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B9N2B0

- LISC2_POPTR

UniProt

B9N2B0 - LISC2_POPTR

Protein

Lipoyl synthase 2, chloroplastic

Gene

LIP1P-2

Organism
Populus trichocarpa (Western balsam poplar) (Populus balsamifera subsp. trichocarpa)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 43 (01 Oct 2014)
      Sequence version 1 (24 Mar 2009)
      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 bindingi128 – 1281Iron-sulfur 1 (4Fe-4S)UniRule annotation
    Metal bindingi133 – 1331Iron-sulfur 1 (4Fe-4S)UniRule annotation
    Metal bindingi139 – 1391Iron-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, chloroplastic (EC:2.8.1.8UniRule annotation)
    Alternative name(s):
    Lipoate synthase 2UniRule annotation
    Short name:
    LS 2UniRule annotation
    Short name:
    Lip-syn 2UniRule annotation
    Lipoate synthase, plastidial 2UniRule annotation
    Short name:
    LIP1p 2UniRule annotation
    Lipoic acid synthase 2UniRule annotation
    Gene namesi
    Name:LIP1P-2UniRule annotation
    ORF Names:POPTR_0019s13380g
    OrganismiPopulus trichocarpa (Western balsam poplar) (Populus balsamifera subsp. trichocarpa)
    Taxonomic identifieri3694 [NCBI]
    Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsfabidsMalpighialesSalicaceaeSaliceaePopulus
    ProteomesiUP000006729: Linkage group LGXIX, UP000006729: Unassembled WGS sequence

    Subcellular locationi

    Plastidchloroplast UniRule annotation

    GO - Cellular componenti

    1. chloroplast Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Chloroplast, Plastid

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transit peptidei1 – 3535ChloroplastUniRule annotationAdd
    BLAST
    Chaini36 – 397362Lipoyl synthase 2, chloroplasticPRO_0000398868Add
    BLAST

    Interactioni

    Protein-protein interaction databases

    STRINGi3694.fgenesh4_pg.C_scaffold_120000064.

    Structurei

    3D structure databases

    ProteinModelPortaliB9N2B0.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

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

    Keywords - Domaini

    Transit peptide

    Phylogenomic databases

    eggNOGiCOG0320.
    HOGENOMiHOG000235998.
    KOiK03644.
    OMAiRKVDCDI.

    Family and domain databases

    Gene3Di3.20.20.70. 1 hit.
    HAMAPiMF_00206. Lipoyl_synth.
    MF_03129. Lipoyl_synth_plantC.
    InterProiIPR013785. Aldolase_TIM.
    IPR006638. Elp3/MiaB/NifB.
    IPR003698. Lipoyl_synth.
    IPR027526. Lipoyl_synth_chlpt.
    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.

    B9N2B0-1 [UniParc]FASTAAdd to Basket

    « Hide

    MIEQSLSKPS FSLSIPIPKA PKSKSSFFCS YSKIRCESVD YPSLTKIDAK    50
    HPQNSTTINN GSSSSASVDL KNNEKGPYPY PGGGKMGPYT GRDLNEKKPE 100
    WLRQRAPQGE RFEEVKESIS RLNLNTVCQE AQCPNIGECW NGGGDGIATA 150
    TIMVLGDTCT RGCRFCAVKT SRTPPPPDPM EPLNTALAIA SWGVDYIVIT 200
    SVDRDDLSDG GSGHFAQTVR AMKELKPEIM VECLTSDFRG DLKAVDTLVH 250
    SGLDVFAHNV ETVKRLQRIV RDPRAGYEQS LSVLKHAKVS KKGMITKTSI 300
    MLGLGETDDE VKEAMTDLRA IDVDILTFGQ YLQPTPLHLT VKEYVSPEKF 350
    AYWKEYGESI GFRYVASGPL VRSSYRAGEL FVKTMVKESA KEAAAIS 397
    Length:397
    Mass (Da):43,638
    Last modified:March 24, 2009 - v1
    Checksum:iFC77A8FC05480DA9
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CM000355 Genomic DNA. Translation: ERP49380.1.
    RefSeqiXP_006371583.1. XM_006371521.1.

    Genome annotation databases

    EnsemblPlantsiPOPTR_0019s13380.1; POPTR_0019s13380.1; POPTR_0019s13380.
    GeneIDi18108579.
    KEGGipop:POPTR_0019s13380g.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CM000355 Genomic DNA. Translation: ERP49380.1 .
    RefSeqi XP_006371583.1. XM_006371521.1.

    3D structure databases

    ProteinModelPortali B9N2B0.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 3694.fgenesh4_pg.C_scaffold_120000064.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblPlantsi POPTR_0019s13380.1 ; POPTR_0019s13380.1 ; POPTR_0019s13380 .
    GeneIDi 18108579.
    KEGGi pop:POPTR_0019s13380g.

    Phylogenomic databases

    eggNOGi COG0320.
    HOGENOMi HOG000235998.
    KOi K03644.
    OMAi RKVDCDI.

    Enzyme and pathway databases

    UniPathwayi UPA00538 ; UER00593 .

    Family and domain databases

    Gene3Di 3.20.20.70. 1 hit.
    HAMAPi MF_00206. Lipoyl_synth.
    MF_03129. Lipoyl_synth_plantC.
    InterProi IPR013785. Aldolase_TIM.
    IPR006638. Elp3/MiaB/NifB.
    IPR003698. Lipoyl_synth.
    IPR027526. Lipoyl_synth_chlpt.
    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 of black cottonwood, Populus trichocarpa (Torr. & Gray)."
      Tuskan G.A., Difazio S., Jansson S., Bohlmann J., Grigoriev I., Hellsten U., Putnam N., Ralph S., Rombauts S., Salamov A., Schein J., Sterck L., Aerts A., Bhalerao R.R., Bhalerao R.P., Blaudez D., Boerjan W., Brun A.
      , Brunner A., Busov V., Campbell M., Carlson J., Chalot M., Chapman J., Chen G.-L., Cooper D., Coutinho P.M., Couturier J., Covert S., Cronk Q., Cunningham R., Davis J., Degroeve S., Dejardin A., dePamphilis C.W., Detter J., Dirks B., Dubchak I., Duplessis S., Ehlting J., Ellis B., Gendler K., Goodstein D., Gribskov M., Grimwood J., Groover A., Gunter L., Hamberger B., Heinze B., Helariutta Y., Henrissat B., Holligan D., Holt R., Huang W., Islam-Faridi N., Jones S., Jones-Rhoades M., Jorgensen R., Joshi C., Kangasjaervi J., Karlsson J., Kelleher C., Kirkpatrick R., Kirst M., Kohler A., Kalluri U., Larimer F., Leebens-Mack J., Leple J.-C., Locascio P., Lou Y., Lucas S., Martin F., Montanini B., Napoli C., Nelson D.R., Nelson C., Nieminen K., Nilsson O., Pereda V., Peter G., Philippe R., Pilate G., Poliakov A., Razumovskaya J., Richardson P., Rinaldi C., Ritland K., Rouze P., Ryaboy D., Schmutz J., Schrader J., Segerman B., Shin H., Siddiqui A., Sterky F., Terry A., Tsai C.-J., Uberbacher E., Unneberg P., Vahala J., Wall K., Wessler S., Yang G., Yin T., Douglas C., Marra M., Sandberg G., Van de Peer Y., Rokhsar D.S.
      Science 313:1596-1604(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: cv. Nisqually.
    2. Cited for: GENOME REANNOTATION.
      Strain: cv. Nisqually.

    Entry informationi

    Entry nameiLISC2_POPTR
    AccessioniPrimary (citable) accession number: B9N2B0
    Secondary accession number(s): U5FF64
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 5, 2010
    Last sequence update: March 24, 2009
    Last modified: October 1, 2014
    This is version 43 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programPlant Protein Annotation Program

    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