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P18330

- SYI1_PSEFL

UniProt

P18330 - SYI1_PSEFL

Protein

Isoleucine--tRNA ligase 1

Gene

ileS1

Organism
Pseudomonas fluorescens
Status
Reviewed - Annotation score: 4 out of 5- Protein inferred from homologyi
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    • History
      Entry version 100 (01 Oct 2014)
      Sequence version 2 (01 Nov 1995)
      Previous versions | rss
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    Functioni

    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.By similarity
    Confers resistance to the antibiotic mupirocin (pseudomonic acid A), an Ile-analog produced by P.fluorescens NCIMB 10586 itself that competitively inhibits activation by Ile-tRNA synthetase, thus inhibiting protein biosynthesis.

    Catalytic activityi

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

    Cofactori

    Binds 1 zinc ion per subunit.By similarity

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei567 – 5671Aminoacyl-adenylateBy similarity
    Binding sitei611 – 6111ATPBy similarity
    Metal bindingi906 – 9061ZincBy similarity
    Metal bindingi909 – 9091ZincBy similarity
    Metal bindingi926 – 9261ZincBy similarity
    Metal bindingi929 – 9291ZincBy similarity

    GO - Molecular functioni

    1. aminoacyl-tRNA editing activity Source: InterPro
    2. ATP binding Source: UniProtKB-HAMAP
    3. isoleucine-tRNA ligase activity Source: UniProtKB-HAMAP
    4. zinc ion binding Source: UniProtKB-HAMAP

    GO - Biological processi

    1. isoleucyl-tRNA aminoacylation Source: UniProtKB-HAMAP
    2. response to antibiotic Source: UniProtKB-KW

    Keywords - Molecular functioni

    Aminoacyl-tRNA synthetase, Ligase

    Keywords - Biological processi

    Antibiotic resistance, Protein biosynthesis

    Keywords - Ligandi

    ATP-binding, Metal-binding, Nucleotide-binding, Zinc

    Enzyme and pathway databases

    SABIO-RKP18330.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Isoleucine--tRNA ligase 1 (EC:6.1.1.5)
    Alternative name(s):
    Isoleucyl-tRNA synthetase 1
    Short name:
    IleRS 1
    Gene namesi
    Name:ileS1
    Synonyms:ileS
    OrganismiPseudomonas fluorescens
    Taxonomic identifieri294 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesPseudomonadaceaePseudomonas

    Subcellular locationi

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cytoplasm

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 943943Isoleucine--tRNA ligase 1PRO_0000098445Add
    BLAST

    Interactioni

    Subunit structurei

    Monomer.

    Structurei

    3D structure databases

    ProteinModelPortaliP18330.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi58 – 6811"HIGH" regionAdd
    BLAST
    Motifi608 – 6125"KMSKS" region

    Domaini

    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.By similarity

    Sequence similaritiesi

    Family and domain databases

    Gene3Di1.10.730.10. 1 hit.
    3.40.50.620. 2 hits.
    3.90.740.10. 1 hit.
    HAMAPiMF_02002. Ile_tRNA_synth_type1.
    InterProiIPR001412. 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]
    PANTHERiPTHR11946:SF9. PTHR11946:SF9. 1 hit.
    PfamiPF08264. Anticodon_1. 1 hit.
    PF00133. tRNA-synt_1. 1 hit.
    PF06827. zf-FPG_IleRS. 1 hit.
    [Graphical view]
    PRINTSiPR00984. TRNASYNTHILE.
    SUPFAMiSSF47323. SSF47323. 1 hit.
    SSF50677. SSF50677. 1 hit.
    TIGRFAMsiTIGR00392. ileS. 1 hit.
    PROSITEiPS00178. AA_TRNA_LIGASE_I. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P18330-1 [UniParc]FASTAAdd to Basket

    « Hide

    MTDYKATLNL PDTAFPMKAG LPQREPQILQ RWNSIGLYGK LREIGKDRPK    50
    FVLHDGPPYA NGTIHIGHAL NKILKDMILR SKTLSGFDAP YVPGWDCHGL 100
    PIEHKVEVTY GKNLGADKTR ELCRAYATEQ IEGQKSEFIR LGVLGEWDNP 150
    YKTMNFKNEA GEIRALAEIV KGGFVFKGLK PVNWCFDCGS ALAEAEVEYE 200
    DKKSSTIDVA FPIADDAKLA EAFGLASLAK PAAIVIWTTT PWTIPANQAL 250
    NVHPEFTYAL VDVGDRLLVL AEEMVESCLA RYELQGSVIA TATGSALELI 300
    NFRHPFYDRL SPVYLADYVE LGSGTGIVHC SPAYGVDDFV ICKKYGMVND 350
    DIINPVQSNG VYVPSLEFFG GQFIFKADQP IIEKLREVGA LMQTAAIQHS 400
    YMHCWRHKTP LIYRATAQWF IGMDKEPTSG DTLRVRSLKA IEDTKFVPSW 450
    GQARLHSMIA NRPDWCISRQ RNWGVPIPFF LNKESGELHP RTVELMEVVA 500
    QRVEQQGIEA WFKLDAAELL GDEAPLYDKI SDTLDVWFDS GTTHWHVLRG 550
    SHPMGHETGP RADLYLEGSD QHRGWFHSSL LTGCAIDNHA PYRELLTHGF 600
    TVDETGRKMS KSLKNVIEPK KINDTLGADI MRLWVASTDY SGEIAVSDQI 650
    LARSADAYRR IRNTARFMLS NLTGFNPASD LLPAEDMLAL DRWAVDRTLL 700
    LQRELQEHYG EYRFWNVYSK IHNFCVQELG GFYLDIIKDR QYTTGANSKA 750
    RRSAQTALYH ISEALVRWIA PILAFTADEL WEYLPGERNE SVMLNTWYEG 800
    LTELPADFEL GREYWEGVMA VKVAVNKELE VQRAAKAVGG NLQAEVTLFA 850
    EDGLTADLAK LSNELRFVLI TSTASLAPFT QAPADAVATE VPGLKLKVVK 900
    SAFPKCARCW HCREDVGVNP EHPEICGRCV DNISGEGEVR HYA 943
    Length:943
    Mass (Da):105,719
    Last modified:November 1, 1995 - v2
    Checksum:i6827B2BF2EB89FC0
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti28 – 292IL → SC(PubMed:2121716)Curated
    Sequence conflicti755 – 7562QT → DR(PubMed:2121716)Curated
    Sequence conflicti758 – 7592LY → VP(PubMed:2121716)Curated
    Sequence conflicti761 – 7644ISEA → QRR(PubMed:2121716)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X80132 Genomic DNA. Translation: CAA56431.1.
    M35366 Genomic DNA. Translation: AAA25883.1.
    M35367 Genomic DNA. Translation: AAA26022.1. Sequence problems.
    PIRiA37152.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X80132 Genomic DNA. Translation: CAA56431.1 .
    M35366 Genomic DNA. Translation: AAA25883.1 .
    M35367 Genomic DNA. Translation: AAA26022.1 . Sequence problems.
    PIRi A37152.

    3D structure databases

    ProteinModelPortali P18330.
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Enzyme and pathway databases

    SABIO-RK P18330.

    Family and domain databases

    Gene3Di 1.10.730.10. 1 hit.
    3.40.50.620. 2 hits.
    3.90.740.10. 1 hit.
    HAMAPi MF_02002. Ile_tRNA_synth_type1.
    InterProi IPR001412. 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 ]
    PANTHERi PTHR11946:SF9. PTHR11946:SF9. 1 hit.
    Pfami PF08264. Anticodon_1. 1 hit.
    PF00133. tRNA-synt_1. 1 hit.
    PF06827. zf-FPG_IleRS. 1 hit.
    [Graphical view ]
    PRINTSi PR00984. TRNASYNTHILE.
    SUPFAMi SSF47323. SSF47323. 1 hit.
    SSF50677. SSF50677. 1 hit.
    TIGRFAMsi TIGR00392. ileS. 1 hit.
    PROSITEi PS00178. AA_TRNA_LIGASE_I. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Relationship of protein structure of isoleucyl-tRNA synthetase with pseudomonic acid resistance of Escherichia coli. A proposed mode of action of pseudomonic acid as an inhibitor of isoleucyl-tRNA synthetase."
      Yanagisawa T., Lee J.T., Wu H.C., Kawakami M.
      J. Biol. Chem. 269:24304-24309(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: ATCC 49323 / NCIMB 10586.
    2. "Nucleotide sequence of the Pseudomonas fluorescens signal peptidase II gene (lsp) and flanking genes."
      Isaki L., Beers R., Wu H.C.
      J. Bacteriol. 172:6512-6517(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-29 AND 701-943.
      Strain: ATCC 49323 / NCIMB 10586.
    3. "How does Pseudomonas fluorescens avoid suicide from its antibiotic pseudomonic acid? Evidence for two evolutionarily distinct isoleucyl-tRNA synthetases conferring self-defense."
      Yanagisawa T., Kawakami M.
      J. Biol. Chem. 278:25887-25894(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: RESISTANCE TO MUPIROCIN.
      Strain: ATCC 49323 / NCIMB 10586.

    Entry informationi

    Entry nameiSYI1_PSEFL
    AccessioniPrimary (citable) accession number: P18330
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1990
    Last sequence update: November 1, 1995
    Last modified: October 1, 2014
    This is version 100 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    P.fluorescens NCIMB 10586 possesses two distinct IleRSs (IleRS-R1 and IleRS-R2), each with a different level of sensitivity to mupirocin. Purified IleRs-R2 shows no sensitivity to mupirocin even at a concentration of 5 mM, 100'000 fold higher than the Ki value of IleRS-R1.

    Documents

    1. Aminoacyl-tRNA synthetases
      List of aminoacyl-tRNA synthetase entries
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3