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A0L509

- LIPA_MAGSM

UniProt

A0L509 - LIPA_MAGSM

Protein

Lipoyl synthase

Gene

lipA

Organism
Magnetococcus sp. (strain MC-1)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 57 (01 Oct 2014)
      Sequence version 1 (12 Dec 2006)
      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 bindingi45 – 451Iron-sulfur 1 (4Fe-4S)UniRule annotation
    Metal bindingi50 – 501Iron-sulfur 1 (4Fe-4S)UniRule annotation
    Metal bindingi56 – 561Iron-sulfur 1 (4Fe-4S)UniRule annotation
    Metal bindingi71 – 711Iron-sulfur 2 (4Fe-4S-S-AdoMet)UniRule annotation
    Metal bindingi75 – 751Iron-sulfur 2 (4Fe-4S-S-AdoMet)UniRule annotation
    Metal bindingi78 – 781Iron-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

    BioCyciMSP156889:GH36-532-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:Mmc1_0527
    OrganismiMagnetococcus sp. (strain MC-1)
    Taxonomic identifieri156889 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaAlphaproteobacteriaMagnetococcalesMagnetococcaceaeMagnetococcus
    ProteomesiUP000002586: 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 – 296296Lipoyl synthasePRO_0000325273Add
    BLAST

    Interactioni

    Protein-protein interaction databases

    STRINGi156889.Mmc1_0527.

    Structurei

    3D structure databases

    ProteinModelPortaliA0L509.
    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.

    A0L509-1 [UniParc]FASTAAdd to Basket

    « Hide

    MISGVDPQTH LPSGKPRWLK VKAPTSPGYL KLKGMLRQGG LHTVCEEATC    50
    PNIGQCWHEG SAAFMILGDT CTRRCAFCNV KTGKPLPPNP DEPQQLALTA 100
    QRMELKHVVI TSVDRDDLED GGAGQFIACI QALRRVLPEA SVEVLTPDFR 150
    HKQGALERLV AARPDVFNHN VETVPRLYAN VRPVSSYAFS LEVLRRAKQL 200
    NPEGMTKSGI MLGLGEDEAE VLAVFADLRA AGVDYLTVGQ YLRPSPAHHA 250
    VVRYWEPERF EALGQQALQL GFKRVSSAPL ARSSFHASEL HGVDNA 296
    Length:296
    Mass (Da):32,465
    Last modified:December 12, 2006 - v1
    Checksum:i97CFEC0BBDC10599
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000471 Genomic DNA. Translation: ABK43052.1.
    RefSeqiYP_864458.1. NC_008576.1.

    Genome annotation databases

    EnsemblBacteriaiABK43052; ABK43052; Mmc1_0527.
    GeneIDi4480692.
    KEGGimgm:Mmc1_0527.
    PATRICi22427570. VBIMagSp23654_0552.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000471 Genomic DNA. Translation: ABK43052.1 .
    RefSeqi YP_864458.1. NC_008576.1.

    3D structure databases

    ProteinModelPortali A0L509.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 156889.Mmc1_0527.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai ABK43052 ; ABK43052 ; Mmc1_0527 .
    GeneIDi 4480692.
    KEGGi mgm:Mmc1_0527.
    PATRICi 22427570. VBIMagSp23654_0552.

    Phylogenomic databases

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

    Enzyme and pathway databases

    UniPathwayi UPA00538 ; UER00593 .
    BioCyci MSP156889:GH36-532-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. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: MC-1.

    Entry informationi

    Entry nameiLIPA_MAGSM
    AccessioniPrimary (citable) accession number: A0L509
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: March 18, 2008
    Last sequence update: December 12, 2006
    Last modified: October 1, 2014
    This is version 57 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. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3