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A4TE16 (SYE_MYCGI) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 56. 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:Mflv_4229
OrganismMycobacterium gilvum (strain PYR-GCK) (Mycobacterium flavescens (strain ATCC 700033 / PYR-GCK)) [Complete proteome] [HAMAP]
Taxonomic identifier350054 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesCorynebacterineaeMycobacteriaceaeMycobacterium

Protein attributes

Sequence length491 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 – 491491Glutamate--tRNA ligase HAMAP-Rule MF_00022
PRO_0000330979

Regions

Motif9 – 1911"HIGH" region HAMAP-Rule MF_00022
Motif253 – 2575"KMSKS" region HAMAP-Rule MF_00022

Sites

Binding site2561ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
A4TE16 [UniParc].

Last modified May 15, 2007. Version 1.
Checksum: E09D2DECBE0E20CA

FASTA49154,453
        10         20         30         40         50         60 
MKVRVRFCPS PTGTPHVGLI RTALFNWAYA RHTGGDFVFR IEDTDAQRDS EESYLALLDA 

        70         80         90        100        110        120 
LRWLGMDWDE GPEVGGPYAP YRQSQRRDLY LDVIRRLLAA GEAYEAFSTA EEVEARHLAA 

       130        140        150        160        170        180 
GRNPKLGYDN FDRDLTEEQR AAFRAEGRQP VVRLRMPDAD MTWVDLVRGE TTFPVGSVPD 

       190        200        210        220        230        240 
FALTRGSGDP LYTLVNPVDD ALMKITHVLR GEDLLPSTPR QLALYAALIR IGVTDMTPQF 

       250        260        270        280        290        300 
AHLPSVLGEG NKKLSKRDPQ SNLFLHRERG FIPEGLLNYL ALLGWSIADD RDIFSVQEMV 

       310        320        330        340        350        360 
AAFDVADVNS NPARFDQKKA DALNAEHIRR LDEAEFVRRL ADYFSTHGYD TGLDDARFAE 

       370        380        390        400        410        420 
AAALVQTRIV VLGDAWDLLK FLDESSFALD EKSAGKELKD TAVPVLTAAL AALKGVGEWT 

       430        440        450        460        470        480 
TAQIEDALKV ALIDGLELKP RKAFGPVRVA VTGSSISPPL FESLELLGRD RSLERLRAGR 

       490 
DHAAAAVTMD A 

« Hide

References

[1]"Complete sequence of chromosome of Mycobacterium gilvum PYR-GCK."
US DOE Joint Genome Institute
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M. expand/collapse author list , Hauser L., Kyrpides N., Mikhailova N., Miller C., Richardson P.
Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: PYR-GCK.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000656 Genomic DNA. Translation: ABP46698.1.
RefSeqYP_001135486.1. NC_009338.1.

3D structure databases

ProteinModelPortalA4TE16.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING350054.Mflv_4229.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABP46698; ABP46698; Mflv_4229.
GeneID4976656.
KEGGmgi:Mflv_4229.
PATRIC18036681. VBIMycGil17082_4309.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0008.
HOGENOMHOG000252720.
KOK01885.
OMAPAHSYLW.
OrthoDBEOG6DRPF7.
ProtClustDBPRK01406.

Enzyme and pathway databases

BioCycMGIL350054:GHK8-4277-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_MYCGI
AccessionPrimary (citable) accession number: A4TE16
Entry history
Integrated into UniProtKB/Swiss-Prot: April 29, 2008
Last sequence update: May 15, 2007
Last modified: February 19, 2014
This is version 56 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