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Q72YB2

- LIPA_BACC1

UniProt

Q72YB2 - LIPA_BACC1

Protein

Lipoyl synthase

Gene

lipA

Organism
Bacillus cereus (strain ATCC 10987)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 74 (01 Oct 2014)
      Sequence version 1 (05 Jul 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.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

    Protein modification; protein lipoylation via endogenous pathway; protein N(6)-(lipoyl)lysine from octanoyl-[acyl-carrier-protein].

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi40 – 401Iron-sulfur 1 (4Fe-4S)UniRule annotation
    Metal bindingi45 – 451Iron-sulfur 1 (4Fe-4S)UniRule annotation
    Metal bindingi51 – 511Iron-sulfur 1 (4Fe-4S)UniRule annotation
    Metal bindingi67 – 671Iron-sulfur 2 (4Fe-4S-S-AdoMet)UniRule annotation
    Metal bindingi71 – 711Iron-sulfur 2 (4Fe-4S-S-AdoMet)UniRule annotation
    Metal bindingi74 – 741Iron-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

    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:BCE_5109
    OrganismiBacillus cereus (strain ATCC 10987)
    Taxonomic identifieri222523 [NCBI]
    Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillusBacillus cereus group
    ProteomesiUP000002527: 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 – 298298Lipoyl synthasePRO_1000012185Add
    BLAST

    Interactioni

    Protein-protein interaction databases

    STRINGi222523.BCE_5109.

    Structurei

    3D structure databases

    ProteinModelPortaliQ72YB2.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

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

    Phylogenomic databases

    eggNOGiCOG0320.
    HOGENOMiHOG000235998.
    KOiK03644.
    OMAiHTICQEA.
    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.

    Q72YB2-1 [UniParc]FASTAAdd to Basket

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    MTKQTEYKRK PEWLKIKLNT NENYTGLKKM MRSKNLHTVC EEAKCPNIHE    50
    CWAVRKTATF MILGAVCTRA CRFCAVKTGL PTELDLQEPE RVADSVVQMG 100
    LKHVVITAVA RDDLKDGGAA VFAETVRAVR RKNPFTSIEV LPSDMGGVEE 150
    NLKMLMDAKP DILNHNIETV RRLSDRVRAR AKYDRSLEFL RRAKEMQPDI 200
    PTKSSIMVGL GETREDLIEA MDDLRANNVD ILTLGQYLQP SKKHLPVLKY 250
    YPPAEFAELK EIALSKGFSH CEAGPLVRSS YHADEQVRSA KENTAEAK 298
    Length:298
    Mass (Da):33,688
    Last modified:July 5, 2004 - v1
    Checksum:i64FB54F922A98774
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AE017194 Genomic DNA. Translation: AAS44010.1.
    RefSeqiNP_981402.1. NC_003909.8.

    Genome annotation databases

    EnsemblBacteriaiAAS44010; AAS44010; BCE_5109.
    GeneIDi2748368.
    KEGGibca:BCE_5109.
    PATRICi18858850. VBIBacCer118379_4895.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AE017194 Genomic DNA. Translation: AAS44010.1 .
    RefSeqi NP_981402.1. NC_003909.8.

    3D structure databases

    ProteinModelPortali Q72YB2.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 222523.BCE_5109.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAS44010 ; AAS44010 ; BCE_5109 .
    GeneIDi 2748368.
    KEGGi bca:BCE_5109.
    PATRICi 18858850. VBIBacCer118379_4895.

    Phylogenomic databases

    eggNOGi COG0320.
    HOGENOMi HOG000235998.
    KOi K03644.
    OMAi HTICQEA.
    OrthoDBi EOG6038ZS.

    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. "The genome sequence of Bacillus cereus ATCC 10987 reveals metabolic adaptations and a large plasmid related to Bacillus anthracis pXO1."
      Rasko D.A., Ravel J., Oekstad O.A., Helgason E., Cer R.Z., Jiang L., Shores K.A., Fouts D.E., Tourasse N.J., Angiuoli S.V., Kolonay J.F., Nelson W.C., Kolstoe A.-B., Fraser C.M., Read T.D.
      Nucleic Acids Res. 32:977-988(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 10987.

    Entry informationi

    Entry nameiLIPA_BACC1
    AccessioniPrimary (citable) accession number: Q72YB2
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 15, 2008
    Last sequence update: July 5, 2004
    Last modified: October 1, 2014
    This is version 74 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