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A2XU53

- LIAS_ORYSI

UniProt

A2XU53 - LIAS_ORYSI

Protein

Lipoyl synthase, mitochondrial

Gene

LIP1

Organism
Oryza sativa subsp. indica (Rice)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 50 (01 Oct 2014)
      Sequence version 2 (05 Oct 2010)
      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 bindingi112 – 1121Iron-sulfur 1 (4Fe-4S)UniRule annotation
    Metal bindingi117 – 1171Iron-sulfur 1 (4Fe-4S)UniRule annotation
    Metal bindingi123 – 1231Iron-sulfur 1 (4Fe-4S)UniRule annotation
    Metal bindingi143 – 1431Iron-sulfur 2 (4Fe-4S-S-AdoMet)UniRule annotation
    Metal bindingi147 – 1471Iron-sulfur 2 (4Fe-4S-S-AdoMet)UniRule annotation
    Metal bindingi150 – 1501Iron-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, mitochondrialUniRule 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:LIP1UniRule annotation
    ORF Names:H0523F07.4, OsI_16128
    OrganismiOryza sativa subsp. indica (Rice)
    Taxonomic identifieri39946 [NCBI]
    Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaLiliopsidaPoalesPoaceaeBEP cladeEhrhartoideaeOryzeaeOryza

    Organism-specific databases

    GrameneiA2XU53.

    Subcellular locationi

    Mitochondrion UniRule annotation

    GO - Cellular componenti

    1. mitochondrial matrix Source: EnsemblPlants/Gramene

    Keywords - Cellular componenti

    Mitochondrion

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transit peptidei1 – 3030MitochondrionUniRule annotationAdd
    BLAST
    Chaini31 – 382352Lipoyl synthase, mitochondrialPRO_0000398848Add
    BLAST

    Interactioni

    Protein-protein interaction databases

    STRINGi39947.LOC_Os04g38330.1.

    Structurei

    3D structure databases

    ProteinModelPortaliA2XU53.
    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.

    Family and domain databases

    Gene3Di3.20.20.70. 1 hit.
    HAMAPiMF_00206. Lipoyl_synth.
    MF_03128. Lipoyl_synth_plantM.
    InterProiIPR013785. Aldolase_TIM.
    IPR006638. Elp3/MiaB/NifB.
    IPR003698. Lipoyl_synth.
    IPR027527. Lipoyl_synth_mt.
    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.

    A2XU53-1 [UniParc]FASTAAdd to Basket

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    MHGRRHLAAS LARALTYAPS RSISSTPSLL QTLDPSTPSP AAAPPTAGRL    50
    AELRQRLQAD APSLGDFTYS VEVGTRKKPL PKPKWMKETI PGGAKYAGIK 100
    AKLRELKLHT VCEEARCPNL GECWSGGETG TATATIMILG DTCTRGCRFC 150
    NVKTSRTPPP PDPDEPSNVA QAIASWGLEY IVITSVDRDD LPDQGSGHFA 200
    ETVQKLKVLK PEMLIEALVP DFRGDPACVE KVATSGLHVF AHNIETVEEL 250
    QRNVRDHRAN FKQSIDVLKL AKEYAPAGTL TKTSIMLGCG ETPDQVISTM 300
    EKVRAAGVDV MTFGQYMRPS KRHMPVSEYV TPEAFERYRS LGVDMGFRYV 350
    ASGPMVRSSY KAGEFYIKAM IEADRAKATT AI 382
    Length:382
    Mass (Da):41,682
    Last modified:October 5, 2010 - v2
    Checksum:i754A727161F5B3D0
    GO

    Sequence cautioni

    The sequence EAY94363.1 differs from that shown. Reason: Erroneous termination at position 361. Translated as Lys.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti32 – 343TLD → NLE in CAH67016. (PubMed:12447439)Curated
    Sequence conflicti41 – 455AAAPP → EDDPT in CAH67016. (PubMed:12447439)Curated
    Sequence conflicti50 – 501L → I in CAH67016. (PubMed:12447439)Curated
    Sequence conflicti55 – 551Q → K in CAH67016. (PubMed:12447439)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CR855164 Genomic DNA. Translation: CAH67016.1.
    CM000129 Genomic DNA. Translation: EAY94363.1. Sequence problems.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CR855164 Genomic DNA. Translation: CAH67016.1 .
    CM000129 Genomic DNA. Translation: EAY94363.1 . Sequence problems.

    3D structure databases

    ProteinModelPortali A2XU53.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 39947.LOC_Os04g38330.1.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Organism-specific databases

    Gramenei A2XU53.

    Phylogenomic databases

    eggNOGi COG0320.
    HOGENOMi HOG000235998.

    Enzyme and pathway databases

    UniPathwayi UPA00538 ; UER00593 .

    Family and domain databases

    Gene3Di 3.20.20.70. 1 hit.
    HAMAPi MF_00206. Lipoyl_synth.
    MF_03128. Lipoyl_synth_plantM.
    InterProi IPR013785. Aldolase_TIM.
    IPR006638. Elp3/MiaB/NifB.
    IPR003698. Lipoyl_synth.
    IPR027527. Lipoyl_synth_mt.
    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. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: cv. Guang-Lu-Ai No.4.
    2. "The genomes of Oryza sativa: a history of duplications."
      Yu J., Wang J., Lin W., Li S., Li H., Zhou J., Ni P., Dong W., Hu S., Zeng C., Zhang J., Zhang Y., Li R., Xu Z., Li S., Li X., Zheng H., Cong L.
      , Lin L., Yin J., Geng J., Li G., Shi J., Liu J., Lv H., Li J., Wang J., Deng Y., Ran L., Shi X., Wang X., Wu Q., Li C., Ren X., Wang J., Wang X., Li D., Liu D., Zhang X., Ji Z., Zhao W., Sun Y., Zhang Z., Bao J., Han Y., Dong L., Ji J., Chen P., Wu S., Liu J., Xiao Y., Bu D., Tan J., Yang L., Ye C., Zhang J., Xu J., Zhou Y., Yu Y., Zhang B., Zhuang S., Wei H., Liu B., Lei M., Yu H., Li Y., Xu H., Wei S., He X., Fang L., Zhang Z., Zhang Y., Huang X., Su Z., Tong W., Li J., Tong Z., Li S., Ye J., Wang L., Fang L., Lei T., Chen C.-S., Chen H.-C., Xu Z., Li H., Huang H., Zhang F., Xu H., Li N., Zhao C., Li S., Dong L., Huang Y., Li L., Xi Y., Qi Q., Li W., Zhang B., Hu W., Zhang Y., Tian X., Jiao Y., Liang X., Jin J., Gao L., Zheng W., Hao B., Liu S.-M., Wang W., Yuan L., Cao M., McDermott J., Samudrala R., Wang J., Wong G.K.-S., Yang H.
      PLoS Biol. 3:266-281(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: cv. 93-11.

    Entry informationi

    Entry nameiLIAS_ORYSI
    AccessioniPrimary (citable) accession number: A2XU53
    Secondary accession number(s): Q01JQ9
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 5, 2010
    Last sequence update: October 5, 2010
    Last modified: October 1, 2014
    This is version 50 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programPlant Protein Annotation Program

    Miscellaneousi

    Documents

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

    External Data

    Dasty 3