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P0CH68

- LIPA_CANAW

UniProt

P0CH68 - LIPA_CANAW

Protein

Lipoyl synthase, mitochondrial

Gene

LAB5

Organism
Candida albicans (strain WO-1) (Yeast)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 26 (01 Oct 2014)
      Sequence version 1 (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 bindingi107 – 1071Iron-sulfur 1 (4Fe-4S)UniRule annotation
    Metal bindingi112 – 1121Iron-sulfur 1 (4Fe-4S)UniRule annotation
    Metal bindingi118 – 1181Iron-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:LAB5
    Synonyms:LIS1
    ORF Names:CAWG_03565
    OrganismiCandida albicans (strain WO-1) (Yeast)
    Taxonomic identifieri294748 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesmitosporic SaccharomycetalesCandida
    ProteomesiUP000001429: Chromosome 4, Supercontig 1.4

    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 – 2121MitochondrionUniRule annotationAdd
    BLAST
    Chaini22 – 386365Lipoyl synthase, mitochondrialPRO_0000398257Add
    BLAST

    Structurei

    3D structure databases

    ProteinModelPortaliP0CH68.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

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

    Keywords - Domaini

    Transit peptide

    Phylogenomic databases

    OMAiHPHIPTK.
    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]
    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.

    P0CH68-1 [UniParc]FASTAAdd to Basket

    « Hide

    MISRNSILLR RLYPTTIIRT LATDATESTS VKTKRRRTIF TDELNKGPSF    50
    DDFVSGKAKD MLEDPLETAR KDPNAKLPSW LKVPIPKGKS FHNVKKDVRE 100
    LKLATVCEEA KCPNIGECWG GKKSEATATI MLLGDTCTRG CRFCSVKTNR 150
    KPAAPDPMEP ENTAEAISRW GLGYVVLTTV DRDDLVDGGA RHLAETVQKI 200
    KQKAPQILVE VLGGDFRGDL SMVEILADSG LDVYAHNLET VEALTPHIRD 250
    RRATYRQSLA VLERAKQTNS SLITKTSLML GFGETDDQVL QTLRDLREIG 300
    CDVVTFGQYM RPTKRHMKVV EYIKPEKFDY WRDTALDMGF LYVASGPLVR 350
    SSYKAGEAFI ENVLKKRKHN VGETPRLAQE IKPSIY 386
    Length:386
    Mass (Da):43,339
    Last modified:October 5, 2010 - v1
    Checksum:i84ACA0D6EAECC691
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CH672349 Genomic DNA. Translation: EEQ45249.1.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CH672349 Genomic DNA. Translation: EEQ45249.1 .

    3D structure databases

    ProteinModelPortali P0CH68.
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Phylogenomic databases

    OMAi HPHIPTK.
    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 ]
    PIRSFi PIRSF005963. Lipoyl_synth. 1 hit.
    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: WO-1.

    Entry informationi

    Entry nameiLIPA_CANAW
    AccessioniPrimary (citable) accession number: P0CH68
    Secondary accession number(s): C4YHL7, Q5AF33
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 5, 2010
    Last sequence update: October 5, 2010
    Last modified: October 1, 2014
    This is version 26 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