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B6YQF6 (SYE_AZOPC) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 36. 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:CFPG_165
OrganismAzobacteroides pseudotrichonymphae genomovar. CFP2 [Complete proteome] [HAMAP]
Taxonomic identifier511995 [NCBI]
Taxonomic lineageBacteriaBacteroidetesBacteroidiaBacteroidalesCandidatus Azobacteroides

Protein attributes

Sequence length494 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

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
Nucleotide-binding
   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

tRNA binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 494494Glutamate--tRNA ligase HAMAP-Rule MF_00022
PRO_0000367610

Regions

Motif9 – 1911"HIGH" region HAMAP-Rule MF_00022
Motif249 – 2535"KMSKS" region HAMAP-Rule MF_00022

Sites

Binding site2521ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
B6YQF6 [UniParc].

Last modified January 20, 2009. Version 1.
Checksum: 184337FC486F2046

FASTA49457,262
        10         20         30         40         50         60 
MKARVRFAPS PTGPLHIGSI RTALYNYLFA KKYHGDFILR IEDTDSTRFI PGAEEYIIET 

        70         80         90        100        110        120 
FKWLGITFDE GPYRQSERKA IYKEYVDELL NKNLAYIAFD TPEELEAKRR NIPNFQYDAI 

       130        140        150        160        170        180 
TRMTMNNSLT LSKEETKKRI ANSNQYVVRI KIDPNQTIIV NDLIRGEMSI SSSTLDDKVL 

       190        200        210        220        230        240 
YKSSDNLPTY HLANIVDDHL MKITHVIRGE EWLSSTPLHI ILYQYFGWGE KMPVFAHLPL 

       250        260        270        280        290        300 
LLKPDGKGKL SKRDGERFGF PIFPLQWTDS KTGKSISGYR EDGYLPEALI NFLALLGWNP 

       310        320        330        340        350        360 
GSEQEFFSID ELSVLFSLKK CSKNGAKFDY KKVEWFNHQY IQKKSDKEIA ELFFHFYSKK 

       370        380        390        400        410        420 
LEKQDFKKIT EVIGMVKGRI SSIRDLWYET AFFFVAPNTY DEKIVQKRWR AESPIQLTEL 

       430        440        450        460        470        480 
SELLATITNF SLQIVEKTIR GWINNKGYHP SNIMNACRLA LVGTAKGPGI FHIIEILGKE 

       490 
EVIIRIKKAI QVLR 

« Hide

References

[1]"Genome of an endosymbiont coupling N2 fixation to cellulolysis within RT protist cells in termite gut."
Hongoh Y., Sharma V.K., Prakash T., Noda S., Toh H., Taylor T.D., Kudo T., Sakaki Y., Toyoda A., Hattori M., Ohkuma M.
Science 322:1108-1109(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AP010656 Genomic DNA. Translation: BAG83428.1.
RefSeqYP_002308839.1. NC_011565.1.

3D structure databases

ProteinModelPortalB6YQF6.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING511995.CFPG_165.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaBAG83428; BAG83428; CFPG_165.
GeneID7039900.
KEGGaps:CFPG_165.
PATRIC31961881. VBICanAzo57536_0321.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0008.
HOGENOMHOG000252720.
KOK01885.
OMAEIFDMEY.
OrthoDBEOG6DRPF7.
ProtClustDBPRK01406.

Enzyme and pathway databases

BioCycCAZO511995:GKF1-176-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.
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.
ProtoNetSearch...

Entry information

Entry nameSYE_AZOPC
AccessionPrimary (citable) accession number: B6YQF6
Entry history
Integrated into UniProtKB/Swiss-Prot: March 24, 2009
Last sequence update: January 20, 2009
Last modified: February 19, 2014
This is version 36 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