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B0KF73 (SYE_PSEPG) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 39. 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:PputGB1_1508
OrganismPseudomonas putida (strain GB-1) [Complete proteome] [HAMAP]
Taxonomic identifier76869 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesPseudomonadaceaePseudomonas

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.

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 – 493493Glutamate--tRNA ligase HAMAP-Rule MF_00022
PRO_1000074327

Regions

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

Sites

Binding site2541ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
B0KF73 [UniParc].

Last modified March 18, 2008. Version 1.
Checksum: E8D871A3B2454862

FASTA49356,481
        10         20         30         40         50         60 
MTTVRTRIAP SPTGDPHVGT AYIALFNYCF AKQHGGEFIL RIEDTDQLRS TRESEQQIFD 

        70         80         90        100        110        120 
ALRWLGIEWN EGPDVGGPHG PYRQSERGDI YAKYAKELVD AGHAFYCFCT AEELEQMRAE 

       130        140        150        160        170        180 
QQARGETPRY DGRALLLSAE EVQRRLDAGE PHVIRMKVPS EGICVVPDML RGDVEIPWDR 

       190        200        210        220        230        240 
MDMQVLMKND GLPTYFLANV VDDHLMGITH VLRGEEWLPS APKLIKLYEY FGWEQPKLCY 

       250        260        270        280        290        300 
MPLLRNPDKS KLSKRKNPTS VTFYERMGFM PEAMLNYLGR MGWSMPDERE KFSLAEMVEH 

       310        320        330        340        350        360 
FDLSRISLGG PIFDIEKLSW LNGQWLRELP VEEFATRLQK WAFNSDYMMK IAPHVQGRVE 

       370        380        390        400        410        420 
TFSQVAPLGG FFFEGALKLD AKLFESKKLS ADQVRQVIQL ILWKLESLRQ WEKERITGCI 

       430        440        450        460        470        480 
QAVVEALELK LRDAMPLMFA AITGQASSVS VLDAMEILGP DLTRYRLRQA LDLLGGVSKK 

       490 
ENKEWEKLLA SIA 

« Hide

References

[1]"Complete sequence of Pseudomonas putida GB-1."
US DOE Joint Genome Institute
Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E., Tice H., Pitluck S., Bruce D., Goodwin L., Chertkov O., Brettin T., Detter J.C., Han C., Kuske C.R., Schmutz J., Larimer F., Land M. expand/collapse author list , Hauser L., Kyrpides N., Kim E., McCarthy J.K., Richardson P.
Submitted (JAN-2008) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: GB-1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000926 Genomic DNA. Translation: ABY97413.1.
RefSeqYP_001667749.1. NC_010322.1.

3D structure databases

ProteinModelPortalB0KF73.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING76869.PputGB1_1508.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABY97413; ABY97413; PputGB1_1508.
GeneID5869278.
KEGGppg:PputGB1_1508.
PATRIC19930021. VBIPsePut76638_1519.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0008.
HOGENOMHOG000252720.
KOK01885.
OMAAFRCFCT.
OrthoDBEOG6DRPF7.
ProtClustDBPRK01406.

Enzyme and pathway databases

BioCycPPUT76869:GIXB-1549-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_PSEPG
AccessionPrimary (citable) accession number: B0KF73
Entry history
Integrated into UniProtKB/Swiss-Prot: May 20, 2008
Last sequence update: March 18, 2008
Last modified: February 19, 2014
This is version 39 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