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Q97KC9 (SYE_CLOAB) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 79. 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:CA_C0990
OrganismClostridium acetobutylicum (strain ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787) [Reference proteome] [HAMAP]
Taxonomic identifier272562 [NCBI]
Taxonomic lineageBacteriaFirmicutesClostridiaClostridialesClostridiaceaeClostridium

Protein attributes

Sequence length485 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
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 – 485485Glutamate--tRNA ligase HAMAP-Rule MF_00022
PRO_0000119544

Regions

Motif12 – 2211"HIGH" region HAMAP-Rule MF_00022
Motif253 – 2575"KMSKS" region HAMAP-Rule MF_00022

Sites

Binding site2561ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
Q97KC9 [UniParc].

Last modified October 1, 2001. Version 1.
Checksum: B7D08618F9A25697

FASTA48555,471
        10         20         30         40         50         60 
MAANEIRTRF APSPTGYMHI GNLRTALYTY LIAKHEDGKF ILRIEDTDQE RYVEDALAVI 

        70         80         90        100        110        120 
YKTLEMTGLK HDEGPDVGGP VGPYVQSERK GLYLDYAKKL VEKGEAYYCF CSKERLDILK 

       130        140        150        160        170        180 
TNSEALKRPF KYDKHCANLS KEEVQEKLDA GVPYVIRQNN PTTGSTTFDD VIYGRISVDN 

       190        200        210        220        230        240 
SELDDMILIK SDGYPTYNFA NVVDDHLMGI THVVRGNEYL SSAPKYNRLY EAFGWNVPIY 

       250        260        270        280        290        300 
VHCPPIMKDA HSKLSKRNGD ASFQDLIEKG YLKEAVLNYI ALLGWNPEGT NEILSLEDMV 

       310        320        330        340        350        360 
KLFDYTHINK SPAVFDPVKL KWMNGEYVRK LSLDEFHKAA LSYYDGVITK ENIDLKKISE 

       370        380        390        400        410        420 
LIQTRVEIFS DIPEMVDFFN ELPDYDIEMY THKKMKTNPE ISLDSLKNCL PVIENIEDWN 

       430        440        450        460        470        480 
LDNIQNTIMN YIKDLGVKNG VVLWPLRTAL SGKKFTPGGA FEIADIIGKD ESIRRIKIGI 


EKLEK 

« Hide

References

[1]"Genome sequence and comparative analysis of the solvent-producing bacterium Clostridium acetobutylicum."
Noelling J., Breton G., Omelchenko M.V., Makarova K.S., Zeng Q., Gibson R., Lee H.M., Dubois J., Qiu D., Hitti J., Wolf Y.I., Tatusov R.L., Sabathe F., Doucette-Stamm L.A., Soucaille P., Daly M.J., Bennett G.N., Koonin E.V., Smith D.R.
J. Bacteriol. 183:4823-4838(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE001437 Genomic DNA. Translation: AAK78966.1.
PIRC97022.
RefSeqNP_347626.1. NC_003030.1.

3D structure databases

ProteinModelPortalQ97KC9.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING272562.CA_C0990.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAK78966; AAK78966; CA_C0990.
GeneID1117173.
KEGGcac:CA_C0990.
PATRIC32036367. VBICloAce74127_1199.

Phylogenomic databases

eggNOGCOG0008.
HOGENOMHOG000252720.
KOK01885.
OMAWINGYYL.
OrthoDBEOG6DRPF7.

Enzyme and pathway databases

BioCycCACE272562:GJIH-1037-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.
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_CLOAB
AccessionPrimary (citable) accession number: Q97KC9
Entry history
Integrated into UniProtKB/Swiss-Prot: April 30, 2003
Last sequence update: October 1, 2001
Last modified: May 14, 2014
This is version 79 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