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C1GFM3

- LIPA_PARBD

UniProt

C1GFM3 - LIPA_PARBD

Protein

Lipoyl synthase, mitochondrial

Gene

PADG_06059

Organism
Paracoccidioides brasiliensis (strain Pb18)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 30 (01 Oct 2014)
      Sequence version 1 (26 May 2009)
      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 bindingi148 – 1481Iron-sulfur 1 (4Fe-4S)UniRule annotation
    Metal bindingi153 – 1531Iron-sulfur 1 (4Fe-4S)UniRule annotation
    Metal bindingi159 – 1591Iron-sulfur 1 (4Fe-4S)UniRule annotation
    Metal bindingi179 – 1791Iron-sulfur 2 (4Fe-4S-S-AdoMet)UniRule annotation
    Metal bindingi183 – 1831Iron-sulfur 2 (4Fe-4S-S-AdoMet)UniRule annotation
    Metal bindingi186 – 1861Iron-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
    ORF Names:PADG_06059
    OrganismiParacoccidioides brasiliensis (strain Pb18)
    Taxonomic identifieri502780 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeOnygenalesmitosporic OnygenalesParacoccidioides
    ProteomesiUP000001628: Unassembled WGS sequence

    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
    Transit peptidei1 – 3131MitochondrionUniRule annotationAdd
    BLAST
    Chaini32 – 438407Lipoyl synthase, mitochondrialPRO_0000398278Add
    BLAST

    Structurei

    3D structure databases

    ProteinModelPortaliC1GFM3.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

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

    Keywords - Domaini

    Transit peptide

    Phylogenomic databases

    OrthoDBiEOG79KPR7.

    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]
    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.

    C1GFM3-1 [UniParc]FASTAAdd to Basket

    « Hide

    MAASARGLRT LQSAHSSTTV PRLQLAVSRC YATTTSPDPP ITNSSNSSNS    50
    SNSTPTPKQR ITAFKDKLNA GPSFSDFVSG GGGGGASNDR VPLDPAEAYA 100
    LKTALVGPPG RKKQIIRLPS WLKTPIPDTP NYRRIKSDLR GLNLHTVCEE 150
    ARCPNISDCW GGSSKSAATA TIMLMGDTCT RGCRFCSVKT SRTPPPLDPH 200
    EPENTAEALS RWGLGYVVMT SVDRDDLADG GARHVVETVR KVKQKAPGIL 250
    LECLTGDYAG DLEMVALVAT SGLDVFAHNV ETVEALTPFV RDRRATFQQS 300
    LRVLKAAKEA RPELITKTSI MLGLGETETQ LWETLRALRA VDVDVVTFGQ 350
    YMRPTKRHMA VHEYVRPEVF DLWKERALEM GFLYCASGPL VRSSYKAGEA 400
    FIENVLKKRR GEGADGGDGG NSTRREDVER LVAGGVVR 438
    Length:438
    Mass (Da):47,521
    Last modified:May 26, 2009 - v1
    Checksum:i348C53B8A25B3F3C
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    DS572756 Genomic DNA. Translation: EEH49980.1.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    DS572756 Genomic DNA. Translation: EEH49980.1 .

    3D structure databases

    ProteinModelPortali C1GFM3.
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Phylogenomic databases

    OrthoDBi EOG79KPR7.

    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 ]
    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: Pb18.

    Entry informationi

    Entry nameiLIPA_PARBD
    AccessioniPrimary (citable) accession number: C1GFM3
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 5, 2010
    Last sequence update: May 26, 2009
    Last modified: October 1, 2014
    This is version 30 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programFungal 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