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B2KAV3 (SYE_ELUMP) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 28. 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 lineageBacteriaElusimicrobiaElusimicrobia (class)ElusimicrobialesElusimicrobiaceaeElusimicrobium

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 MF_00022_B

Catalytic activity

ATP + L-glutamate + tRNA(Glu) = AMP + diphosphate + L-glutamyl-tRNA(Glu). HAMAP MF_00022_B

Cofactor

Binds 1 zinc ion per subunit By similarity. HAMAP MF_00022_B

Subunit structure

Monomer By similarity. HAMAP MF_00022_B

Subcellular location

Cytoplasm By similarity HAMAP MF_00022_B.

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: 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

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 488488Glutamate--tRNA ligase HAMAP MF_00022_B
PRO_0000367667

Regions

Motif9 – 1911"HIGH" region HAMAP MF_00022_B
Motif256 – 2605"KMSKS" region HAMAP MF_00022_B

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: 19270133] [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...

Protein-protein interaction databases

STRINGB2KAV3.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID6263768.
GenomeReviewsGene locus Emin_0083 in contig CP001055_GR.
KEGGemi:Emin_0083.
PATRIC21847252. VBIEluMin86178_0085.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHBG628189.
OMADKETAND.

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 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: January 25, 2012
This is version 28 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