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B2GB86 (SYI_LACF3) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 50. 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:LAF_0582
OrganismLactobacillus fermentum (strain NBRC 3956 / LMG 18251) [Complete proteome] [HAMAP]
Taxonomic identifier334390 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliLactobacillalesLactobacillaceaeLactobacillus

Protein attributes

Sequence length930 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 – 930930Isoleucine--tRNA ligase HAMAP-Rule MF_02002
PRO_1000189175

Regions

Motif57 – 6711"HIGH" region HAMAP-Rule MF_02002
Motif596 – 6005"KMSKS" region HAMAP-Rule MF_02002

Sites

Metal binding8891Zinc By similarity
Metal binding8921Zinc By similarity
Metal binding9091Zinc By similarity
Metal binding9121Zinc By similarity
Binding site5551Aminoacyl-adenylate By similarity
Binding site5991ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
B2GB86 [UniParc].

Last modified June 10, 2008. Version 1.
Checksum: A87228F73E2C1A54

FASTA930105,635
        10         20         30         40         50         60 
MRVKDTLNLG KTKFPMRGRL PETEAQREAL WEENKVYEQR QKLNEGKPSF VLHDGPPYAN 

        70         80         90        100        110        120 
GPIHIGHAMN KISKDFIVRY KSMTGYRAPY VPGWDTHGLP IEHQLTKAGY DRKKMSLTEF 

       130        140        150        160        170        180 
RDLCQKYALE QVEIQKKGFK RLGVAGEWDH PYLTLAKEFE AAQIKVFGAF AKRGLLYQAK 

       190        200        210        220        230        240 
KPVYWSWSSE SALAEAEVEY HDVVAKTAFF TEQVQDGKGL LDSDTYLVGW TTTPWTIPAS 

       250        260        270        280        290        300 
EAVAVSADFE YALVQPSGSD RKYVVAASLL GDLAQKFNWT DYQVVKTFKG AEMEGMTTKH 

       310        320        330        340        350        360 
PYIDRELLVG LADYVTDDAG TGLVHTAPGY GDDDYNFGKK YNLPIFAPMN DQGVLTAENG 

       370        380        390        400        410        420 
PEFDGVFYQD ADDISLRLLE EHDALLLEED LEHSYPFDWR TKKPIVFRAT DQWFVSIDKM 

       430        440        450        460        470        480 
RDEILKAVDE VTYYPTWGKV RLRNMLKDRG DWVISRQRVW GVPLPIFYAE DGTPIMTEET 

       490        500        510        520        530        540 
INHVSDLFRE YGSNVWFDRE AKDLLPAGFT SEHSPNGKFT KETDIMDVWF DSGSSHQGVL 

       550        560        570        580        590        600 
AERDYLTYPA DMYLEGSDQY RGWFNSSLIT SVVVSGHAPY KSVLSQGFTL DQSGKKMSKS 

       610        620        630        640        650        660 
LGNVIDPNKV VKQMGAEIIR LWVMSADTSA DVRVSMETLQ QISESYRKLR NTFRFLLANT 

       670        680        690        700        710        720 
SDFGPENFVA YEKREAVDQY MTVNFNHFLA GMRDEFDRYD FLNAYKHLIN FVNNDLSSFY 

       730        740        750        760        770        780 
MNVAKDVLYI EPEDSHVRRS MQATFYEILS GLTKLLTPIL PHTTEEVWSY MDEPEDFVQL 

       790        800        810        820        830        840 
TEIPEARTFE NGNALLEKWE GFMELRSHVL KCLEEARNAK LIGRSLEASA DLYLTASQQE 

       850        860        870        880        890        900 
LLADLGTDAG LLCGVSALSV HDASEAPAEA ESFSDNAAVL VQAAKGEVCD RCRMTKEDVG 

       910        920        930 
SDPAYQQLCA RCAKLVRENF PQTVEEGLEK 

« Hide

References

[1]"Comparative genome analysis of Lactobacillus reuteri and Lactobacillus fermentum reveal a genomic island for reuterin and cobalamin production."
Morita H., Toh H., Fukuda S., Horikawa H., Oshima K., Suzuki T., Murakami M., Hisamatsu S., Kato Y., Takizawa T., Fukuoka H., Yoshimura T., Itoh K., O'Sullivan D.J., McKay L.L., Ohno H., Kikuchi J., Masaoka T., Hattori M.
DNA Res. 15:151-161(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: NBRC 3956 / LMG 18251.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AP008937 Genomic DNA. Translation: BAG26918.1.
RefSeqYP_001843398.1. NC_010610.1.

3D structure databases

ProteinModelPortalB2GB86.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING334390.LAF_0582.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaBAG26918; BAG26918; LAF_0582.
GeneID6233688.
KEGGlfe:LAF_0582.
PATRIC22225282. VBILacFer15497_0628.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0060.
HOGENOMHOG000246402.
KOK01870.
OMALGRRSCQ.
OrthoDBEOG644ZM1.

Enzyme and pathway databases

BioCycLFER334390:GJ2S-626-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_LACF3
AccessionPrimary (citable) accession number: B2GB86
Entry history
Integrated into UniProtKB/Swiss-Prot: July 28, 2009
Last sequence update: June 10, 2008
Last modified: May 14, 2014
This is version 50 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