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Q7JQW6

- LIAS_DROME

UniProt

Q7JQW6 - LIAS_DROME

Protein

Lipoyl synthase, mitochondrial

Gene

Las

Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 42 (01 Oct 2014)
      Sequence version 2 (05 Oct 2010)
      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.

    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:CG5231
    OrganismiDrosophila melanogaster (Fruit fly)
    Taxonomic identifieri7227 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
    ProteomesiUP000000803: Chromosome 3L

    Organism-specific databases

    FlyBaseiFBgn0029158. Las.

    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? – 377Lipoyl synthase, mitochondrialPRO_0000398219
    Transit peptidei1 – ?MitochondrionUniRule annotation

    Proteomic databases

    PaxDbiQ7JQW6.

    Expressioni

    Gene expression databases

    BgeeiQ7JQW6.

    Interactioni

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    CG11808Q7K1H51EBI-126542,EBI-159475

    Protein-protein interaction databases

    BioGridi65517. 1 interaction.
    IntActiQ7JQW6. 1 interaction.
    MINTiMINT-1650285.
    STRINGi7227.FBpp0288705.

    Structurei

    3D structure databases

    ProteinModelPortaliQ7JQW6.
    SMRiQ7JQW6. Positions 125-307.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

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

    Keywords - Domaini

    Transit peptide

    Phylogenomic databases

    eggNOGiCOG0320.
    GeneTreeiENSGT00390000006234.
    InParanoidiQ9VPF7.
    KOiK03644.
    OMAiPEEPYNT.
    OrthoDBiEOG7P2XS7.
    PhylomeDBiQ7JQW6.

    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.

    Q7JQW6-1 [UniParc]FASTAAdd to Basket

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    MLRALKTHAE APIVVATRAA STNAEKLEEI RERLAKGPNF HDFVQNPDNT    50
    RNEWEQYDGK LRREKGEEQR LRLPPWLKTT IPVGKNYAKI KAQMRELKLS 100
    TVCEEARCPN IGECWGGGEH GTQTATIMLM GDTCTRGCRF CSVKTARKPP 150
    PLDVNEPVNT ATAIASWGLD YIVLTSVDRD DLPDGGSEHI AETVREIKAR 200
    NSNIFVECLV PDFRGNLECV KTIANSGLDV YAHNIETVEK LTPYVRDRRA 250
    HYRQTLQVLT EAKRFNPNLI TKSSIMLGLG ETDEEIENTL KDLREAGVDC 300
    VTLGQYMQPT NKHLKVIEYV TPEKFKHWEE RGNELGFLYT ASGPLVRSSY 350
    KAGEFFITSI LENRKKRQND TEVPKKQ 377
    Length:377
    Mass (Da):42,734
    Last modified:October 5, 2010 - v2
    Checksum:iE702B1AB55DD5DC3
    GO

    Sequence cautioni

    The sequence AAL13786.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.
    The sequence AAO41414.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AE014296 Genomic DNA. Translation: AAF51596.2.
    AY058557 mRNA. Translation: AAL13786.1. Different initiation.
    BT003750 mRNA. Translation: AAO41414.1. Different initiation.
    RefSeqiNP_524183.2. NM_079459.3.
    UniGeneiDm.2512.

    Genome annotation databases

    EnsemblMetazoaiFBtr0290266; FBpp0288705; FBgn0029158.
    GeneIDi40259.
    KEGGidme:Dmel_CG5231.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AE014296 Genomic DNA. Translation: AAF51596.2 .
    AY058557 mRNA. Translation: AAL13786.1 . Different initiation.
    BT003750 mRNA. Translation: AAO41414.1 . Different initiation.
    RefSeqi NP_524183.2. NM_079459.3.
    UniGenei Dm.2512.

    3D structure databases

    ProteinModelPortali Q7JQW6.
    SMRi Q7JQW6. Positions 125-307.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 65517. 1 interaction.
    IntActi Q7JQW6. 1 interaction.
    MINTi MINT-1650285.
    STRINGi 7227.FBpp0288705.

    Proteomic databases

    PaxDbi Q7JQW6.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblMetazoai FBtr0290266 ; FBpp0288705 ; FBgn0029158 .
    GeneIDi 40259.
    KEGGi dme:Dmel_CG5231.

    Organism-specific databases

    CTDi 40259.
    FlyBasei FBgn0029158. Las.

    Phylogenomic databases

    eggNOGi COG0320.
    GeneTreei ENSGT00390000006234.
    InParanoidi Q9VPF7.
    KOi K03644.
    OMAi PEEPYNT.
    OrthoDBi EOG7P2XS7.
    PhylomeDBi Q7JQW6.

    Enzyme and pathway databases

    UniPathwayi UPA00538 ; UER00593 .

    Miscellaneous databases

    GenomeRNAii 40259.
    NextBioi 817833.
    PROi Q7JQW6.

    Gene expression databases

    Bgeei Q7JQW6.

    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. "The genome sequence of Drosophila melanogaster."
      Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., Sutton G.G., Wortman J.R., Yandell M.D.
      , Zhang Q., Chen L.X., Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J., Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.
      Science 287:2185-2195(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: Berkeley.
    2. Cited for: GENOME REANNOTATION.
      Strain: Berkeley.
    3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: Berkeley.
      Tissue: Embryo.
    4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: Berkeley.

    Entry informationi

    Entry nameiLIAS_DROME
    AccessioniPrimary (citable) accession number: Q7JQW6
    Secondary accession number(s): Q9VPF7
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 5, 2010
    Last sequence update: October 5, 2010
    Last modified: October 1, 2014
    This is version 42 of the entry and version 2 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