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B1JF83 (SYI_PSEPW) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 47. 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:
Isoleucine--tRNA ligase

EC=6.1.1.5
Alternative name(s):
Isoleucyl-tRNA synthetase
Short name=IleRS
Gene names
Name:ileS
Ordered Locus Names:PputW619_4559
OrganismPseudomonas putida (strain W619) [Complete proteome] [HAMAP]
Taxonomic identifier390235 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesPseudomonadaceaePseudomonas

Protein attributes

Sequence length943 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Catalyzes the attachment of isoleucine to tRNA(Ile). As IleRS can inadvertently accommodate and process structurally similar amino acids such as valine, to avoid such errors it has two additional distinct tRNA(Ile)-dependent editing activities. One activity is designated as 'pretransfer' editing and involves the hydrolysis of activated Val-AMP. The other activity is designated 'posttransfer' editing and involves deacylation of mischarged Val-tRNA(Ile) By similarity. HAMAP-Rule MF_02002

Catalytic activity

ATP + L-isoleucine + tRNA(Ile) = AMP + diphosphate + L-isoleucyl-tRNA(Ile). HAMAP-Rule MF_02002

Cofactor

Binds 1 zinc ion per subunit By similarity. HAMAP-Rule MF_02002

Subunit structure

Monomer By similarity. HAMAP-Rule MF_02002

Subcellular location

Cytoplasm By similarity HAMAP-Rule MF_02002.

Domain

IleRS has two distinct active sites: one for aminoacylation and one for editing. The misactivated valine is translocated from the active site to the editing site, which sterically excludes the correctly activated isoleucine. The single editing site contains two valyl binding pockets, one specific for each substrate (Val-AMP or Val-tRNA(Ile)) By similarity. HAMAP-Rule MF_02002

Sequence similarities

Belongs to the class-I aminoacyl-tRNA synthetase family. IleS type 1 subfamily.

Ontologies

Keywords
   Biological processProtein biosynthesis
   Cellular componentCytoplasm
   LigandATP-binding
Metal-binding
Nucleotide-binding
Zinc
   Molecular functionAminoacyl-tRNA synthetase
Ligase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological_processisoleucyl-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

aminoacyl-tRNA editing activity

Inferred from electronic annotation. Source: InterPro

isoleucine-tRNA ligase activity

Inferred from electronic annotation. Source: UniProtKB-HAMAP

zinc ion binding

Inferred from electronic annotation. Source: UniProtKB-HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 943943Isoleucine--tRNA ligase HAMAP-Rule MF_02002
PRO_1000189189

Regions

Motif58 – 6811"HIGH" region HAMAP-Rule MF_02002
Motif608 – 6125"KMSKS" region HAMAP-Rule MF_02002

Sites

Metal binding9061Zinc By similarity
Metal binding9091Zinc By similarity
Metal binding9261Zinc By similarity
Metal binding9291Zinc By similarity
Binding site5671Aminoacyl-adenylate By similarity
Binding site6111ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
B1JF83 [UniParc].

Last modified April 29, 2008. Version 1.
Checksum: 32EE8EB6B6946E6F

FASTA943105,817
        10         20         30         40         50         60 
MTDYKATLNL PDTAFPMKAG LPQREPQILQ RWDSIGLYQK LREIGKDRPK FVLHDGPPYA 

        70         80         90        100        110        120 
NGKIHIGHAL NKILKDMIVR SKTLSGFDAP YVPGWDCHGL PIEHKVEVTH GKHLTADRTR 

       130        140        150        160        170        180 
ELCREYAAEQ IEGQKTEFIR LGVLGDWDNP YKTMNFANEA GEIRALAEMV KQGFVFKGLK 

       190        200        210        220        230        240 
PVNWCFDCGS ALAEAEVEYA DKKSQTIDVA FPVADADKLA AAFGLPALAK PAAIVIWTTT 

       250        260        270        280        290        300 
PWTIPANQAL NIHPEFKYAL VDTGERLLVL AEELVESCLK RYNLEGSVIA TAQGSALELV 

       310        320        330        340        350        360 
NFRHPFYDRL SPVYLADYVE LGAGTGVVHS APAYGEDDFV TCKRYGMVND DILTPVQSNG 

       370        380        390        400        410        420 
VYVESLEFFG GQFIWKANPA IVEKLSEVGA LMHTETISHS YMHCWRHKTP LIYRATAQWF 

       430        440        450        460        470        480 
VGMDKQPSTG EPLRERALKA IEDTQFVPAW GQARLHSMIA NRPDWCISRQ RNWGVPIPFF 

       490        500        510        520        530        540 
LHKQTGELHP RTVELMEAVA KRVEQEGIEA WFKLDAAELL GDEAGQYDKI TDTLDVWFDS 

       550        560        570        580        590        600 
GTTHWHVLRG SHDIGHATGP RADLYLEGSD QHRGWFHSSL LTGCAIDNHA PYRELLTHGF 

       610        620        630        640        650        660 
TVDESGRKMS KSLGNTIEPE KVNNTLGADI LRLWVSATDY SGEMAVSEQI LQRSADAYRR 

       670        680        690        700        710        720 
IRNTARFLLS NLSGFDPARD LLAPEDMLAL DRWAVDRTLL LQRELEEHYS EYRFWNVYSK 

       730        740        750        760        770        780 
IHNFCVQELG GFYLDIIKDR QYTTGANSVA RRSCQTALYH ISEALVRWIA PILAFTADEI 

       790        800        810        820        830        840 
WQYLPGERNE SVMLNGWYQG LSELPEGTEL DRAYWDRVMA VKAAVNKELE NQRTAKVIGG 

       850        860        870        880        890        900 
NLQAEVTLFA EEGLSADLSK LGDELRFVLI TSAASVVPFA QAPADAVATE VEGLKLKVVK 

       910        920        930        940 
SGHAKCGRCW HFRADVGSHP EHPEICSRCV DNLSGSGEVR HYA 

« Hide

References

[1]"Complete sequence of Pseudomonas putida W619."
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Dalin E., Tice H., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N. expand/collapse author list , Kim E., Taghavi S., Vangronsveld D., van der Lelie D., Richardson P.
Submitted (FEB-2008) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: W619.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000949 Genomic DNA. Translation: ACA75039.1.
RefSeqYP_001751408.1. NC_010501.1.

3D structure databases

ProteinModelPortalB1JF83.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING390235.PputW619_4559.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACA75039; ACA75039; PputW619_4559.
GeneID6113535.
KEGGppw:PputW619_4559.
PATRIC19959029. VBIPsePut93764_4585.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0060.
HOGENOMHOG000246402.
KOK01870.
OMAKPVHWCL.
OrthoDBEOG644ZM1.

Enzyme and pathway databases

BioCycPPUT390235:GHHJ-4628-MONOMER.

Family and domain databases

Gene3D1.10.730.10. 1 hit.
3.40.50.620. 2 hits.
3.90.740.10. 1 hit.
HAMAPMF_02002. Ile_tRNA_synth_type1.
InterProIPR001412. aa-tRNA-synth_I_CS.
IPR002300. aa-tRNA-synth_Ia.
IPR002301. Ile-tRNA-ligase.
IPR023585. Ile-tRNA-ligase_type1.
IPR014729. Rossmann-like_a/b/a_fold.
IPR009080. tRNAsynth_1a_anticodon-bd.
IPR013155. V/L/I-tRNA-synth_anticodon-bd.
IPR009008. Val/Leu/Ile-tRNA-synth_edit.
IPR010663. Znf_DNA_glyclase/IsotRNA_synth.
[Graphical view]
PANTHERPTHR11946:SF9. PTHR11946:SF9. 1 hit.
PfamPF08264. Anticodon_1. 1 hit.
PF00133. tRNA-synt_1. 1 hit.
PF06827. zf-FPG_IleRS. 1 hit.
[Graphical view]
PRINTSPR00984. TRNASYNTHILE.
SUPFAMSSF47323. SSF47323. 1 hit.
SSF50677. SSF50677. 1 hit.
TIGRFAMsTIGR00392. ileS. 1 hit.
PROSITEPS00178. AA_TRNA_LIGASE_I. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameSYI_PSEPW
AccessionPrimary (citable) accession number: B1JF83
Entry history
Integrated into UniProtKB/Swiss-Prot: July 28, 2009
Last sequence update: April 29, 2008
Last modified: May 14, 2014
This is version 47 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