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Q9PJI2

- LIPA_CHLMU

UniProt

Q9PJI2 - LIPA_CHLMU

Protein

Lipoyl synthase

Gene

lipA

Organism
Chlamydia muridarum (strain MoPn / Nigg)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 97 (01 Oct 2014)
      Sequence version 1 (01 Oct 2000)
      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 bindingi48 – 481Iron-sulfur 1 (4Fe-4S)UniRule annotation
    Metal bindingi53 – 531Iron-sulfur 1 (4Fe-4S)UniRule annotation
    Metal bindingi59 – 591Iron-sulfur 1 (4Fe-4S)UniRule annotation
    Metal bindingi74 – 741Iron-sulfur 2 (4Fe-4S-S-AdoMet)UniRule annotation
    Metal bindingi78 – 781Iron-sulfur 2 (4Fe-4S-S-AdoMet)UniRule annotation
    Metal bindingi81 – 811Iron-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

    BioCyciCMUR243161:GHYU-877-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:TC_0847
    OrganismiChlamydia muridarum (strain MoPn / Nigg)
    Taxonomic identifieri243161 [NCBI]
    Taxonomic lineageiBacteriaChlamydiaeChlamydialesChlamydiaceaeChlamydia/Chlamydophila groupChlamydia
    ProteomesiUP000000800: 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 – 308308Lipoyl synthasePRO_0000102303Add
    BLAST

    Interactioni

    Protein-protein interaction databases

    STRINGi243161.TC0847.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9PJI2.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

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

    Phylogenomic databases

    eggNOGiCOG0320.
    KOiK03644.
    OMAiRPMMSET.
    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.

    Q9PJI2-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSNSPESSTP KQSIPARFPK WLRQKLPLGK VFSRTDGTIK NKGLPTVCEE    50
    ASCPNRTHCW SRHTATYLAL GDACTRRCGF CDIDFTKKPL PPDPQEGEKI 100
    AASAKALGLK HIVITMVSRD DLEDGGADAL ARIITTLHIE LPEATIEVLA 150
    SDFEGNIDAL HHLLDARIAI YNHNVETVER LSPLVRHKAT YRRSLMMLEQ 200
    AAQYLPDLMI KSGIMVGLGE QESEIKQTLK DLADHGVKIV TIGQYLRPSR 250
    RHIPVKSYVS PETFDYYRSV GEALGLFIYA GPFVRSSFNA DAVFEAMSQR 300
    ERLSASIQ 308
    Length:308
    Mass (Da):34,278
    Last modified:October 1, 2000 - v1
    Checksum:i617846CB79C12A92
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AE002160 Genomic DNA. Translation: AAF39645.1.
    PIRiC81658.
    RefSeqiNP_297220.1. NC_002620.2.

    Genome annotation databases

    EnsemblBacteriaiAAF39645; AAF39645; TC_0847.
    GeneIDi1246215.
    KEGGicmu:TC_0847.
    PATRICi20373208. VBIChlMur19118_0908.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AE002160 Genomic DNA. Translation: AAF39645.1 .
    PIRi C81658.
    RefSeqi NP_297220.1. NC_002620.2.

    3D structure databases

    ProteinModelPortali Q9PJI2.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 243161.TC0847.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAF39645 ; AAF39645 ; TC_0847 .
    GeneIDi 1246215.
    KEGGi cmu:TC_0847.
    PATRICi 20373208. VBIChlMur19118_0908.

    Phylogenomic databases

    eggNOGi COG0320.
    KOi K03644.
    OMAi RPMMSET.
    OrthoDBi EOG6038ZS.

    Enzyme and pathway databases

    UniPathwayi UPA00538 ; UER00593 .
    BioCyci CMUR243161:GHYU-877-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: MoPn / Nigg.

    Entry informationi

    Entry nameiLIPA_CHLMU
    AccessioniPrimary (citable) accession number: Q9PJI2
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: June 1, 2001
    Last sequence update: October 1, 2000
    Last modified: October 1, 2014
    This is version 97 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

    Documents

    1. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3