Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q8NNP0 (SYI_CORGL) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 76. 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:Cgl2148, cg2359
OrganismCorynebacterium glutamicum (strain ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025) [Reference proteome] [HAMAP]
Taxonomic identifier196627 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesCorynebacterineaeCorynebacteriaceaeCorynebacterium

Protein attributes

Sequence length1054 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_02003

Catalytic activity

ATP + L-isoleucine + tRNA(Ile) = AMP + diphosphate + L-isoleucyl-tRNA(Ile). HAMAP-Rule MF_02003

Cofactor

Zinc By similarity. HAMAP-Rule MF_02003

Subunit structure

Monomer By similarity. HAMAP-Rule MF_02003

Subcellular location

Cytoplasm By similarity HAMAP-Rule MF_02003.

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_02003

Sequence similarities

Belongs to the class-I aminoacyl-tRNA synthetase family. IleS type 2 subfamily.

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_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 – 10541054Isoleucine--tRNA ligase HAMAP-Rule MF_02003
PRO_0000098538

Regions

Motif58 – 6811"HIGH" region HAMAP-Rule MF_02003
Motif627 – 6315"KMSKS" region HAMAP-Rule MF_02003

Sites

Binding site6301ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
Q8NNP0 [UniParc].

Last modified October 1, 2002. Version 1.
Checksum: C3333C86C8554B1F

FASTA1,054117,404
        10         20         30         40         50         60 
MSEAVGGVYP QVDLSGGSSR FPEMEENVLS YWKKDDTFQA SIDQRDGAED YVFYDGPPFA 

        70         80         90        100        110        120 
NGLPHYGHLL TGYVKDIVPR YQTMRGYRVP RVFGWDTHGL PAELEAEKQL GIKDKGEIEA 

       130        140        150        160        170        180 
MGLAKFNEYC ATSVLQYTKE WEEYVTRQAR WVDFENGYKT MDLSFMESVI WAFKELYDKG 

       190        200        210        220        230        240 
LIYQGFRVLP YSWAEHTPLS NQETRLDDSY KLRQDPTLTV TFPVTGVVEG SSANAGLVGA 

       250        260        270        280        290        300 
LALAWTTTPW TLPSNLALAV NPAVTYALVE VAEDGEAEFV GKRVLLAKDL VGSYAKELGA 

       310        320        330        340        350        360 
EAVIVSEHPG SELVGLTYEP IFGYFRDHAN GFQILGAEYV TTEDGTGIVH QAPAFGEDDM 

       370        380        390        400        410        420 
NTCNAAGIEP VIPVDIDGKF TGLVPEYQGQ LVFDANKDII KDLKAAGRVV RHQTIEHSYP 

       430        440        450        460        470        480 
HSWRSGEPLI YMALPSWFVN VTEIRDRMVE VNQDIEWMPA HIRDGQFGKW LEGARDWNIS 

       490        500        510        520        530        540 
RSRYWGSPIP AWVSDNDEYP RVDVYGSLDE LEADFGVRPK SLHRPDIDEL TRPNPDDPTG 

       550        560        570        580        590        600 
KSTMRRVTDV LDVWFDSGSM PFAQVHYPFE NKEWFDTHAP ADFIVEYIGQ TRGWFYLLHV 

       610        620        630        640        650        660 
LSTALFDRPA FKKVVAHGIV LGDDGLKMSK SKGNYPNVNE VFDRDGSDAM RWFLMSSPIL 

       670        680        690        700        710        720 
RGGNLIVTEK GIREGVRQAQ LPMWNAYSFL QLYTSKNATW SVDSTDVLDR YILAKLHDLV 

       730        740        750        760        770        780 
AETQAALDGT DIAKACDLVR NFCDALTNWY VRRSRDRFWA GDEAHPEAFN TLYTVLETLT 

       790        800        810        820        830        840 
RVAAPLLPMT TEVIWRGLTG ERSVHLTDFP SAESFPADAD LVRTMDEIRG VCSAASSVRK 

       850        860        870        880        890        900 
AHKLRNRLPL PGLTVALPDS ARLADFASII RDEVNVKNVD LTSDVDSVGT FEVVVNAKVA 

       910        920        930        940        950        960 
GPRLGKDVQR VIKAVKAGNY TREGDVVVAD GIELNEGEFT ERLVAANPDS TAQIDGVDGL 

       970        980        990       1000       1010       1020 
VVLDMEVTEE LEAEGWAADA IRGLQDARKN SGFEVSDRIS VVVSVPEDKK EWITTHADHI 

      1030       1040       1050 
AAEVLATSFE IVTDALDGET HDIVAGVTAK VTKN 

« Hide

References

[1]"The Corynebacterium glutamicum genome: features and impacts on biotechnological processes."
Ikeda M., Nakagawa S.
Appl. Microbiol. Biotechnol. 62:99-109(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025.
[2]"The complete Corynebacterium glutamicum ATCC 13032 genome sequence and its impact on the production of L-aspartate-derived amino acids and vitamins."
Kalinowski J., Bathe B., Bartels D., Bischoff N., Bott M., Burkovski A., Dusch N., Eggeling L., Eikmanns B.J., Gaigalat L., Goesmann A., Hartmann M., Huthmacher K., Kraemer R., Linke B., McHardy A.C., Meyer F., Moeckel B. expand/collapse author list , Pfefferle W., Puehler A., Rey D.A., Rueckert C., Rupp O., Sahm H., Wendisch V.F., Wiegraebe I., Tauch A.
J. Biotechnol. 104:5-25(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BA000036 Genomic DNA. Translation: BAB99541.1.
BX927154 Genomic DNA. Translation: CAF20488.1.
RefSeqNP_601350.1. NC_003450.3.
YP_226389.1. NC_006958.1.

3D structure databases

ProteinModelPortalQ8NNP0.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING196627.cg2359.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaBAB99541; BAB99541; BAB99541.
CAF20488; CAF20488; cg2359.
GeneID1020100.
3345452.
KEGGcgb:cg2359.
cgl:NCgl2068.
PATRIC21496300. VBICorGlu203724_2086.

Phylogenomic databases

eggNOGCOG0060.
HOGENOMHOG000246403.
KOK01870.
OMADWNLSRS.
OrthoDBEOG644ZM1.
ProtClustDBPRK06039.

Family and domain databases

Gene3D1.10.730.10. 1 hit.
3.40.50.620. 2 hits.
3.90.740.10. 1 hit.
HAMAPMF_02003. Ile_tRNA_synth_type2.
InterProIPR001412. aa-tRNA-synth_I_CS.
IPR002300. aa-tRNA-synth_Ia.
IPR002301. Ile-tRNA-ligase.
IPR023586. Ile-tRNA-ligase_type2.
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.
[Graphical view]
PfamPF08264. Anticodon_1. 1 hit.
PF00133. tRNA-synt_1. 1 hit.
[Graphical view]
PRINTSPR00984. TRNASYNTHILE.
SUPFAMSSF47323. SSF47323. 2 hits.
SSF50677. SSF50677. 1 hit.
TIGRFAMsTIGR00392. ileS. 1 hit.
PROSITEPS00178. AA_TRNA_LIGASE_I. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameSYI_CORGL
AccessionPrimary (citable) accession number: Q8NNP0
Secondary accession number(s): Q6M3S6
Entry history
Integrated into UniProtKB/Swiss-Prot: December 20, 2005
Last sequence update: October 1, 2002
Last modified: April 16, 2014
This is version 76 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