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B3EMG1 (SYE_CHLPB) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 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:Cphamn1_1989
OrganismChlorobium phaeobacteroides (strain BS1) [Complete proteome] [HAMAP]
Taxonomic identifier331678 [NCBI]
Taxonomic lineageBacteriaChlorobiChlorobiaChlorobialesChlorobiaceaeChlorobium/Pelodictyon groupChlorobium

Protein attributes

Sequence length503 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 – 503503Glutamate--tRNA ligase HAMAP-Rule MF_00022
PRO_0000367646

Regions

Motif15 – 2511"HIGH" region HAMAP-Rule MF_00022
Motif262 – 2665"KMSKS" region HAMAP-Rule MF_00022

Sites

Binding site2651ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
B3EMG1 [UniParc].

Last modified July 22, 2008. Version 1.
Checksum: 42327C3C8C9CD6F3

FASTA50357,362
        10         20         30         40         50         60 
MQATPGQRVR TRFAPSPTGH LHVGGLRTAL YNYLYAKSMG GDFIVRIEDT DQARKVEGAE 

        70         80         90        100        110        120 
RSLLNTLEVT GIVPDESFIH GGNFGPYVQS ERLGIYSKYC EQLLEQKQAY YCFSTAEELE 

       130        140        150        160        170        180 
ANRKLQMKQG MQPKYDRKWL PEEMGGNMPE SEIRRKREEG APFVVRMKVP DYISIMFEDM 

       190        200        210        220        230        240 
IRGPIEFDSA TVDDQVLMKS DGFPTYHFAS IIDDHLMEIS HVIRGEEWLS SMPKHILLYE 

       250        260        270        280        290        300 
FFGWEPPKVA HLPLLLNPDR SKLSKRQGDV AAEDFISKGY SPEAIINFVA LLGWNEGEGC 

       310        320        330        340        350        360 
EREVYSLDEL KDKFTLRRVG KAGAVFNVEK LGWLEKQYIK ARPASEIISA IKPLLQAELA 

       370        380        390        400        410        420 
KKETGMDADR LVSDDYLGQV IELMRERVNF EHEFISFSRY FYFDPEEFDE KAVAKRWVDD 

       430        440        450        460        470        480 
TNEVLGEFIE VLENTADFSA DNIEAALKAF VAPREKKPAF LIHPVRILTS GVGFGPSLYH 

       490        500 
MLEVLGKETV IRRLRKGIGV VGK 

« Hide

References

[1]"Complete sequence of Chlorobium phaeobacteroides BS1."
US DOE Joint Genome Institute
Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H., Bruce D., Goodwin L., Pitluck S., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Ovchinnikova G., Li T., Liu Z., Zhao F. expand/collapse author list , Overmann J., Bryant D.A., Richardson P.
Submitted (JUN-2008) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: BS1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP001101 Genomic DNA. Translation: ACE04900.1.
RefSeqYP_001960381.1. NC_010831.1.

3D structure databases

ProteinModelPortalB3EMG1.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING331678.Cphamn1_1989.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACE04900; ACE04900; Cphamn1_1989.
GeneID6375682.
KEGGcpb:Cphamn1_1989.
PATRIC21386360. VBIChlPha121022_2163.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0008.
HOGENOMHOG000252720.
KOK01885.
OMAWLPEEMG.
OrthoDBEOG6DRPF7.

Enzyme and pathway databases

BioCycCPHA331678:GHME-2040-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_CHLPB
AccessionPrimary (citable) accession number: B3EMG1
Entry history
Integrated into UniProtKB/Swiss-Prot: March 24, 2009
Last sequence update: July 22, 2008
Last modified: May 14, 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