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B1MDQ5 (SYE_MYCA9) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 48. 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:MAB_3298c
OrganismMycobacterium abscessus (strain ATCC 19977 / DSM 44196) [Complete proteome] [HAMAP]
Taxonomic identifier561007 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesCorynebacterineaeMycobacteriaceaeMycobacteriumMycobacterium abscessus

Protein attributes

Sequence length496 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 – 496496Glutamate--tRNA ligase HAMAP-Rule MF_00022
PRO_1000090091

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
B1MDQ5 [UniParc].

Last modified April 29, 2008. Version 1.
Checksum: F09F0D61315C53DD

FASTA49654,711
        10         20         30         40         50         60 
MSNTKIRVRF CPSPTGTPHV GLIRTALFNW AYARHCGGDF VFRIEDTDAG RDSEESYLAI 

        70         80         90        100        110        120 
LDALRWLGLD WDEGPEVGGP YEPYRQSQRK ELHREVVRKL LEAGEAYEAF STAEEVEARH 

       130        140        150        160        170        180 
LAAGRNPKLG YDNYDRDLTE EQRAAFRAEG RDPVVRLRMP DHDITWNDLV RGETTFAAGV 

       190        200        210        220        230        240 
VPDFALTRGN GDPLYTLVNP VDDALMKITH VLRGEDLLPS TPRQIALYEA MIRIGVTDSI 

       250        260        270        280        290        300 
PAFAHLPSVL GEGTKKLSKR DPQSNLFLHR DRGFIPEGLL NYLALLGWSI ADDHDIFSLA 

       310        320        330        340        350        360 
EMVTAFDVTD VNSNPARFDQ KKADAINAEH IRLLAPEEFV TRLRTYFAAH GHELGLDESA 

       370        380        390        400        410        420 
FAVAADLVQT RIVVLGDAWG LLKFLNDDAY AIDPGAARKE LGEASLPVLD AAIGALESLE 

       430        440        450        460        470        480 
AWTTPAIEGA LKSALIEGLE LKPRKAFGPL RVAVTGATVS PPLFESMELL GSGRTLTRLR 

       490 
NARSWENGVG DQTDSG 

« Hide

References

[1]"Acquisition of foreign virulence genes by the cystic fibrosis pathogen Mycobacterium abscessus."
Genoscope
Ripoll F., Pasek S., Schenowitz C., Dossat C., Barbe V., Rottman M., Heym B., Herrmann J.L., Daffe M., Brosch R., Risler J.L., Gaillard J.L.
Submitted (MAR-2008) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 19977 / DSM 44196.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CU458896 Genomic DNA. Translation: CAM63374.1.
RefSeqYP_001704028.1. NC_010397.1.

3D structure databases

ProteinModelPortalB1MDQ5.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING561007.MAB_3298c.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAM63374; CAM63374; MAB_3298c.
GeneID5967485.
KEGGmab:MAB_3298c.
PATRIC17978370. VBIMycAbs55940_3356.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0008.
HOGENOMHOG000252720.
KOK01885.
OMAPEGMLNY.
OrthoDBEOG6DRPF7.

Enzyme and pathway databases

BioCycMABS36809-WGS:GSQO-3314-MONOMER.
MABS561007:GJTG-3314-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_MYCA9
AccessionPrimary (citable) accession number: B1MDQ5
Entry history
Integrated into UniProtKB/Swiss-Prot: March 24, 2009
Last sequence update: April 29, 2008
Last modified: July 9, 2014
This is version 48 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