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A9NNH7

- LIAS_PICSI

UniProt

A9NNH7 - LIAS_PICSI

Protein

Lipoyl synthase, mitochondrial

Gene

LIP1

Organism
Picea sitchensis (Sitka spruce) (Pinus sitchensis)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 28 (01 Oct 2014)
      Sequence version 1 (05 Feb 2008)
      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 bindingi115 – 1151Iron-sulfur 1 (4Fe-4S)UniRule annotation
    Metal bindingi120 – 1201Iron-sulfur 1 (4Fe-4S)UniRule annotation
    Metal bindingi126 – 1261Iron-sulfur 1 (4Fe-4S)UniRule annotation
    Metal bindingi146 – 1461Iron-sulfur 2 (4Fe-4S-S-AdoMet)UniRule annotation
    Metal bindingi150 – 1501Iron-sulfur 2 (4Fe-4S-S-AdoMet)UniRule annotation
    Metal bindingi153 – 1531Iron-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
    OrganismiPicea sitchensis (Sitka spruce) (Pinus sitchensis)
    Taxonomic identifieri3332 [NCBI]
    Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaPinidaePinalesPinaceaePicea

    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? – 386Lipoyl synthase, mitochondrialPRO_0000398853
    Transit peptidei1 – ?MitochondrionUniRule annotation

    Structurei

    3D structure databases

    ProteinModelPortaliA9NNH7.
    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.

    A9NNH7-1 [UniParc]FASTAAdd to Basket

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    MSINPAFLRR ITWGSKSLHH QFTRCQVRAL SSSVEQTPES TTPALSALRE    50
    RLANGGPTLS DFLTRNLGEE PYSVDVGTKK NPLPKPKWMK AAVPGGDKYT 100
    AIKAKLREMN LHTVCEEAKC PNLGECWSGG ETGTATATIM ILGDTCTRGC 150
    RFCAVKTSRT PPPPDPNEPT NVAEAIVSWG LDYVVLTSVD RDDLPDQGSG 200
    HFAKTVQKLK QLKPKMLVEA LVPDFQGNSE CVQKVATSGL DVFAHNIETV 250
    EELQRVVRDH RANFNQSLEV LKMAKTYSPL GVLTKTSVML GCGETPAQVI 300
    ETMEKVREAG VDVITFGQYM RPTKRHMAVS EYVTPEAFEK YQKLGMEMGF 350
    RYVASGPMVR SSYKAGEFYI KSMIEDDRKK ASSSSI 386
    Length:386
    Mass (Da):42,579
    Last modified:February 5, 2008 - v1
    Checksum:i0FAA92A285A950F8
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    EF082836 mRNA. Translation: ABK22188.1.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    EF082836 mRNA. Translation: ABK22188.1 .

    3D structure databases

    ProteinModelPortali A9NNH7.
    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. "A conifer genomics resource of 200,000 spruce (Picea spp.) ESTs and 6,464 high-quality, sequence-finished full-length cDNAs for Sitka spruce (Picea sitchensis)."
      Ralph S.G., Chun H.J., Kolosova N., Cooper D., Oddy C., Ritland C.E., Kirkpatrick R., Moore R., Barber S., Holt R.A., Jones S.J., Marra M.A., Douglas C.J., Ritland K., Bohlmann J.
      BMC Genomics 9:484-484(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

    Entry informationi

    Entry nameiLIAS_PICSI
    AccessioniPrimary (citable) accession number: A9NNH7
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 5, 2010
    Last sequence update: February 5, 2008
    Last modified: October 1, 2014
    This is version 28 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