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Q9XCL6 (SYE_PSEAE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 95. 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:PA3134
OrganismPseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228) [Reference proteome] [HAMAP]
Taxonomic identifier208964 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesPseudomonadaceaePseudomonas

Protein attributes

Sequence length494 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

Cofactor

Binds 1 zinc ion per subunit By similarity. 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
Metal-binding
Nucleotide-binding
Zinc
   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

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

tRNA binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 494494Glutamate--tRNA ligase HAMAP-Rule MF_00022
PRO_0000119627

Regions

Motif10 – 2011"HIGH" region HAMAP-Rule MF_00022
Motif251 – 2555"KMSKS" region HAMAP-Rule MF_00022

Sites

Metal binding1071Zinc By similarity
Metal binding1091Zinc By similarity
Metal binding1341Zinc By similarity
Metal binding1361Zinc By similarity
Binding site2541ATP By similarity

Experimental info

Sequence conflict931K → R in AAD33773. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q9XCL6 [UniParc].

Last modified December 8, 2000. Version 2.
Checksum: EC3EFD97BA5AFD72

FASTA49456,749
        10         20         30         40         50         60 
MTTVRTRIAP SPTGDPHVGT AYIALFNLCF ARQHGGQFIL RIEDTDQLRS TRESEQQIYD 

        70         80         90        100        110        120 
ALRWLGIEWD EGPDVGGPHG PYRQSERGHI YKKYSDELVE KGHAFTCFCT PERLDAVRAE 

       130        140        150        160        170        180 
QMARKETPRY DGHCMHLPKD EVQRRLAAGE SHVTRMKVPT EGVCVVPDML RGDVEIPWDR 

       190        200        210        220        230        240 
MDMQVLMKAD GLPTYFLANV VDDHLMGITH VLRGEEWLPS APKLIKLYEY FGWEQPQLCY 

       250        260        270        280        290        300 
MPLLRNPDKS KLSKRKNPTS ITFYERMGYL PQALLNYLGR MGWSMPDERE KFTLAEMIEH 

       310        320        330        340        350        360 
FDLSRVSLGG PIFDLEKLSW LNGQWIREQS VEEFAREVQK WALNPEYLMK IAPHVQGRVE 

       370        380        390        400        410        420 
NFSQIAPLAG FFFSGGVPLD ASLFEHKKLD PTQVRQVLQL VLWKLESLRQ WEKERITGCI 

       430        440        450        460        470        480 
QAVAEHLQLK LRDVMPLMFP AITGHASSVS VLDAMEILGA DLSRYRLRQA LELLGGASKK 

       490 
ETKEWEKIRD AIPG 

« Hide

References

« Hide 'large scale' references
[1]"Cloning of the glutamyl-tRNA synthetase (gltX) gene from Pseudomonas aeruginosa."
Franklund C.V., Goldberg J.B.
J. Bacteriol. 181:3582-3586(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: PAK.
[2]"Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic pathogen."
Stover C.K., Pham X.-Q.T., Erwin A.L., Mizoguchi S.D., Warrener P., Hickey M.J., Brinkman F.S.L., Hufnagle W.O., Kowalik D.J., Lagrou M., Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y., Brody L.L., Coulter S.N., Folger K.R. expand/collapse author list , Kas A., Larbig K., Lim R.M., Smith K.A., Spencer D.H., Wong G.K.-S., Wu Z., Paulsen I.T., Reizer J., Saier M.H. Jr., Hancock R.E.W., Lory S., Olson M.V.
Nature 406:959-964(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF139107 Genomic DNA. Translation: AAD33773.1.
AE004091 Genomic DNA. Translation: AAG06522.1.
PIRE83254.
RefSeqNP_251824.1. NC_002516.2.

3D structure databases

ProteinModelPortalQ9XCL6.
SMRQ9XCL6. Positions 4-471.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING208964.PA3134.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAG06522; AAG06522; PA3134.
GeneID882647.
KEGGpae:PA3134.
PATRIC19840849. VBIPseAer58763_3286.

Organism-specific databases

PseudoCAPPA3134.

Phylogenomic databases

eggNOGCOG0008.
HOGENOMHOG000252720.
KOK01885.
OMADSHEHHA.
OrthoDBEOG6DRPF7.
PhylomeDBQ9XCL6.

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_PSEAE
AccessionPrimary (citable) accession number: Q9XCL6
Entry history
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: December 8, 2000
Last modified: July 9, 2014
This is version 95 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