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B2T6I7 (SYI_BURPP) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 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:Bphyt_3159
OrganismBurkholderia phytofirmans (strain DSM 17436 / PsJN) [Complete proteome] [HAMAP]
Taxonomic identifier398527 [NCBI]
Taxonomic lineageBacteriaProteobacteriaBetaproteobacteriaBurkholderialesBurkholderiaceaeBurkholderia

Protein attributes

Sequence length945 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 – 945945Isoleucine--tRNA ligase HAMAP-Rule MF_02002
PRO_1000189140

Regions

Motif66 – 7611"HIGH" region HAMAP-Rule MF_02002
Motif622 – 6265"KMSKS" region HAMAP-Rule MF_02002

Sites

Metal binding9081Zinc By similarity
Metal binding9111Zinc By similarity
Metal binding9281Zinc By similarity
Metal binding9311Zinc By similarity
Binding site5811Aminoacyl-adenylate By similarity
Binding site6251ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
B2T6I7 [UniParc].

Last modified July 1, 2008. Version 1.
Checksum: B698B672B54B10FA

FASTA945105,985
        10         20         30         40         50         60 
MSNKKADSKP QSRYPVNLLD TPFPMRGDLP KREPQWVKEW QERKVYETIR AASKGRKKFI 

        70         80         90        100        110        120 
LHDGPPYANG DIHLGHAVNK ILKDMIVKAR NLAGFDAVYV PGWDCHGMPI EIQIEKQFGK 

       130        140        150        160        170        180 
SLPAAEVMQK ARAYATEQIE KQKVGFRRLG VLGDWDNPYK TMNFTNEAGE IRALAKIMEK 

       190        200        210        220        230        240 
GYVFRGLKPV NWCFDCGSAL AEAEVEYKDK TDPTIDVLFS FAEPEKTAQA FGLSALPREE 

       250        260        270        280        290        300 
GGIVIWTTTP WTIPANQALN LHPEIVYALV DTPRGLLILA EERVEACLKL YGLEGTIVAT 

       310        320        330        340        350        360 
APGAKLVNVR FNHPLASAHP GYKRTAPVFL GDYVTTETGT GIVHSSPAYG VEDFVSCKAH 

       370        380        390        400        410        420 
GMADSDIINP VMGDGRYIES LALFGGLSIW AANPQIVEAL QGAGSLMRTE KYTHSYMHCW 

       430        440        450        460        470        480 
RHKTPIIYRA TSQWFAGMDV KPNDTDKTLR ETALEGIENT AFYPAWGKQR LFSMIANRPD 

       490        500        510        520        530        540 
WTLSRQRQWG VPMAFFVHKE TGELHPRTLE LLEEVAQRVE KAGIEAWQTL DPRELLGDDA 

       550        560        570        580        590        600 
NMYEKNRDTL DVWFDSGTTH WHVLRGSHKD ELQFPADLYL EGSDQHRGWF HSSLLTASML 

       610        620        630        640        650        660 
DGRPPYNALL THGFTVDGEG RKMSKSLGNG IDPHEVANRL GAEIIRLWIA STDYSGELAI 

       670        680        690        700        710        720 
SEEILKRVTE GYRRIRNTLR FLLANLSDFD FAQHARPVED WLEIDRYAVA LSTNLQNDIL 

       730        740        750        760        770        780 
SHYDKYEFHP VVAKLQTFCS EDLGGFYLDV LKDRLYTTAA DSVARRSAQT ALYHIAHGLL 

       790        800        810        820        830        840 
RLMAPFLSFT AEEAWKIFQP NSETIFTETY HAFPAVPDAG ALLDKWTLLR AARSDVTKAL 

       850        860        870        880        890        900 
EEARVANLIG SSLQAEVEIR ASGARYDALT SLGDDLKFVL ITSAATVVKV DSEAEEAVEV 

       910        920        930        940 
IASKYLKCER CWHYRADVGA NAEHPTLCDR CFSNLFGNGE IRSAA 

« Hide

References

[1]"Complete sequence of chromosome 1 of Burkholderia phytofirmans PsJN."
Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Lang D., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N. expand/collapse author list , Nowak J., Sessitsch A., Lazarovits G., Compant S., Barka E., Tiedje J.
Submitted (MAY-2008) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: DSM 17436 / PsJN.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP001052 Genomic DNA. Translation: ACD17551.1.
RefSeqYP_001896775.1. NC_010681.1.

3D structure databases

ProteinModelPortalB2T6I7.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING398527.Bphyt_3159.

Proteomic databases

PRIDEB2T6I7.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACD17551; ACD17551; Bphyt_3159.
GeneID6283688.
KEGGbpy:Bphyt_3159.
PATRIC19216798. VBIBurPhy117947_7147.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0060.
HOGENOMHOG000246402.
KOK01870.
OMAVLGDWDN.
OrthoDBEOG644ZM1.
ProtClustDBPRK05743.

Enzyme and pathway databases

BioCycBPHY398527:GJEX-3204-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_BURPP
AccessionPrimary (citable) accession number: B2T6I7
Entry history
Integrated into UniProtKB/Swiss-Prot: July 28, 2009
Last sequence update: July 1, 2008
Last modified: April 16, 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