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A2S5Y9

- LIPA_BURM9

UniProt

A2S5Y9 - LIPA_BURM9

Protein

Lipoyl synthase

Gene

lipA

Organism
Burkholderia mallei (strain NCTC 10229)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 51 (01 Oct 2014)
      Sequence version 1 (06 Mar 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 bindingi76 – 761Iron-sulfur 1 (4Fe-4S)UniRule annotation
    Metal bindingi81 – 811Iron-sulfur 1 (4Fe-4S)UniRule annotation
    Metal bindingi87 – 871Iron-sulfur 1 (4Fe-4S)UniRule annotation
    Metal bindingi102 – 1021Iron-sulfur 2 (4Fe-4S-S-AdoMet)UniRule annotation
    Metal bindingi106 – 1061Iron-sulfur 2 (4Fe-4S-S-AdoMet)UniRule annotation
    Metal bindingi109 – 1091Iron-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

    BioCyciBMAL412022:GJI8-1375-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:BMA10229_A1375
    OrganismiBurkholderia mallei (strain NCTC 10229)
    Taxonomic identifieri412022 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaBetaproteobacteriaBurkholderialesBurkholderiaceaeBurkholderiapseudomallei group
    ProteomesiUP000002283: 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 – 329329Lipoyl synthasePRO_1000012198Add
    BLAST

    Interactioni

    Protein-protein interaction databases

    STRINGi412022.BMA10229_A1375.

    Structurei

    3D structure databases

    ProteinModelPortaliA2S5Y9.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

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

    Phylogenomic databases

    eggNOGiCOG0320.
    HOGENOMiHOG000235997.
    KOiK03644.
    OMAiPEEPYNT.
    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.

    A2S5Y9-1 [UniParc]FASTAAdd to Basket

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    MTDLTATPAP AEPAASAYDP TAKQKAQAKT ARIPIKIVPI EKLKKPEWIR    50
    VKAATSSSRF NEIKTILREH NLHTVCEEAS CPNIGECFGK GTATFMIMGD 100
    KCTRRCPFCD VGHGRPDPLD ADEPKNLART IAALKLKYVV ITSVDRDDLR 150
    DGGAGHFVEC IREVREQSPA TRIEILTPDF RGRLDRALAI LNAAPPDVMN 200
    HNLETVPRLY KEARPGSDYA HSLKLLKDFK ALHPDVATKS GLMVGLGETT 250
    DEILQVMRDL RAHDVDMLTI GQYLQPSEHH LPVREYVHPD TFKMYEEEAY 300
    KMGFTHAAVG AMVRSSYHAD LQAHGAGVV 329
    Length:329
    Mass (Da):36,459
    Last modified:March 6, 2007 - v1
    Checksum:i209EA922ADB5BC9A
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000546 Genomic DNA. Translation: ABN01937.1.
    RefSeqiYP_001027358.1. NC_008836.1.

    Genome annotation databases

    EnsemblBacteriaiABN01937; ABN01937; BMA10229_A1375.
    GeneIDi4791180.
    KEGGibml:BMA10229_A1375.
    PATRICi19133710. VBIBurMal46188_3574.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000546 Genomic DNA. Translation: ABN01937.1 .
    RefSeqi YP_001027358.1. NC_008836.1.

    3D structure databases

    ProteinModelPortali A2S5Y9.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 412022.BMA10229_A1375.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai ABN01937 ; ABN01937 ; BMA10229_A1375 .
    GeneIDi 4791180.
    KEGGi bml:BMA10229_A1375.
    PATRICi 19133710. VBIBurMal46188_3574.

    Phylogenomic databases

    eggNOGi COG0320.
    HOGENOMi HOG000235997.
    KOi K03644.
    OMAi PEEPYNT.
    OrthoDBi EOG6038ZS.

    Enzyme and pathway databases

    UniPathwayi UPA00538 ; UER00593 .
    BioCyci BMAL412022:GJI8-1375-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. DeShazer D., Woods D.E., Nierman W.C.
      Submitted (JAN-2007) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: NCTC 10229.

    Entry informationi

    Entry nameiLIPA_BURM9
    AccessioniPrimary (citable) accession number: A2S5Y9
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 15, 2008
    Last sequence update: March 6, 2007
    Last modified: October 1, 2014
    This is version 51 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