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Q5NQQ7 (SYI_ZYMMO) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 74. 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:ZMO0323
OrganismZymomonas mobilis subsp. mobilis (strain ATCC 31821 / ZM4 / CP4) [Complete proteome] [HAMAP]
Taxonomic identifier264203 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaSphingomonadalesSphingomonadaceaeZymomonas

Protein attributes

Sequence length941 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 – 941941Isoleucine--tRNA ligase HAMAP-Rule MF_02002
PRO_0000098513

Regions

Motif69 – 7911"HIGH" region HAMAP-Rule MF_02002
Motif630 – 6345"KMSKS" region HAMAP-Rule MF_02002

Sites

Metal binding9151Zinc By similarity
Metal binding9181Zinc By similarity
Metal binding9321Zinc By similarity
Metal binding9351Zinc By similarity
Binding site5891Aminoacyl-adenylate By similarity
Binding site6331ATP By similarity

Experimental info

Sequence conflict92 – 943SQT → TKP in AAD56932. Ref.1
Sequence conflict1401E → K in AAD56932. Ref.1
Sequence conflict1811A → S in AAD56932. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q5NQQ7 [UniParc].

Last modified February 1, 2005. Version 1.
Checksum: 645DF7E9C0E82279

FASTA941106,263
        10         20         30         40         50         60 
MSDQKSADAT QARDWRPTVF LPKTSFPMKA GLAKKEPEIL ARWQKEDLYQ QLREQRKGAE 

        70         80         90        100        110        120 
RFILHDGPPY ANGDIHIGHA LNKILKDIIM RSQTLLGKDV PYIPGWDCHG LPIEWKVEEQ 

       130        140        150        160        170        180 
FRKKKLNVDK DVNAVEFRQE CRKYAVHWVD TQRQEFKRLG VLGEWDNPYL TMNFEAEAII 

       190        200        210        220        230        240 
AGELMRFSET GQIYRGAKPV LWSVVEKTAL AEAEVDYADV DSTTIDLAFK ITDSKIPELV 

       250        260        270        280        290        300 
GGYAVIWTTT PWTIPANRAL AYGPDIDYVL VDLNGKHYLF AEALLEDSLK RIGHEGDAPV 

       310        320        330        340        350        360 
LWRGKGAELD GSIAQHPMFE KGGFFAEPRP FLGGSHVTTE AGTGIVHMAP DYGEDDFLLC 

       370        380        390        400        410        420 
KAHNIDPVFA VEDDGRYRKD WLWMGGEGLV ISPKINAADG PICSDLREVG ALLATSVLHH 

       430        440        450        460        470        480 
SYPHSWRSKA KLIYRCTPQW FIALDRPVEK GAIAGKTLRE TALKAIDEVS WFPAKGKNRI 

       490        500        510        520        530        540 
QTMVEGRPDW VISRQRAWGV PITLYVNRES GDYLRDPEVN ARILAAFRKE GADAWFKANH 

       550        560        570        580        590        600 
QLFLGDKYRL EDYEPVNDIL DVWFDSGSTH AFVVEARYGE GTRAQLYLEG SDQHRGWFQS 

       610        620        630        640        650        660 
SLLESCGSRG HAPYEAVLTH GFTLDGTGRK MSKSVGNVID PLKVINESGA DILRMWVAST 

       670        680        690        700        710        720 
DYNEDVRISK EVLSGTSDGY RKLRNSFRYL LGALEGFSEE EKVDLADLPE LEKYILHLLA 

       730        740        750        760        770        780 
ELDQALHESV NGFAFNRYLR LLSDFVNNDL SAFFFDIRKD RLYCDVGEAA PQGTEERRAY 

       790        800        810        820        830        840 
RTVLDILFHA LVRYAAPILC FTAEEVWLHR FPDAGSVHLS VWPEVDGQWK NAVLGEKWAV 

       850        860        870        880        890        900 
IREQRQIVTE KIEPLRREKI VGSSLEAEVT LPVDAATAKI LSSVDFSEIC ITAKINLVDA 

       910        920        930        940 
SDAAITVDRT QNHKCGRCWQ HLPEVEEDGA LCDRCKSVVG E 

« Hide

References

« Hide 'large scale' references
[1]Lee H.J., Kang H.S.
Submitted (AUG-1999) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC 31821 / ZM4 / CP4.
[2]"The genome sequence of the ethanologenic bacterium Zymomonas mobilis ZM4."
Seo J.-S., Chong H., Park H.S., Yoon K.-O., Jung C., Kim J.J., Hong J.H., Kim H., Kim J.-H., Kil J.-I., Park C.J., Oh H.-M., Lee J.-S., Jin S.-J., Um H.-W., Lee H.-J., Oh S.-J., Kim J.Y. expand/collapse author list , Kang H.L., Lee S.Y., Lee K.J., Kang H.S.
Nat. Biotechnol. 23:63-68(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 31821 / ZM4 / CP4.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF180145 Genomic DNA. Translation: AAD56932.1.
AE008692 Genomic DNA. Translation: AAV88947.1.
RefSeqYP_162058.1. NC_006526.2.

3D structure databases

ProteinModelPortalQ5NQQ7.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING264203.ZMO0323.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAV88947; AAV88947; ZMO0323.
GeneID3188160.
KEGGzmo:ZMO0323.
PATRIC32565986. VBIZymMob102260_0307.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0060.
HOGENOMHOG000246402.
KOK01870.
OMAKPVHWCL.
OrthoDBEOG644ZM1.

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.
[Graphical view]
PANTHERPTHR11946:SF9. PTHR11946:SF9. 1 hit.
PfamPF08264. Anticodon_1. 1 hit.
PF00133. tRNA-synt_1. 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_ZYMMO
AccessionPrimary (citable) accession number: Q5NQQ7
Secondary accession number(s): Q9RNJ5
Entry history
Integrated into UniProtKB/Swiss-Prot: December 20, 2005
Last sequence update: February 1, 2005
Last modified: May 14, 2014
This is version 74 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