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A7H9S6 (SYE_ANADF) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 50. 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:Anae109_1264
OrganismAnaeromyxobacter sp. (strain Fw109-5) [Complete proteome] [HAMAP]
Taxonomic identifier404589 [NCBI]
Taxonomic lineageBacteriaProteobacteriaDeltaproteobacteriaMyxococcalesCystobacterineaeMyxococcaceaeAnaeromyxobacter

Protein attributes

Sequence length471 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 – 471471Glutamate--tRNA ligase HAMAP-Rule MF_00022
PRO_1000001870

Regions

Motif10 – 2011"HIGH" region HAMAP-Rule MF_00022
Motif244 – 2485"KMSKS" region HAMAP-Rule MF_00022

Sites

Metal binding1071Zinc By similarity
Metal binding1091Zinc By similarity
Metal binding1341Zinc By similarity
Metal binding1361Zinc By similarity
Binding site2471ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
A7H9S6 [UniParc].

Last modified September 11, 2007. Version 1.
Checksum: 3D835E21C7030832

FASTA47153,010
        10         20         30         40         50         60 
MDKPRVRFAP SPTGYLHIGG ARTALFNWLW ARRNGGTFVL RIEDTDRERS TQAAVDAIFD 

        70         80         90        100        110        120 
GLRWLGLDWD EGPDVGGPHG PYFQTQRLEI YKTHAEKLIR EGKAYACYCT KDVLDAQRKQ 

       130        140        150        160        170        180 
AEAEKRQFRY PGTCRELPYD PSRPHVIRFR VPQTGSKTFV DLVKGPIETP YEVLQDEVIL 

       190        200        210        220        230        240 
RGDGVPLYNF GAVVDDVTMA INLVARGDDH VNNTARQILM YEALGYPAPR FAHLPMILGA 

       250        260        270        280        290        300 
DKTRLSKRHG ATSVTAYRDM GYLPEAVVNY LVRLGWSHGD QELFTRDELV RFFDFKDVGA 

       310        320        330        340        350        360 
TAGVFNQDKM AWVNHEWLKK LSDEELARRA LPYFQAAGLP AADDAKLRHV CAVARERART 

       370        380        390        400        410        420 
FGEYVQQFRY FYAPVQLDPK AKDKFLTQDT RPILEAIRAG IAALEALETA ALEKLFHDEA 

       430        440        450        460        470 
AKRGLGLGKV AQPVRVALTG GTASPGMYDV LQILGKDEAL RRLDDALRII G 

« Hide

References

[1]"Complete sequence of Anaeromyxobacter sp. Fw109-5."
US DOE Joint Genome Institute
Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E., Tice H., Pitluck S., Sims D., Brettin T., Bruce D., Detter J.C., Han C., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N. expand/collapse author list , Lykidis A., Fields M., Richardson P.
Submitted (JUL-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Fw109-5.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000769 Genomic DNA. Translation: ABS25472.1.
RefSeqYP_001378456.1. NC_009675.1.

3D structure databases

ProteinModelPortalA7H9S6.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING404589.Anae109_1264.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABS25472; ABS25472; Anae109_1264.
GeneID5376489.
KEGGafw:Anae109_1264.
PATRIC20927691. VBIAnaSp113478_1325.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0008.
HOGENOMHOG000252722.
KOK01885.
OMAAMGWEVP.
OrthoDBEOG6DRPF7.
ProtClustDBPRK01406.

Enzyme and pathway databases

BioCycASP404589:GHMT-1273-MONOMER.

Family and domain databases

Gene3D1.10.10.350. 1 hit.
1.10.1160.10. 1 hit.
1.10.8.70. 1 hit.
3.40.50.620. 2 hits.
HAMAPMF_00022_B. Glu_tRNA_synth_B.
InterProIPR008925. aa-tRNA-synth_I_codon-bd.
IPR020752. aa-tRNA-synth_I_codon-bd_sub1.
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_ANADF
AccessionPrimary (citable) accession number: A7H9S6
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: September 11, 2007
Last modified: February 19, 2014
This is version 50 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