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B4UI79 (SYE_ANASK) 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:AnaeK_1251
OrganismAnaeromyxobacter sp. (strain K) [Complete proteome] [HAMAP]
Taxonomic identifier447217 [NCBI]
Taxonomic lineageBacteriaProteobacteriaDeltaproteobacteriaMyxococcalesCystobacterineaeMyxococcaceaeAnaeromyxobacter

Protein attributes

Sequence length474 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 – 474474Glutamate--tRNA ligase HAMAP-Rule MF_00022
PRO_1000090052

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
B4UI79 [UniParc].

Last modified September 23, 2008. Version 1.
Checksum: EC21C2F7AE95E48F

FASTA47453,038
        10         20         30         40         50         60 
MDKPRVRFAP SPTGYLHIGG ARTALFNWLW ARRNGGTFVL RIEDTDRERS TQLAVDAILD 

        70         80         90        100        110        120 
GLRWLGLDWD EGPGVGGPHP PYFQTERLDL YKAHAERLIR EGKAYACYCT REELDAQRKQ 

       130        140        150        160        170        180 
AEAEKRQFRY PGTCRDKPYD PSRPHVVRFR VPDAGATSWN DLVKGVISTP HDTLQDEVIL 

       190        200        210        220        230        240 
RGDGVPLYNF GAVVDDITME INLVGRGDDH VNNTARQILM YEALGYPVPT FAHFPMILGA 

       250        260        270        280        290        300 
DKARLSKRHG ATSVTAYRDM GFLPEAVVNY LVRLGWSHGD QELFTLDELV RYFDLKDVGA 

       310        320        330        340        350        360 
TAGVFNPEKM AWVNHEWLKR RSPEELAKLA LPHFRAAGLP AEDDEKLRHV CAVARERAKT 

       370        380        390        400        410        420 
LGEYVQQFRY FYAPIALDPK AKAKFLTADT RPVLQAVRDA IAALPALETQ AVEQVFHGEA 

       430        440        450        460        470 
ERRGVGLGKV AQPVRVALTG GTASPGMYDV VQILGKDETL KRLDEALRIA GEPG 

« Hide

References

[1]"Complete sequence of Anaeromyxobacter sp. K."
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., Saunders E., Brettin T., Detter J.C., Han C., Larimer F., Land M., Hauser L., Kyrpides N., Ovchinnikiva G., Beliaev A.
Submitted (AUG-2008) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP001131 Genomic DNA. Translation: ACG72484.1.
RefSeqYP_002133613.1. NC_011145.1.

3D structure databases

ProteinModelPortalB4UI79.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING447217.AnaeK_1251.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACG72484; ACG72484; AnaeK_1251.
GeneID6786195.
KEGGank:AnaeK_1251.
PATRIC20937118. VBIAnaSp90767_1264.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0008.
HOGENOMHOG000252722.
KOK01885.
OMAHCLRASI.
OrthoDBEOG6DRPF7.

Enzyme and pathway databases

BioCycASP447217:GHB0-1268-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_ANASK
AccessionPrimary (citable) accession number: B4UI79
Entry history
Integrated into UniProtKB/Swiss-Prot: March 24, 2009
Last sequence update: September 23, 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