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A9R703

- LIPA_YERPG

UniProt

A9R703 - LIPA_YERPG

Protein

Lipoyl synthase

Gene

lipA

Organism
Yersinia pestis bv. Antiqua (strain Angola)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 52 (01 Oct 2014)
      Sequence version 1 (05 Feb 2008)
      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 bindingi68 – 681Iron-sulfur 1 (4Fe-4S)UniRule annotation
    Metal bindingi73 – 731Iron-sulfur 1 (4Fe-4S)UniRule annotation
    Metal bindingi79 – 791Iron-sulfur 1 (4Fe-4S)UniRule annotation
    Metal bindingi94 – 941Iron-sulfur 2 (4Fe-4S-S-AdoMet)UniRule annotation
    Metal bindingi98 – 981Iron-sulfur 2 (4Fe-4S-S-AdoMet)UniRule annotation
    Metal bindingi101 – 1011Iron-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

    BioCyciYPES349746:GHPB-1862-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:YpAngola_A1855
    OrganismiYersinia pestis bv. Antiqua (strain Angola)
    Taxonomic identifieri349746 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeYersinia
    ProteomesiUP000001204: 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 – 321321Lipoyl synthasePRO_1000099647Add
    BLAST

    Interactioni

    Protein-protein interaction databases

    STRINGi349746.YpAngola_A1855.

    Structurei

    3D structure databases

    ProteinModelPortaliA9R703.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

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

    Phylogenomic databases

    eggNOGiCOG0320.
    HOGENOMiHOG000235997.
    KOiK03644.
    OMAiHPHIPTK.
    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.

    A9R703-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSKPIQMERG VKYRDADKMA LIPVKNVVTE RQELLRKPEW LKIKLPTDSS    50
    RIQGIKAAMR KNGLHSVCEE ASCPNLSECF NHGTATFMIL GAICTRRCPF 100
    CDVAHGRPVT PDANEPEKLA QTIQDMGLRY VVITSVDRDD LRDGGAQHFA 150
    DCISAIRAKN PTIKIETLVP DFRGRMDRAL DILTATPPDV FNHNLENVPR 200
    VYRQVRPGAN YDWSLKLLER FKEAHPDIPT KSGLMVGLGE TNAEIVEVMH 250
    DLRRHGVTML TLGQYLQPSR HHLPVQRYVS PAEFDEMKAE AMAMGFTHAA 300
    CGPFVRSSYH ADLQAKGMEV K 321
    Length:321
    Mass (Da):36,086
    Last modified:February 5, 2008 - v1
    Checksum:iABA14E24EA640399
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000901 Genomic DNA. Translation: ABX87091.1.
    RefSeqiYP_001606342.1. NC_010159.1.

    Genome annotation databases

    EnsemblBacteriaiABX87091; ABX87091; YpAngola_A1855.
    GeneIDi5800326.
    KEGGiypg:YpAngola_A1855.
    PATRICi18572938. VBIYerPes97331_2253.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000901 Genomic DNA. Translation: ABX87091.1 .
    RefSeqi YP_001606342.1. NC_010159.1.

    3D structure databases

    ProteinModelPortali A9R703.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 349746.YpAngola_A1855.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai ABX87091 ; ABX87091 ; YpAngola_A1855 .
    GeneIDi 5800326.
    KEGGi ypg:YpAngola_A1855.
    PATRICi 18572938. VBIYerPes97331_2253.

    Phylogenomic databases

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

    Enzyme and pathway databases

    UniPathwayi UPA00538 ; UER00593 .
    BioCyci YPES349746:GHPB-1862-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. "Genome sequence of the deep-rooted Yersinia pestis strain Angola reveals new insights into the evolution and pangenome of the plague bacterium."
      Eppinger M., Worsham P.L., Nikolich M.P., Riley D.R., Sebastian Y., Mou S., Achtman M., Lindler L.E., Ravel J.
      J. Bacteriol. 192:1685-1699(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: Angola.

    Entry informationi

    Entry nameiLIPA_YERPG
    AccessioniPrimary (citable) accession number: A9R703
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: March 24, 2009
    Last sequence update: February 5, 2008
    Last modified: October 1, 2014
    This is version 52 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