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A0QUY7 (SYE_MYCS2) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 61. 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:MSMEG_2383, MSMEI_2323
OrganismMycobacterium smegmatis (strain ATCC 700084 / mc(2)155) [Reference proteome] [HAMAP]
Taxonomic identifier246196 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesCorynebacterineaeMycobacteriaceaeMycobacterium

Protein attributes

Sequence length486 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

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
Reference 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 – 486486Glutamate--tRNA ligase HAMAP-Rule MF_00022
PRO_0000330980

Regions

Motif12 – 2211"HIGH" region HAMAP-Rule MF_00022
Motif256 – 2605"KMSKS" region HAMAP-Rule MF_00022

Sites

Binding site2591ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
A0QUY7 [UniParc].

Last modified January 9, 2007. Version 1.
Checksum: 4A7B779612605BBC

FASTA48654,019
        10         20         30         40         50         60 
MTTKKVRVRF CPSPTGTPHV GLVRTALFNW AYARHTGGDF VFRIEDTDAA RDSDESYAAI 

        70         80         90        100        110        120 
LDALRWLGMD WDEGPEVGGP YEPYRQSQRR EIYRDVVARL LEAGEVYEAY STPEEVEARH 

       130        140        150        160        170        180 
LAAGRNPKLG YDNYDRDLTD AQRKAFADEG RRPVLRLRMP DEDLSWNDLV RGPTTFAAGS 

       190        200        210        220        230        240 
VPDFAITRSN GDPLYTLVNP VDDALMKITH VLRGEDILPS TPRQIALYRA LMRIGVAEFV 

       250        260        270        280        290        300 
PEFAHLPSVL GEGNKKLSKR DPQSNLFLHR DRGFIPEGLL NYLALLGWGI ADDHDVFSLD 

       310        320        330        340        350        360 
EMVAAFDVAD VNSNPARFDQ KKADAINAEH IRMLAPEDFT ARLREYFVTH GYDTTLDDAA 

       370        380        390        400        410        420 
FAEAAALVQT RVVVLGDAWG LLKFFNDDAY EIDEKSAAKE LKPESAAVLD AALSALEAVG 

       430        440        450        460        470        480 
DWTTPAIEAA LKTALLEGLE LKPRKAFGPI RVAVTGAAVS PPLFESMELL GRDRSLARLR 


AARDRV 

« Hide

References

[1]Fleischmann R.D., Dodson R.J., Haft D.H., Merkel J.S., Nelson W.C., Fraser C.M.
Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 700084 / mc(2)155.
[2]"Interrupted coding sequences in Mycobacterium smegmatis: authentic mutations or sequencing errors?"
Deshayes C., Perrodou E., Gallien S., Euphrasie D., Schaeffer C., Van-Dorsselaer A., Poch O., Lecompte O., Reyrat J.-M.
Genome Biol. 8:R20.1-R20.9(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 700084 / mc(2)155.
[3]"Ortho-proteogenomics: multiple proteomes investigation through orthology and a new MS-based protocol."
Gallien S., Perrodou E., Carapito C., Deshayes C., Reyrat J.-M., Van Dorsselaer A., Poch O., Schaeffer C., Lecompte O.
Genome Res. 19:128-135(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Strain: ATCC 700084 / mc(2)155.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000480 Genomic DNA. Translation: ABK74186.1.
CP001663 Genomic DNA. Translation: AFP38793.1.
RefSeqYP_006567088.1. NC_018289.1.
YP_886725.1. NC_008596.1.

3D structure databases

ProteinModelPortalA0QUY7.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING246196.MSMEG_2383.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABK74186; ABK74186; MSMEG_2383.
AFP38793; AFP38793; MSMEI_2323.
GeneID4533604.
KEGGmsg:MSMEI_2323.
msm:MSMEG_2383.
PATRIC18077190. VBIMycSme59918_2349.

Phylogenomic databases

eggNOGCOG0008.
HOGENOMHOG000252722.
KOK01885.
OMAVTGQTHG.
OrthoDBEOG6DRPF7.

Enzyme and pathway databases

BioCycMSME246196:GJ4Y-2383-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_MYCS2
AccessionPrimary (citable) accession number: A0QUY7
Secondary accession number(s): I7FJ34
Entry history
Integrated into UniProtKB/Swiss-Prot: April 29, 2008
Last sequence update: January 9, 2007
Last modified: July 9, 2014
This is version 61 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