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C0SDG9

- LIPA_PARBP

UniProt

C0SDG9 - LIPA_PARBP

Protein

Lipoyl synthase, mitochondrial

Gene

PABG_05724

Organism
Paracoccidioides brasiliensis (strain Pb03)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 29 (01 Oct 2014)
      Sequence version 1 (05 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 bindingi144 – 1441Iron-sulfur 1 (4Fe-4S)UniRule annotation
    Metal bindingi149 – 1491Iron-sulfur 1 (4Fe-4S)UniRule annotation
    Metal bindingi155 – 1551Iron-sulfur 1 (4Fe-4S)UniRule annotation
    Metal bindingi175 – 1751Iron-sulfur 2 (4Fe-4S-S-AdoMet)UniRule annotation
    Metal bindingi179 – 1791Iron-sulfur 2 (4Fe-4S-S-AdoMet)UniRule annotation
    Metal bindingi182 – 1821Iron-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:PABG_05724
    OrganismiParacoccidioides brasiliensis (strain Pb03)
    Taxonomic identifieri482561 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeOnygenalesmitosporic OnygenalesParacoccidioides
    ProteomesiUP000002740: 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 – 434403Lipoyl synthase, mitochondrialPRO_0000398277Add
    BLAST

    Structurei

    3D structure databases

    ProteinModelPortaliC0SDG9.
    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.

    C0SDG9-1 [UniParc]FASTAAdd to Basket

    « Hide

    MAASARGLRT LQSAHSSTTV PRLQLAVSRC YATTTSPDPP ITNSSNSSNS    50
    TPTPKQRITA FKDKLNAGPS FSDFVSGGGG GASNDRVPLD PAEAYALKTA 100
    LVGPPGRKKQ IIRLPSWLKT PIPDTPNYRR IKSDLRGLNL HTVCEEARCP 150
    NISDCWGGSS KSAATATIML MGDTCTRGCR FCSVKTSRTP PPLDPHEPEN 200
    TAEALSRWGL GYVVMTSVDR DDLADGGARH VAETVRKVKQ KAPGILLECL 250
    TGDYAGDLEM VALVATSGLD VFAHNVETVE ALTPFVRDRR ATFQQSLRVL 300
    KAAKEARPEL ITKTSIMLGL GETETQLWET LRALRTVDVD VVTFGQYMRP 350
    TKRHMAVHEY VRPGVFDLWK ERALEMGFLY CASGPLVRSS YKAGEAFIEN 400
    VLKKRRGEGA DGGDGGNSTR REDVERLVAG GVVR 434
    Length:434
    Mass (Da):47,106
    Last modified:May 5, 2009 - v1
    Checksum:i02DABF6FB68CDDA9
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    DS544811 Genomic DNA. Translation: EEH23513.1.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    DS544811 Genomic DNA. Translation: EEH23513.1 .

    3D structure databases

    ProteinModelPortali C0SDG9.
    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: Pb03.

    Entry informationi

    Entry nameiLIPA_PARBP
    AccessioniPrimary (citable) accession number: C0SDG9
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 5, 2010
    Last sequence update: May 5, 2009
    Last modified: October 1, 2014
    This is version 29 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