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Q72RU2

- LIPA_LEPIC

UniProt

Q72RU2 - LIPA_LEPIC

Protein

Lipoyl synthase

Gene

lipA

Organism
Leptospira interrogans serogroup Icterohaemorrhagiae serovar copenhageni (strain Fiocruz L1-130)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 75 (01 Oct 2014)
      Sequence version 1 (05 Jul 2004)
      Previous versions | rss
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    Functioni

    Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.UniRule annotation

    Catalytic activityi

    Protein N(6)-(octanoyl)lysine + 2 sulfur-(sulfur carrier) + 2 S-adenosyl-L-methionine = protein N(6)-(lipoyl)lysine + 2 (sulfur carrier) + 2 L-methionine + 2 5'-deoxyadenosine.UniRule annotation

    Cofactori

    Binds 2 4Fe-4S clusters per subunit. One cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine.UniRule annotation

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi53 – 531Iron-sulfur 1 (4Fe-4S)UniRule annotation
    Metal bindingi58 – 581Iron-sulfur 1 (4Fe-4S)UniRule annotation
    Metal bindingi64 – 641Iron-sulfur 1 (4Fe-4S)UniRule annotation
    Metal bindingi79 – 791Iron-sulfur 2 (4Fe-4S-S-AdoMet)UniRule annotation
    Metal bindingi83 – 831Iron-sulfur 2 (4Fe-4S-S-AdoMet)UniRule annotation
    Metal bindingi86 – 861Iron-sulfur 2 (4Fe-4S-S-AdoMet)UniRule annotation

    GO - Molecular functioni

    1. 4 iron, 4 sulfur cluster binding Source: UniProtKB-HAMAP
    2. lipoate synthase activity Source: UniProtKB-HAMAP
    3. metal ion binding Source: UniProtKB-KW

    GO - Biological processi

    1. protein lipoylation Source: UniProtKB-HAMAP

    Keywords - Molecular functioni

    Transferase

    Keywords - Ligandi

    4Fe-4S, Iron, Iron-sulfur, Metal-binding, S-adenosyl-L-methionine

    Enzyme and pathway databases

    BioCyciLINT267671:GHQI-1643-MONOMER.
    UniPathwayiUPA00538; UER00593.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Lipoyl synthaseUniRule annotation (EC:2.8.1.8UniRule annotation)
    Alternative name(s):
    Lip-synUniRule annotation
    Short name:
    LSUniRule annotation
    Lipoate synthaseUniRule annotation
    Lipoic acid synthaseUniRule annotation
    Sulfur insertion protein LipAUniRule annotation
    Gene namesi
    Name:lipAUniRule annotation
    Ordered Locus Names:LIC_11646
    OrganismiLeptospira interrogans serogroup Icterohaemorrhagiae serovar copenhageni (strain Fiocruz L1-130)
    Taxonomic identifieri267671 [NCBI]
    Taxonomic lineageiBacteriaSpirochaetesSpirochaetalesLeptospiraceaeLeptospira
    ProteomesiUP000007037: Chromosome I

    Subcellular locationi

    Cytoplasm UniRule annotation

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cytoplasm

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 301301Lipoyl synthasePRO_0000102322Add
    BLAST

    Interactioni

    Protein-protein interaction databases

    STRINGi267671.LIC11646.

    Structurei

    3D structure databases

    ProteinModelPortaliQ72RU2.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the radical SAM superfamily. Lipoyl synthase family.UniRule annotation

    Phylogenomic databases

    KOiK03644.
    OMAiTIRAVRH.
    OrthoDBiEOG6038ZS.

    Family and domain databases

    Gene3Di3.20.20.70. 1 hit.
    HAMAPiMF_00206. Lipoyl_synth.
    InterProiIPR013785. Aldolase_TIM.
    IPR006638. Elp3/MiaB/NifB.
    IPR003698. Lipoyl_synth.
    IPR007197. rSAM.
    [Graphical view]
    PANTHERiPTHR10949. PTHR10949. 1 hit.
    PfamiPF04055. Radical_SAM. 1 hit.
    [Graphical view]
    PIRSFiPIRSF005963. Lipoyl_synth. 1 hit.
    SMARTiSM00729. Elp3. 1 hit.
    [Graphical view]
    TIGRFAMsiTIGR00510. lipA. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    Q72RU2-1 [UniParc]FASTAAdd to Basket

    « Hide

    MNPLKKKPRT HSLQNAPEKP DWLKVKLAFP DPKNNPVAIV RNSLEEKKLN    50
    TVCESASCPN LNHCWSRKTA TYMLGGDICT RRCSYCDVAS GKPFPLDPEE 100
    PKRIAESSIA LGLRHVVITS VNRDDLEDGG AAHFAKTVKE IRKGLPDCKI 150
    ELLIPDLKVK QEALEIIFEC NPDIFNHNLE TVKRLFPEVA PQKRYERSLD 200
    VLKIASARGF LTKSGLILGM GETLEEVKEC MQDLASVGVS LLTLGQYLQP 250
    TSTHLPVKEY VVPQVFKDLR IYGKSIGFKG VFSGPLVRSS YHADEQISWN 300
    P 301
    Length:301
    Mass (Da):33,666
    Last modified:July 5, 2004 - v1
    Checksum:iD2C8CAB824202EB6
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AE016823 Genomic DNA. Translation: AAS70241.1.
    RefSeqiYP_001604.1. NC_005823.1.

    Genome annotation databases

    EnsemblBacteriaiAAS70241; AAS70241; LIC_11646.
    GeneIDi2771666.
    KEGGilic:LIC11646.
    PATRICi22375649. VBILepInt6257_1989.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AE016823 Genomic DNA. Translation: AAS70241.1 .
    RefSeqi YP_001604.1. NC_005823.1.

    3D structure databases

    ProteinModelPortali Q72RU2.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 267671.LIC11646.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAS70241 ; AAS70241 ; LIC_11646 .
    GeneIDi 2771666.
    KEGGi lic:LIC11646.
    PATRICi 22375649. VBILepInt6257_1989.

    Phylogenomic databases

    KOi K03644.
    OMAi TIRAVRH.
    OrthoDBi EOG6038ZS.

    Enzyme and pathway databases

    UniPathwayi UPA00538 ; UER00593 .
    BioCyci LINT267671:GHQI-1643-MONOMER.

    Family and domain databases

    Gene3Di 3.20.20.70. 1 hit.
    HAMAPi MF_00206. Lipoyl_synth.
    InterProi IPR013785. Aldolase_TIM.
    IPR006638. Elp3/MiaB/NifB.
    IPR003698. Lipoyl_synth.
    IPR007197. rSAM.
    [Graphical view ]
    PANTHERi PTHR10949. PTHR10949. 1 hit.
    Pfami PF04055. Radical_SAM. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF005963. Lipoyl_synth. 1 hit.
    SMARTi SM00729. Elp3. 1 hit.
    [Graphical view ]
    TIGRFAMsi TIGR00510. lipA. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. "Comparative genomics of two Leptospira interrogans serovars reveals novel insights into physiology and pathogenesis."
      Nascimento A.L.T.O., Ko A.I., Martins E.A.L., Monteiro-Vitorello C.B., Ho P.L., Haake D.A., Verjovski-Almeida S., Hartskeerl R.A., Marques M.V., Oliveira M.C., Menck C.F.M., Leite L.C.C., Carrer H., Coutinho L.L., Degrave W.M., Dellagostin O.A., El-Dorry H., Ferro E.S.
      , Ferro M.I.T., Furlan L.R., Gamberini M., Giglioti E.A., Goes-Neto A., Goldman G.H., Goldman M.H.S., Harakava R., Jeronimo S.M.B., Junqueira-de-Azevedo I.L.M., Kimura E.T., Kuramae E.E., Lemos E.G.M., Lemos M.V.F., Marino C.L., Nunes L.R., de Oliveira R.C., Pereira G.G., Reis M.S., Schriefer A., Siqueira W.J., Sommer P., Tsai S.M., Simpson A.J.G., Ferro J.A., Camargo L.E.A., Kitajima J.P., Setubal J.C., Van Sluys M.A.
      J. Bacteriol. 186:2164-2172(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: Fiocruz L1-130.

    Entry informationi

    Entry nameiLIPA_LEPIC
    AccessioniPrimary (citable) accession number: Q72RU2
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 15, 2005
    Last sequence update: July 5, 2004
    Last modified: October 1, 2014
    This is version 75 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome

    Documents

    1. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3