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Q6GQ48

- LIAS_XENLA

UniProt

Q6GQ48 - LIAS_XENLA

Protein

Lipoyl synthase, mitochondrial

Gene

lias

Organism
Xenopus laevis (African clawed frog)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 60 (01 Oct 2014)
      Sequence version 1 (19 Jul 2004)
      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 bindingi106 – 1061Iron-sulfur 1 (4Fe-4S)UniRule annotation
    Metal bindingi111 – 1111Iron-sulfur 1 (4Fe-4S)UniRule annotation
    Metal bindingi117 – 1171Iron-sulfur 1 (4Fe-4S)UniRule annotation
    Metal bindingi137 – 1371Iron-sulfur 2 (4Fe-4S-S-AdoMet)UniRule annotation
    Metal bindingi141 – 1411Iron-sulfur 2 (4Fe-4S-S-AdoMet)UniRule annotation
    Metal bindingi144 – 1441Iron-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:lias
    OrganismiXenopus laevis (African clawed frog)
    Taxonomic identifieri8355 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiAmphibiaBatrachiaAnuraPipoideaPipidaeXenopodinaeXenopusXenopus

    Organism-specific databases

    XenbaseiXB-GENE-6251515. lias.

    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? – 372Lipoyl synthase, mitochondrialPRO_0000398212
    Transit peptidei1 – ?MitochondrionUniRule annotation

    Structurei

    3D structure databases

    ProteinModelPortaliQ6GQ48.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

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

    Keywords - Domaini

    Transit peptide

    Phylogenomic databases

    HOVERGENiHBG023328.
    KOiK03644.

    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.

    Q6GQ48-1 [UniParc]FASTAAdd to Basket

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    MRQCGLVRAA QLLRTCGLAE WHTPYRALSS LPDEKKELIK NGPDLQDFLS    50
    GELVDKSSWA AYKGDLKRQK GERLRLPPWV KTEIPMGKNY NKLKNTLRNL 100
    NLHTVCEEAR CPNIGECWGG GEYGTATATI MLMGDTCTRG CRFCSVKTAR 150
    NPPPLDPDEP YNTSKAIAEW GLDYVVLTSV DRDDISDGGA EHIAQTVSML 200
    KERNKTILIE CLTPDFRGNM KAVETVAKSG LDVYAHNVET VPALQRHVRD 250
    PRANFDQSLN VLKHAKNVRP DLVSKTSIML GLGETDEQIY STMKALREAG 300
    VDCLTLGQYM QPTKRHLKVE EYITPEKFKY WEKAGNELGF LYTASGPLVR 350
    SSYKAGEFFL KNLIEKRKTK AI 372
    Length:372
    Mass (Da):41,803
    Last modified:July 19, 2004 - v1
    Checksum:i905039EBFE3CC48C
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    BC072900 mRNA. Translation: AAH72900.1.
    RefSeqiNP_001085534.1. NM_001092065.1.
    UniGeneiXl.55041.

    Genome annotation databases

    GeneIDi443960.
    KEGGixla:443960.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    BC072900 mRNA. Translation: AAH72900.1 .
    RefSeqi NP_001085534.1. NM_001092065.1.
    UniGenei Xl.55041.

    3D structure databases

    ProteinModelPortali Q6GQ48.
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 443960.
    KEGGi xla:443960.

    Organism-specific databases

    CTDi 11019.
    Xenbasei XB-GENE-6251515. lias.

    Phylogenomic databases

    HOVERGENi HBG023328.
    KOi K03644.

    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. NIH - Xenopus Gene Collection (XGC) project
      Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Ovary.

    Entry informationi

    Entry nameiLIAS_XENLA
    AccessioniPrimary (citable) accession number: Q6GQ48
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 5, 2010
    Last sequence update: July 19, 2004
    Last modified: October 1, 2014
    This is version 60 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Documents

    1. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3