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Q4DYL7

- LIPA2_TRYCC

UniProt

Q4DYL7 - LIPA2_TRYCC

Protein

Lipoyl synthase 2, mitochondrial

Gene

Tc00.1047053506211.10

Organism
Trypanosoma cruzi (strain CL Brener)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 49 (01 Oct 2014)
      Sequence version 1 (13 Sep 2005)
      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.

    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 bindingi127 – 1271Iron-sulfur 1 (4Fe-4S)UniRule annotation
    Metal bindingi132 – 1321Iron-sulfur 1 (4Fe-4S)UniRule annotation
    Metal bindingi138 – 1381Iron-sulfur 1 (4Fe-4S)UniRule annotation
    Metal bindingi159 – 1591Iron-sulfur 2 (4Fe-4S-S-AdoMet)UniRule annotation
    Metal bindingi163 – 1631Iron-sulfur 2 (4Fe-4S-S-AdoMet)UniRule annotation
    Metal bindingi166 – 1661Iron-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 2, mitochondrial (EC:2.8.1.8UniRule annotation)
    Alternative name(s):
    Lipoate synthase 2UniRule annotation
    Short name:
    LS 2UniRule annotation
    Short name:
    Lip-syn 2UniRule annotation
    Lipoic acid synthase 2UniRule annotation
    Gene namesi
    ORF Names:Tc00.1047053506211.10
    OrganismiTrypanosoma cruzi (strain CL Brener)
    Taxonomic identifieri353153 [NCBI]
    Taxonomic lineageiEukaryotaEuglenozoaKinetoplastidaTrypanosomatidaeTrypanosomaSchizotrypanum
    ProteomesiUP000002296: Unassembled WGS sequence

    Subcellular locationi

    Mitochondrion UniRule annotation

    GO - Cellular componenti

    1. mitochondrion Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Mitochondrion

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini? – 431Lipoyl synthase 2, mitochondrialPRO_0000398242
    Transit peptidei1 – ?MitochondrionUniRule annotation

    Structurei

    3D structure databases

    ProteinModelPortaliQ4DYL7.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

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

    Keywords - Domaini

    Transit peptide

    Phylogenomic databases

    KOiK03644.

    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.

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

    Q4DYL7-1 [UniParc]FASTAAdd to Basket

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    MFHRHLCKLC SKTPSAATLA SPLGKLQEER GEGVAKDPKK DKQHRQIFLQ    50
    KFRERLDSDT TGKNTLAGFI DLPEGISPTM AAVGPLKRGE EPLPPWLKMK 100
    VAKGVSRLPR FNRIRNSMRE KRLATVCEEA KCPNIGECWG GDEEEGTATA 150
    TIMVMGSHCT RGCRFCSVLT SRTPPPLDPD EPQKVANAVA EMGVDYIVMT 200
    MVDRDDLTDG GAAHVVRCVN TIKEKNPLLL LEALVGDFHG DLKLVETVAL 250
    SPLSVYAHNI ECVERITPNV RDRRASYRQS LKVLEHVNSF TKGAMLTKSS 300
    IMLGLGEKEE EVRQTLRDLR TAGVSAVTLG QYLQPARTRL KVSRYAHPKE 350
    FQMWEEEAMA MGFLYCASGP LVRSSYRAGE YYIKSLVKQR GAAATKSNTT 400
    TTTTTTTTTT TTNTASLAAA TVTDSATLQG E 431
    Length:431
    Mass (Da):47,395
    Last modified:September 13, 2005 - v1
    Checksum:i0A657B825EEC52C0
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AAHK01000092 Genomic DNA. Translation: EAN97594.1.
    RefSeqiXP_819445.1. XM_814352.1.

    Genome annotation databases

    GeneIDi3551901.
    KEGGitcr:506211.10.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AAHK01000092 Genomic DNA. Translation: EAN97594.1 .
    RefSeqi XP_819445.1. XM_814352.1.

    3D structure databases

    ProteinModelPortali Q4DYL7.
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 3551901.
    KEGGi tcr:506211.10.

    Phylogenomic databases

    KOi K03644.

    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 ]
    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 Trypanosoma cruzi, etiologic agent of Chagas disease."
      El-Sayed N.M.A., Myler P.J., Bartholomeu D.C., Nilsson D., Aggarwal G., Tran A.-N., Ghedin E., Worthey E.A., Delcher A.L., Blandin G., Westenberger S.J., Caler E., Cerqueira G.C., Branche C., Haas B., Anupama A., Arner E., Aslund L.
      , Attipoe P., Bontempi E., Bringaud F., Burton P., Cadag E., Campbell D.A., Carrington M., Crabtree J., Darban H., da Silveira J.F., de Jong P., Edwards K., Englund P.T., Fazelina G., Feldblyum T., Ferella M., Frasch A.C., Gull K., Horn D., Hou L., Huang Y., Kindlund E., Klingbeil M., Kluge S., Koo H., Lacerda D., Levin M.J., Lorenzi H., Louie T., Machado C.R., McCulloch R., McKenna A., Mizuno Y., Mottram J.C., Nelson S., Ochaya S., Osoegawa K., Pai G., Parsons M., Pentony M., Pettersson U., Pop M., Ramirez J.L., Rinta J., Robertson L., Salzberg S.L., Sanchez D.O., Seyler A., Sharma R., Shetty J., Simpson A.J., Sisk E., Tammi M.T., Tarleton R., Teixeira S., Van Aken S., Vogt C., Ward P.N., Wickstead B., Wortman J., White O., Fraser C.M., Stuart K.D., Andersson B.
      Science 309:409-415(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: CL Brener.

    Entry informationi

    Entry nameiLIPA2_TRYCC
    AccessioniPrimary (citable) accession number: Q4DYL7
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 5, 2010
    Last sequence update: September 13, 2005
    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

    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