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Q8FNP4

- LIPA_COREF

UniProt

Q8FNP4 - LIPA_COREF

Protein

Lipoyl synthase

Gene

lipA

Organism
Corynebacterium efficiens (strain DSM 44549 / YS-314 / AJ 12310 / JCM 11189 / NBRC 100395)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 77 (01 Oct 2014)
      Sequence version 1 (01 Mar 2003)
      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.UniRule annotation

    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 bindingi55 – 551Iron-sulfur 1 (4Fe-4S)UniRule annotation
    Metal bindingi60 – 601Iron-sulfur 1 (4Fe-4S)UniRule annotation
    Metal bindingi66 – 661Iron-sulfur 1 (4Fe-4S)UniRule annotation
    Metal bindingi81 – 811Iron-sulfur 2 (4Fe-4S-S-AdoMet)UniRule annotation
    Metal bindingi85 – 851Iron-sulfur 2 (4Fe-4S-S-AdoMet)UniRule annotation
    Metal bindingi88 – 881Iron-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

    BioCyciCEFF196164:GJW8-2136-MONOMER.
    UniPathwayiUPA00538; UER00593.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Lipoyl synthaseUniRule annotation (EC:2.8.1.8UniRule annotation)
    Alternative name(s):
    Lip-synUniRule annotation
    Short name:
    LSUniRule annotation
    Lipoate synthaseUniRule annotation
    Lipoic acid synthaseUniRule annotation
    Sulfur insertion protein LipAUniRule annotation
    Gene namesi
    Name:lipAUniRule annotation
    Ordered Locus Names:CE2100
    OrganismiCorynebacterium efficiens (strain DSM 44549 / YS-314 / AJ 12310 / JCM 11189 / NBRC 100395)
    Taxonomic identifieri196164 [NCBI]
    Taxonomic lineageiBacteriaActinobacteriaActinobacteridaeActinomycetalesCorynebacterineaeCorynebacteriaceaeCorynebacterium
    ProteomesiUP000001409: Chromosome

    Subcellular locationi

    Cytoplasm UniRule annotation

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cytoplasm

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 348348Lipoyl synthasePRO_0000102309Add
    BLAST

    Interactioni

    Protein-protein interaction databases

    STRINGi196164.CE2100.

    Structurei

    3D structure databases

    ProteinModelPortaliQ8FNP4.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

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

    Phylogenomic databases

    HOGENOMiHOG000235997.
    KOiK03644.
    OMAiEWLRRPI.
    OrthoDBiEOG6038ZS.

    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]

    Sequencei

    Sequence statusi: Complete.

    Q8FNP4-1 [UniParc]FASTAAdd to Basket

    « Hide

    MTIAPEGRRM LRVEARNSQT PIETKPRWIR NQVKNGPEYK DMKERVAGAS    50
    LHTVCQEAGC PNIHECWESR EATFLIGGAN CSRRCDFCMI NSARPEPLDR 100
    GEPLRVAESV REMRLNYSTI TGVTRDDLPD EGAWLYSEVV RKIHELNPNT 150
    GVENLVPDFS GKRDLLQEVF ESRPEVFAHN LETVPRIFKR IRPAFRYDRS 200
    LDVIRQARDF GLVTKSNLIL GMGETREEIS EALRDLHSAG TDIITITQYL 250
    RPGPLFHPIE RWVKPEEFLE LSDEAYEIGF AAVMSGPLVR SSYRAGKLYA 300
    QALKFRGEEL PANLSHLAET TEGPTTQEAS SLLERYGASE DAPVIPRG 348
    Length:348
    Mass (Da):39,384
    Last modified:March 1, 2003 - v1
    Checksum:i88847EB26A179C8F
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    BA000035 Genomic DNA. Translation: BAC18910.1.
    RefSeqiNP_738710.1. NC_004369.1.
    WP_011075761.1. NC_004369.1.

    Genome annotation databases

    EnsemblBacteriaiBAC18910; BAC18910; BAC18910.
    GeneIDi1034292.
    KEGGicef:CE2100.
    PATRICi21490335. VBICorEff9312_2082.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    BA000035 Genomic DNA. Translation: BAC18910.1 .
    RefSeqi NP_738710.1. NC_004369.1.
    WP_011075761.1. NC_004369.1.

    3D structure databases

    ProteinModelPortali Q8FNP4.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 196164.CE2100.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai BAC18910 ; BAC18910 ; BAC18910 .
    GeneIDi 1034292.
    KEGGi cef:CE2100.
    PATRICi 21490335. VBICorEff9312_2082.

    Phylogenomic databases

    HOGENOMi HOG000235997.
    KOi K03644.
    OMAi EWLRRPI.
    OrthoDBi EOG6038ZS.

    Enzyme and pathway databases

    UniPathwayi UPA00538 ; UER00593 .
    BioCyci CEFF196164:GJW8-2136-MONOMER.

    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 ]
    ProtoNeti Search...

    Publicationsi

    1. "Comparative complete genome sequence analysis of the amino acid replacements responsible for the thermostability of Corynebacterium efficiens."
      Nishio Y., Nakamura Y., Kawarabayasi Y., Usuda Y., Kimura E., Sugimoto S., Matsui K., Yamagishi A., Kikuchi H., Ikeo K., Gojobori T.
      Genome Res. 13:1572-1579(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: DSM 44549 / YS-314 / AJ 12310 / JCM 11189 / NBRC 100395.

    Entry informationi

    Entry nameiLIPA_COREF
    AccessioniPrimary (citable) accession number: Q8FNP4
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 10, 2004
    Last sequence update: March 1, 2003
    Last modified: October 1, 2014
    This is version 77 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic 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