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Q0APQ9

- LIPA_MARMM

UniProt

Q0APQ9 - LIPA_MARMM

Protein

Lipoyl synthase

Gene

lipA

Organism
Maricaulis maris (strain MCS10)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 60 (01 Oct 2014)
      Sequence version 1 (17 Oct 2006)
      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 bindingi65 – 651Iron-sulfur 1 (4Fe-4S)UniRule annotation
    Metal bindingi70 – 701Iron-sulfur 1 (4Fe-4S)UniRule annotation
    Metal bindingi76 – 761Iron-sulfur 1 (4Fe-4S)UniRule annotation
    Metal bindingi91 – 911Iron-sulfur 2 (4Fe-4S-S-AdoMet)UniRule annotation
    Metal bindingi95 – 951Iron-sulfur 2 (4Fe-4S-S-AdoMet)UniRule annotation
    Metal bindingi98 – 981Iron-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

    BioCyciMMAR394221:GHNB-1463-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:Mmar10_1436
    OrganismiMaricaulis maris (strain MCS10)
    Taxonomic identifieri394221 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaAlphaproteobacteriaRhodobacteralesHyphomonadaceaeMaricaulis
    ProteomesiUP000001964: 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 – 325325Lipoyl synthasePRO_0000325274Add
    BLAST

    Interactioni

    Protein-protein interaction databases

    STRINGi394221.Mmar10_1436.

    Structurei

    3D structure databases

    ProteinModelPortaliQ0APQ9.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

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

    Phylogenomic databases

    eggNOGiCOG0320.
    HOGENOMiHOG000235997.
    KOiK03644.
    OMAiTIRAVRH.
    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]
    TIGRFAMsiTIGR00510. lipA. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    Q0APQ9-1 [UniParc]FASTAAdd to Basket

    « Hide

    MANLIDNTAR SAASDARAAR HPEKQKRADT PVLRKPDWIR VKAPLGKTFS    50
    ETQKIVKDGG LVTVCEEAGC PNIGECWEQK HATFMILGDT CTRACSFCNV 100
    KTGLPAAVDT DEPRRVAEAV AQMGLNHVVI TSVDRDDLDD GGAQHFVDVI 150
    EAIRAATPST TIEILTPDFL RKPGAAEAVI DARPDVFNHN LETVPRLYLS 200
    IRPGARYFHS LRLLERVKDR DPAQFTKSGI MVGLGESKEE VMQVMDDMRS 250
    AGIDFLTIGQ YLQPTRKHAA VDRFVHPDEF KAYETIARAK GFLMVSATPL 300
    TRSSHHAGDD FAKLRAAREQ MMARG 325
    Length:325
    Mass (Da):35,867
    Last modified:October 17, 2006 - v1
    Checksum:i98F2586DF49E41FA
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000449 Genomic DNA. Translation: ABI65728.1.
    RefSeqiWP_011643375.1. NC_008347.1.
    YP_756666.1. NC_008347.1.

    Genome annotation databases

    EnsemblBacteriaiABI65728; ABI65728; Mmar10_1436.
    GeneIDi4285675.
    KEGGimmr:Mmar10_1436.
    PATRICi22450966. VBIMarMar77530_1473.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000449 Genomic DNA. Translation: ABI65728.1 .
    RefSeqi WP_011643375.1. NC_008347.1.
    YP_756666.1. NC_008347.1.

    3D structure databases

    ProteinModelPortali Q0APQ9.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 394221.Mmar10_1436.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai ABI65728 ; ABI65728 ; Mmar10_1436 .
    GeneIDi 4285675.
    KEGGi mmr:Mmar10_1436.
    PATRICi 22450966. VBIMarMar77530_1473.

    Phylogenomic databases

    eggNOGi COG0320.
    HOGENOMi HOG000235997.
    KOi K03644.
    OMAi TIRAVRH.
    OrthoDBi EOG6038ZS.

    Enzyme and pathway databases

    UniPathwayi UPA00538 ; UER00593 .
    BioCyci MMAR394221:GHNB-1463-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 ]
    TIGRFAMsi TIGR00510. lipA. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: MCS10.

    Entry informationi

    Entry nameiLIPA_MARMM
    AccessioniPrimary (citable) accession number: Q0APQ9
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: March 18, 2008
    Last sequence update: October 17, 2006
    Last modified: October 1, 2014
    This is version 60 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