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B2KAV3 (SYE_ELUMP) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 41. 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:Emin_0083
OrganismElusimicrobium minutum (strain Pei191) [Complete proteome] [HAMAP]
Taxonomic identifier445932 [NCBI]
Taxonomic lineageBacteriaElusimicrobiaElusimicrobiaElusimicrobialesElusimicrobiaceaeElusimicrobium

Protein attributes

Sequence length488 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 – 488488Glutamate--tRNA ligase HAMAP-Rule MF_00022
PRO_0000367667

Regions

Motif9 – 1911"HIGH" region HAMAP-Rule MF_00022
Motif256 – 2605"KMSKS" region HAMAP-Rule MF_00022

Sites

Metal binding1121Zinc By similarity
Metal binding1141Zinc By similarity
Metal binding1391Zinc By similarity
Metal binding1411Zinc By similarity
Binding site2591ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
B2KAV3 [UniParc].

Last modified June 10, 2008. Version 1.
Checksum: ADF084EAF76A5D6F

FASTA48855,376
        10         20         30         40         50         60 
MKIRVRFAPS PTGFLHIGGV RTALFNYLFA KRYGGTFVLR IEDTDELRST EESTQAIFDG 

        70         80         90        100        110        120 
LEWTKLLWDE GPFRDGKENG PYPPYLQSER VKAGIYQKYI DQLLEEGKAY KCYCTPEELE 

       130        140        150        160        170        180 
AMREEAAAKK LPPRYPGKCK HLTKDEQAAL EAQGRKPVIR FNMPSEGSVE WADLIRGPVS 

       190        200        210        220        230        240 
FASKDLYDLV ISKPSGFPTY NFACVIDDHL MEMSHIIRGE DHISNTPMQI QMYKAFGWTP 

       250        260        270        280        290        300 
PEFGHLPMIH GSDGTKLSKR HGATNVIEYQ KQGYLSEALV NYLALLGWSN SESQQLFAPG 

       310        320        330        340        350        360 
ELEQKFDIKG VQKSPAIFDN AKLDWMNSEY IRATPISKLT DLAIPFIKEE NIDISKTDRA 

       370        380        390        400        410        420 
ALENIIAIEQ EKYRTLKEIP GLIKFFFEDV VFEEGAKEKV YGKPESKDVL LGITRVYQNI 

       430        440        450        460        470        480 
EPFKEADLEA ATRAFAKDNG FKTGQIFHPV RVAVSGRTHG PTLFKMLELL GKETVIKRLN 


EAAKYSNI 

« Hide

References

[1]"Genomic analysis of 'Elusimicrobium minutum,' the first cultivated representative of the phylum 'Elusimicrobia' (formerly termite group 1)."
Herlemann D.P.R., Geissinger O., Ikeda-Ohtsubo W., Kunin V., Sun H., Lapidus A., Hugenholtz P., Brune A.
Appl. Environ. Microbiol. 75:2841-2849(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Pei191.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP001055 Genomic DNA. Translation: ACC97649.1.
RefSeqYP_001874986.1. NC_010644.1.

3D structure databases

ProteinModelPortalB2KAV3.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING445932.Emin_0083.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACC97649; ACC97649; Emin_0083.
GeneID6263768.
KEGGemi:Emin_0083.
PATRIC21847252. VBIEluMin86178_0085.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0008.
HOGENOMHOG000252720.
KOK01885.
OMAAFRCFCT.
OrthoDBEOG6DRPF7.

Enzyme and pathway databases

BioCycEMIN445932:GHM0-84-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_ELUMP
AccessionPrimary (citable) accession number: B2KAV3
Entry history
Integrated into UniProtKB/Swiss-Prot: March 24, 2009
Last sequence update: June 10, 2008
Last modified: February 19, 2014
This is version 41 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