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A0PNH7

- LIPA_MYCUA

UniProt

A0PNH7 - LIPA_MYCUA

Protein

Lipoyl synthase

Gene

lipA

Organism
Mycobacterium ulcerans (strain Agy99)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 56 (01 Oct 2014)
      Sequence version 1 (09 Jan 2007)
      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 bindingi65 – 651Iron-sulfur 1 (4Fe-4S)UniRule annotation
    Metal bindingi70 – 701Iron-sulfur 1 (4Fe-4S)UniRule annotation
    Metal bindingi76 – 761Iron-sulfur 1 (4Fe-4S)UniRule annotation
    Metal bindingi91 – 911Iron-sulfur 2 (4Fe-4S-S-AdoMet)UniRule annotation
    Metal bindingi95 – 951Iron-sulfur 2 (4Fe-4S-S-AdoMet)UniRule annotation
    Metal bindingi98 – 981Iron-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:MUL_1343
    OrganismiMycobacterium ulcerans (strain Agy99)
    Taxonomic identifieri362242 [NCBI]
    Taxonomic lineageiBacteriaActinobacteriaActinobacteridaeActinomycetalesCorynebacterineaeMycobacteriaceaeMycobacterium
    ProteomesiUP000000765: Chromosome

    Organism-specific databases

    GenoListiMUL_1343.

    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 – 324324Lipoyl synthasePRO_1000012240Add
    BLAST

    Interactioni

    Protein-protein interaction databases

    STRINGi362242.MUL_1343.

    Structurei

    3D structure databases

    ProteinModelPortaliA0PNH7.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

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

    Phylogenomic databases

    eggNOGiCOG0320.
    HOGENOMiHOG000235997.
    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.

    A0PNH7-1 [UniParc]FASTAAdd to Basket

    « Hide

    MNVAPEPGAA GAAAPQGRKL LRLEVRNAQT PIERKPPWIR TRARMGPEYT    50
    ELKNLVRREG LHTVCEEAGC PNIFECWEDR EATFLIGGDQ CTRRCDFCQI 100
    DTGKPAPLDR DEPRRVAESV HTMGLRYATV TGVARDDLPD GGAWLYAETV 150
    RAIKELNPST GVELLIPDFN GKADQLGEVF EARPEVLAHN VETVPRVFKR 200
    IRPAFTYQRS LDVLTAARQF GLVTKSNLIL GMGETPEEVR TALVDLHDAG 250
    CDIITITQYL RPSPRHHPVE RWVRPEEFVE FAQYAEGLGF AGVLAGPLVR 300
    SSYRAGRLYE QARSRNTSGA SNSG 324
    Length:324
    Mass (Da):36,021
    Last modified:January 9, 2007 - v1
    Checksum:i7EB830150D893E88
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000325 Genomic DNA. Translation: ABL03896.1.
    RefSeqiYP_905367.1. NC_008611.1.

    Genome annotation databases

    EnsemblBacteriaiABL03896; ABL03896; MUL_1343.
    GeneIDi4554083.
    KEGGimul:MUL_1343.
    PATRICi18169528. VBIMycUlc37413_1620.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000325 Genomic DNA. Translation: ABL03896.1 .
    RefSeqi YP_905367.1. NC_008611.1.

    3D structure databases

    ProteinModelPortali A0PNH7.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 362242.MUL_1343.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai ABL03896 ; ABL03896 ; MUL_1343 .
    GeneIDi 4554083.
    KEGGi mul:MUL_1343.
    PATRICi 18169528. VBIMycUlc37413_1620.

    Organism-specific databases

    GenoListi MUL_1343.

    Phylogenomic databases

    eggNOGi COG0320.
    HOGENOMi HOG000235997.
    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. "Reductive evolution and niche adaptation inferred from the genome of Mycobacterium ulcerans, the causative agent of Buruli ulcer."
      Stinear T.P., Seemann T., Pidot S., Frigui W., Reysset G., Garnier T., Meurice G., Simon D., Bouchier C., Ma L., Tichit M., Porter J.L., Ryan J., Johnson P.D.R., Davies J.K., Jenkin G.A., Small P.L.C., Jones L.M.
      , Tekaia F., Laval F., Daffe M., Parkhill J., Cole S.T.
      Genome Res. 17:192-200(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: Agy99.

    Entry informationi

    Entry nameiLIPA_MYCUA
    AccessioniPrimary (citable) accession number: A0PNH7
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 15, 2008
    Last sequence update: January 9, 2007
    Last modified: October 1, 2014
    This is version 56 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