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Q86G50

- LIPA_TOXGO

UniProt

Q86G50 - LIPA_TOXGO

Protein

Lipoyl synthase, apicoplast

Gene

lipA

Organism
Toxoplasma gondii
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 49 (01 Oct 2014)
      Sequence version 1 (01 Jun 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.1 PublicationUniRule 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.

    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 bindingi252 – 2521Iron-sulfur 1 (4Fe-4S)UniRule annotation
    Metal bindingi257 – 2571Iron-sulfur 1 (4Fe-4S)UniRule annotation
    Metal bindingi263 – 2631Iron-sulfur 1 (4Fe-4S)UniRule annotation
    Metal bindingi278 – 2781Iron-sulfur 2 (4Fe-4S-S-AdoMet)UniRule annotation
    Metal bindingi282 – 2821Iron-sulfur 2 (4Fe-4S-S-AdoMet)UniRule annotation
    Metal bindingi285 – 2851Iron-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

    UniPathwayiUPA00538; UER00593.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Lipoyl synthase, apicoplastUniRule annotation (EC:2.8.1.8UniRule annotation)
    Alternative name(s):
    Lipoate synthaseUniRule annotation
    Short name:
    LSUniRule annotation
    Short name:
    Lip-synUniRule annotation
    Lipoic acid synthaseUniRule annotation
    Gene namesi
    Name:lipAUniRule annotation
    OrganismiToxoplasma gondii
    Taxonomic identifieri5811 [NCBI]
    Taxonomic lineageiEukaryotaAlveolataApicomplexaConoidasidaCoccidiaEucoccidioridaEimeriorinaSarcocystidaeToxoplasma

    Subcellular locationi

    Plastidapicoplast 1 PublicationUniRule annotation

    GO - Cellular componenti

    1. apicoplast Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Apicoplast, Plastid

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 6363UniRule annotationAdd
    BLAST
    Chaini64 – 543480Lipoyl synthase, apicoplastPRO_0000398234Add
    BLAST

    Structurei

    3D structure databases

    ProteinModelPortaliQ86G50.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

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

    Keywords - Domaini

    Signal

    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]
    SMARTiSM00729. Elp3. 1 hit.
    [Graphical view]
    TIGRFAMsiTIGR00510. lipA. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    Q86G50-1 [UniParc]FASTAAdd to Basket

    « Hide

    MAYFFDFPTD TWVEDASPGG PPKRAFGHGL AAGSSHFASP VSRRRLPTIT    50
    ALLLFSLLSA SQSGALSVSQ CSRRVSLGPL LSRVSSVSCT PSAAASALAS 100
    SLYPTDSLSS VEGSVAPRPP PSSLAFVLRR VPPAAYSSSL SPSVLRFKHS 150
    LPRPLQGSLV CAPGILGGAA GSARFAGCCG SQGRSCGSGK NPELPLKGSK 200
    DEVIPRVGTS TAGPRPDWFH VPAPQAASRG AEESRYQQLQ KQIRGLDLHT 250
    VCEEAKCPNI GECWNGGTAT LILLGDTCTR GCRFCAIKTS SKPPPPDPLE 300
    PEKVADAVAK WDIDYVVMTS VDRDDMPDGG AGHFARTVQL VKKAKPSMLI 350
    ECLVSDFQGM EESVRTLAQS GLDVYAHNIE TVRRLTPYVR DKRAKYDQSL 400
    RVLHLAKQFN PSLFTKSSIM LGLGETSEEV VRTLRDLRDH DVDVVTLGQY 450
    LRPTKQQLGV VEYVTPETFK KYQDIAEEMG FKYVASGPLV RSSYKAGEYY 500
    MKHLIDDARK HGRRETVKQV KLEADVGTLK GTTTTFQVNE KEA 543
    Length:543
    Mass (Da):58,706
    Last modified:June 1, 2003 - v1
    Checksum:i1DDCD0A1150680E6
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AJ556158 mRNA. Translation: CAD88789.1.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AJ556158 mRNA. Translation: CAD88789.1 .

    3D structure databases

    ProteinModelPortali Q86G50.
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Enzyme and pathway databases

    UniPathwayi UPA00538 ; UER00593 .

    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 ]
    SMARTi SM00729. Elp3. 1 hit.
    [Graphical view ]
    TIGRFAMsi TIGR00510. lipA. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. "Apicomplexan parasites contain a single lipoic acid synthase located in the plastid."
      Thomsen-Zieger N., Schachtner J., Seeber F.
      FEBS Lett. 547:80-86(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION.
      Strain: RH.

    Entry informationi

    Entry nameiLIPA_TOXGO
    AccessioniPrimary (citable) accession number: Q86G50
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 5, 2010
    Last sequence update: June 1, 2003
    Last modified: October 1, 2014
    This is version 49 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)

    Miscellaneousi

    Documents

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

    External Data

    Dasty 3