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Q3LSN5

- LIAS2_PEA

UniProt

Q3LSN5 - LIAS2_PEA

Protein

Lipoyl synthase 2, mitochondrial

Gene

LIP1-2

Organism
Pisum sativum (Garden pea)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 39 (01 Oct 2014)
      Sequence version 1 (25 Oct 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.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 bindingi109 – 1091Iron-sulfur 1 (4Fe-4S)UniRule annotation
    Metal bindingi114 – 1141Iron-sulfur 1 (4Fe-4S)UniRule annotation
    Metal bindingi120 – 1201Iron-sulfur 1 (4Fe-4S)UniRule annotation
    Metal bindingi140 – 1401Iron-sulfur 2 (4Fe-4S-S-AdoMet)UniRule annotation
    Metal bindingi144 – 1441Iron-sulfur 2 (4Fe-4S-S-AdoMet)UniRule annotation
    Metal bindingi147 – 1471Iron-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
    Name:LIP1-2UniRule annotation
    OrganismiPisum sativum (Garden pea)
    Taxonomic identifieri3888 [NCBI]
    Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsfabidsFabalesFabaceaePapilionoideaeFabeaePisum

    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? – 376Lipoyl synthase 2, mitochondrialPRO_0000398852
    Transit peptidei1 – ?MitochondrionUniRule annotation

    Structurei

    3D structure databases

    ProteinModelPortaliQ3LSN5.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

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

    Keywords - Domaini

    Transit peptide

    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.

    Q3LSN5-1 [UniParc]FASTAAdd to Basket

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    MMYSRFRTVA GNLNCAAKRL SSSSTTTTTT SAPSELQQNL AALRARLAME    50
    SPSLSDFISL KSDNAYSVEV GTKKKPLPKP KWMKESIPGG EKYVQIKKKL 100
    RELKLHTVCE EAKCPNLGEC WSGGETGTAT ATIMILGDTC TRGCRFCNVK 150
    TSRTPPPPDP DEPTNVAEAI ASWGLDYVVI TSVDRDDLPD QGSGHFTETV 200
    QKLKALKPSM LIEALVPDFR GNAECVEKVS KSGLDVFAHN IETVEELQSA 250
    VRDHRANFKQ SLDVLMMAKE YAPAGTLTKT SIMLGCGETP DQIVKTMEKV 300
    RAAGVDVMTF GQHMRPSKRH MPVSEYITPE AFEKYQTLGM EMGFRYVASG 350
    PMVRSSYKAG EFYIKSMIDS DRAASS 376
    Length:376
    Mass (Da):41,294
    Last modified:October 25, 2005 - v1
    Checksum:i3613E2F6A0492FAA
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    DQ181623 mRNA. Translation: ABA29155.1.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    DQ181623 mRNA. Translation: ABA29155.1 .

    3D structure databases

    ProteinModelPortali Q3LSN5.
    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.
    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. Doss R.P., Price R.R.
      Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].

    Entry informationi

    Entry nameiLIAS2_PEA
    AccessioniPrimary (citable) accession number: Q3LSN5
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 5, 2010
    Last sequence update: October 25, 2005
    Last modified: October 1, 2014
    This is version 39 of the entry and version 1 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