH_2322.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACD52707; ACD52707; CLH_2322.
GeneID6318920.
KEGGcbt:CLH_2322.
PATRIC19420901. VBICloBot115804_2242.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0008.
HOGENOMHOG000252720.
KOK01885.
OMADSHEHHA.
OrthoDBEOG6DRPF7.

Enzyme and pathway databases

BioCycCBOT508767:GHKO-2314-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_CLOBA
AccessionPrimary (citable) accession number: B2V5H4
Entry history
Integrated into UniProtKB/Swiss-Prot: March 24, 2009
Last sequence update: July 1, 2008
Last modified: May 14, 2014
This is version 43 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