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O05959

- LIPA_RICPR

UniProt

O05959 - LIPA_RICPR

Protein

Lipoyl synthase

Gene

lipA

Organism
Rickettsia prowazekii (strain Madrid E)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 96 (01 Oct 2014)
      Sequence version 1 (01 Jul 1997)
      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 bindingi37 – 371Iron-sulfur 1 (4Fe-4S)UniRule annotation
    Metal bindingi42 – 421Iron-sulfur 1 (4Fe-4S)UniRule annotation
    Metal bindingi48 – 481Iron-sulfur 1 (4Fe-4S)UniRule annotation
    Metal bindingi63 – 631Iron-sulfur 2 (4Fe-4S-S-AdoMet)UniRule annotation
    Metal bindingi67 – 671Iron-sulfur 2 (4Fe-4S-S-AdoMet)UniRule annotation
    Metal bindingi70 – 701Iron-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

    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:RP742
    OrganismiRickettsia prowazekii (strain Madrid E)
    Taxonomic identifieri272947 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaAlphaproteobacteriaRickettsialesRickettsiaceaeRickettsieaeRickettsiatyphus group
    ProteomesiUP000002480: Chromosome

    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 – 297297Lipoyl synthasePRO_0000102352Add
    BLAST

    Interactioni

    Protein-protein interaction databases

    STRINGi272947.RP742.

    Structurei

    3D structure databases

    ProteinModelPortaliO05959.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

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

    Phylogenomic databases

    eggNOGiCOG0320.
    HOGENOMiHOG000235998.
    KOiK03644.
    OMAiHPHIPTK.
    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.

    O05959-1 [UniParc]FASTAAdd to Basket

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    MTNLNKRPDW IKVKAPNSVE YYQTKDLIKN LRLNTVCEEA ACPNIGDCWS    50
    RKHATVMILG AVCTRACRFC NVKTGRPDLL DPHEPRRLAE AVQKLNLQHV 100
    VITSVDRDDL EDGGASHFAE CINEIRRSSP NTTIEILTPD FLRKEGAVEI 150
    IANAKPDVFN HNVETVPSLY KTIRPGARYY NSLSLLHNIK KLSPEIFTKS 200
    GMMVGLGEEI NEVVQVMDDL REANVDFLTI GQYLQPTKSH AEIRKYVTPE 250
    EFKYLERIAK TKGFLMVSAT PLTRSSYHAD KDFQKLKGNY NIRLASM 297
    Length:297
    Mass (Da):33,711
    Last modified:July 1, 1997 - v1
    Checksum:iB956BEB63464600A
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Y11778 Genomic DNA. Translation: CAA72454.1.
    AJ235273 Genomic DNA. Translation: CAA15170.1.
    PIRiB71634.
    RefSeqiNP_221094.1. NC_000963.1.

    Genome annotation databases

    EnsemblBacteriaiCAA15170; CAA15170; CAA15170.
    GeneIDi883696.
    KEGGirpr:RP742.
    PATRICi17902343. VBIRicPro72556_0775.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Y11778 Genomic DNA. Translation: CAA72454.1 .
    AJ235273 Genomic DNA. Translation: CAA15170.1 .
    PIRi B71634.
    RefSeqi NP_221094.1. NC_000963.1.

    3D structure databases

    ProteinModelPortali O05959.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 272947.RP742.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai CAA15170 ; CAA15170 ; CAA15170 .
    GeneIDi 883696.
    KEGGi rpr:RP742.
    PATRICi 17902343. VBIRicPro72556_0775.

    Phylogenomic databases

    eggNOGi COG0320.
    HOGENOMi HOG000235998.
    KOi K03644.
    OMAi HPHIPTK.
    OrthoDBi EOG6038ZS.

    Enzyme and pathway databases

    UniPathwayi UPA00538 ; UER00593 .

    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. "Genomic rearrangements during evolution of the obligate intracellular parasite Rickettsia prowazekii as inferred from an analysis of 52015 bp nucleotide sequence."
      Andersson J.O., Andersson S.G.E.
      Microbiology 143:2783-2795(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: Madrid E.
    2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: Madrid E.

    Entry informationi

    Entry nameiLIPA_RICPR
    AccessioniPrimary (citable) accession number: O05959
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 15, 1998
    Last sequence update: July 1, 1997
    Last modified: October 1, 2014
    This is version 96 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, Reference proteome

    Documents

    1. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    2. Rickettsia prowazekii
      Rickettsia prowazekii (strain Madrid E): entries and gene names
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3