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Q6CLS2

- LIPA_KLULA

UniProt

Q6CLS2 - LIPA_KLULA

Protein

Lipoyl synthase, mitochondrial

Gene

KLLA0F00836g

Organism
Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37) (Yeast) (Candida sphaerica)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 71 (01 Oct 2014)
      Sequence version 1 (16 Aug 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 bindingi104 – 1041Iron-sulfur 1 (4Fe-4S)UniRule annotation
    Metal bindingi109 – 1091Iron-sulfur 1 (4Fe-4S)UniRule annotation
    Metal bindingi115 – 1151Iron-sulfur 1 (4Fe-4S)UniRule annotation
    Metal bindingi135 – 1351Iron-sulfur 2 (4Fe-4S-S-AdoMet)UniRule annotation
    Metal bindingi139 – 1391Iron-sulfur 2 (4Fe-4S-S-AdoMet)UniRule annotation
    Metal bindingi142 – 1421Iron-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
    Ordered Locus Names:KLLA0F00836g
    OrganismiKluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37) (Yeast) (Candida sphaerica)
    Taxonomic identifieri284590 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeKluyveromyces
    ProteomesiUP000000598: Chromosome F

    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? – 370Lipoyl synthase, mitochondrialPRO_0000398268
    Transit peptidei1 – ?MitochondrionUniRule annotation

    Interactioni

    Protein-protein interaction databases

    STRINGi28985.Q6CLS2.

    Structurei

    3D structure databases

    ProteinModelPortaliQ6CLS2.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

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

    Keywords - Domaini

    Transit peptide

    Phylogenomic databases

    eggNOGiCOG0320.
    HOGENOMiHOG000235998.
    KOiK03644.
    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.

    Q6CLS2-1 [UniParc]FASTAAdd to Basket

    « Hide

    MLKPGIRSVQ KRFITETVVR STQPSVSRRR KTTHFTDKLN KGPSFEDFVN    50
    GNAQKFTLDP LEKARQNSEE VQRLPTWLKV PIAKGSNFHK LKNDVKELKL 100
    STVCEEAKCP NIGECWGGGD KSKATATIML LGDTCTRGCR FCSVKTNRKP 150
    SAPDPTEPEN TAEAISRWGL GYVVLTTVDR DDLVDGGAYH LAETVQKIKQ 200
    KAPNILVETL SGDFRGDLEM VKVMALSGLD VYAHNMETVE ALTPHVRDRR 250
    ATYRQSLSVL ECAKKTVPTL VTKTSVMLGL GETDEQVLQT MKDLRAIGCD 300
    VITFGQYMRP TKRHMKVVEY VTPEKFDYWK QKALELGFLY CASGPLVRSS 350
    YKAGESFIEN VLRGRSRARI 370
    Length:370
    Mass (Da):41,470
    Last modified:August 16, 2004 - v1
    Checksum:i86A501949025496B
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CR382126 Genomic DNA. Translation: CAG97824.1.
    RefSeqiXP_455117.1. XM_455117.1.

    Genome annotation databases

    GeneIDi2895837.
    KEGGikla:KLLA0F00836g.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CR382126 Genomic DNA. Translation: CAG97824.1 .
    RefSeqi XP_455117.1. XM_455117.1.

    3D structure databases

    ProteinModelPortali Q6CLS2.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 28985.Q6CLS2.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 2895837.
    KEGGi kla:KLLA0F00836g.

    Phylogenomic databases

    eggNOGi COG0320.
    HOGENOMi HOG000235998.
    KOi K03644.
    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...

    Entry informationi

    Entry nameiLIPA_KLULA
    AccessioniPrimary (citable) accession number: Q6CLS2
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 5, 2010
    Last sequence update: August 16, 2004
    Last modified: October 1, 2014
    This is version 71 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