Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

B3M996

- LIAS_DROAN

UniProt

B3M996 - LIAS_DROAN

Protein

Lipoyl synthase, mitochondrial

Gene

Las

Organism
Drosophila ananassae (Fruit fly)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 37 (01 Oct 2014)
      Sequence version 1 (02 Sep 2008)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    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.

    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 bindingi103 – 1031Iron-sulfur 1 (4Fe-4S)UniRule annotation
    Metal bindingi108 – 1081Iron-sulfur 1 (4Fe-4S)UniRule annotation
    Metal bindingi114 – 1141Iron-sulfur 1 (4Fe-4S)UniRule annotation
    Metal bindingi134 – 1341Iron-sulfur 2 (4Fe-4S-S-AdoMet)UniRule annotation
    Metal bindingi138 – 1381Iron-sulfur 2 (4Fe-4S-S-AdoMet)UniRule annotation
    Metal bindingi141 – 1411Iron-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 synthase, mitochondrialUniRule annotation (EC:2.8.1.8UniRule annotation)
    Alternative name(s):
    Lipoate synthaseUniRule annotation
    Short name:
    LSUniRule annotation
    Short name:
    Lip-synUniRule annotation
    Lipoic acid synthaseUniRule annotation
    Gene namesi
    Name:LasUniRule annotation
    ORF Names:GF24134
    OrganismiDrosophila ananassae (Fruit fly)
    Taxonomic identifieri7217 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
    ProteomesiUP000007801: Unassembled WGS sequence

    Organism-specific databases

    FlyBaseiFBgn0101128. Dana\GF24134.

    Subcellular locationi

    Mitochondrion UniRule annotation

    GO - Cellular componenti

    1. mitochondrion Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Mitochondrion

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini? – 376Lipoyl synthase, mitochondrialPRO_0000398216
    Transit peptidei1 – ?MitochondrionUniRule annotation

    Interactioni

    Protein-protein interaction databases

    STRINGi7217.FBpp0127326.

    Structurei

    3D structure databases

    ProteinModelPortaliB3M996.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

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

    Keywords - Domaini

    Transit peptide

    Phylogenomic databases

    eggNOGiCOG0320.
    InParanoidiB3M996.
    KOiK03644.
    OrthoDBiEOG7P2XS7.
    PhylomeDBiB3M996.

    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.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    B3M996-1 [UniParc]FASTAAdd to Basket

    « Hide

    MLRALKGHVE SPLIVVTRAA STNAEKLEEI RERLAKGPNF QDFVQNPDYS    50
    KSEWENYEGK LRREKGEEQR LRLPPWLKTT IPMGKNYAKI KNQLRELKLS 100
    TVCEEARCPN IGECWGGGEH GTQTATIMLM GDTCTRGCRF CSVKTARKPP 150
    PLDENEPVNT ATAIASWGLD YIVLTSVDRD DLPDGGSKHI AKTVKEIKAR 200
    NSNIFVECLV PDFRGDLGCV ETIANCGLDV YAHNIETVEK LTPYVRDRRA 250
    HYRQTLKVLS EAKRFNPNLI TKSSIMLGLG ETDEEVENTL KDLREAGVDC 300
    ITLGQYMQPT NKHLKVIEYV TPEKFKHWED RGNQLGFLYT ASGPLVRSSY 350
    KAGEFFITSI LENRKKRQAL NSKPEQ 376
    Length:376
    Mass (Da):42,549
    Last modified:September 2, 2008 - v1
    Checksum:i49136A35750CDB7C
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CH902618 Genomic DNA. Translation: EDV40080.1.
    RefSeqiXP_001957274.1. XM_001957238.1.

    Genome annotation databases

    EnsemblMetazoaiFBtr0128834; FBpp0127326; FBgn0101128.
    GeneIDi6506768.
    KEGGidan:Dana_GF24134.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CH902618 Genomic DNA. Translation: EDV40080.1 .
    RefSeqi XP_001957274.1. XM_001957238.1.

    3D structure databases

    ProteinModelPortali B3M996.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 7217.FBpp0127326.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblMetazoai FBtr0128834 ; FBpp0127326 ; FBgn0101128 .
    GeneIDi 6506768.
    KEGGi dan:Dana_GF24134.

    Organism-specific databases

    FlyBasei FBgn0101128. Dana\GF24134.

    Phylogenomic databases

    eggNOGi COG0320.
    InParanoidi B3M996.
    KOi K03644.
    OrthoDBi EOG7P2XS7.
    PhylomeDBi B3M996.

    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. "Evolution of genes and genomes on the Drosophila phylogeny."
      Drosophila 12 genomes consortium
      Nature 450:203-218(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: Tucson 14024-0371.13.

    Entry informationi

    Entry nameiLIAS_DROAN
    AccessioniPrimary (citable) accession number: B3M996
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 5, 2010
    Last sequence update: September 2, 2008
    Last modified: October 1, 2014
    This is version 37 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programDrosophila annotation project

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Drosophila
      Drosophila: entries, gene names and cross-references to FlyBase
    2. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3