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Q8NQX9 (SYE_CORGL) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 80. 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
Synonyms:gltS
Ordered Locus Names:Cgl1293, cg1463
OrganismCorynebacterium glutamicum (strain ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025) [Reference proteome] [HAMAP]
Taxonomic identifier196627 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesCorynebacterineaeCorynebacteriaceaeCorynebacterium

Protein attributes

Sequence length493 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.

Sequence caution

The sequence CAF19995.1 differs from that shown. Reason: Erroneous initiation.

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 – 493493Glutamate--tRNA ligase HAMAP-Rule MF_00022
PRO_0000119549

Regions

Motif10 – 2011"HIGH" region HAMAP-Rule MF_00022
Motif254 – 2585"KMSKS" region HAMAP-Rule MF_00022

Sites

Binding site2571ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
Q8NQX9 [UniParc].

Last modified April 30, 2003. Version 2.
Checksum: 38EB2B2CE1BC5A14

FASTA49355,391
        10         20         30         40         50         60 
MTDVRVRFCP SPTGTPHVGL VRTALFNWAY ARHTGGKLVF RIEDTDAARD SEESYSAIID 

        70         80         90        100        110        120 
SLRWLGMDWD EGVEKGGPHE PYRQSQRKDI YQDVLKQLID AGEVYPAYST AEEVEERHKA 

       130        140        150        160        170        180 
AGRDPKLGYD NFDRDLTEEQ VAAFEAEGRK PVWRLRMPEQ DWKWTDLVRG EVEFKSFTQP 

       190        200        210        220        230        240 
DFVVARSNGE PLYTLVNPVD DALMEVTHVL RGEDLLPSTP RQLALYEALK RIGVAKATPA 

       250        260        270        280        290        300 
FGHLPFVMGE GNKKLSKRDP QSSLFNHRDN GIIPEGMLNY LALLGWSLSA DQDIFGVDEL 

       310        320        330        340        350        360 
IANFDVADVL GNPARFDQKK LEAINADHIR LLEPKDFEAR LRAYMTEYTE FPADYPAEKF 

       370        380        390        400        410        420 
AIAAELVQTR IKVLSEAWDL LKFLVTADED LVFNEKAAKK NLKETAVEPL NAGIAALEAV 

       430        440        450        460        470        480 
EEWTTPNIEA ALNKALIEDL GLKPRVAFGA LRIGISGEAV SPPLFESMEL LGKESTLVRL 

       490 
KVTREQTPFV VAE 

« Hide

References

[1]"The Corynebacterium glutamicum genome: features and impacts on biotechnological processes."
Ikeda M., Nakagawa S.
Appl. Microbiol. Biotechnol. 62:99-109(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025.
[2]"The complete Corynebacterium glutamicum ATCC 13032 genome sequence and its impact on the production of L-aspartate-derived amino acids and vitamins."
Kalinowski J., Bathe B., Bartels D., Bischoff N., Bott M., Burkovski A., Dusch N., Eggeling L., Eikmanns B.J., Gaigalat L., Goesmann A., Hartmann M., Huthmacher K., Kraemer R., Linke B., McHardy A.C., Meyer F., Moeckel B. expand/collapse author list , Pfefferle W., Puehler A., Rey D.A., Rueckert C., Rupp O., Sahm H., Wendisch V.F., Wiegraebe I., Tauch A.
J. Biotechnol. 104:5-25(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BA000036 Genomic DNA. Translation: BAB98686.1.
BX927151 Genomic DNA. Translation: CAF19995.1. Different initiation.
RefSeqNP_600515.1. NC_003450.3.
YP_225581.1. NC_006958.1.

3D structure databases

ProteinModelPortalQ8NQX9.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING196627.cg1463.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaBAB98686; BAB98686; BAB98686.
CAF19995; CAF19995; cg1463.
GeneID1019274.
KEGGcgb:cg1463.
cgl:NCgl1244.
PATRIC21494628. VBICorGlu203724_1270.

Phylogenomic databases

eggNOGCOG0008.
KOK01885.
OMAPEGMLNY.
OrthoDBEOG6DRPF7.

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_CORGL
AccessionPrimary (citable) accession number: Q8NQX9
Entry history
Integrated into UniProtKB/Swiss-Prot: March 25, 2003
Last sequence update: April 30, 2003
Last modified: July 9, 2014
This is version 80 of the entry and version 2 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