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Q74ZH6

- LIPA_ASHGO

UniProt

Q74ZH6 - LIPA_ASHGO

Protein

Lipoyl synthase, mitochondrial

Gene

AGR231C

Organism
Ashbya gossypii (strain ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056) (Yeast) (Eremothecium gossypii)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 77 (01 Oct 2014)
      Sequence version 1 (05 Jul 2004)
      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 bindingi106 – 1061Iron-sulfur 1 (4Fe-4S)UniRule annotation
    Metal bindingi111 – 1111Iron-sulfur 1 (4Fe-4S)UniRule annotation
    Metal bindingi117 – 1171Iron-sulfur 1 (4Fe-4S)UniRule annotation
    Metal bindingi136 – 1361Iron-sulfur 2 (4Fe-4S-S-AdoMet)UniRule annotation
    Metal bindingi140 – 1401Iron-sulfur 2 (4Fe-4S-S-AdoMet)UniRule annotation
    Metal bindingi143 – 1431Iron-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
    Ordered Locus Names:AGR231C
    OrganismiAshbya gossypii (strain ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056) (Yeast) (Eremothecium gossypii)
    Taxonomic identifieri284811 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeEremothecium
    ProteomesiUP000000591: Chromosome VII

    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
    Transit peptidei1 – 3232MitochondrionUniRule annotationAdd
    BLAST
    Chaini33 – 369337Lipoyl synthase, mitochondrialPRO_0000398250Add
    BLAST

    Interactioni

    Protein-protein interaction databases

    STRINGi33169.AGOS_AGR231C.

    Structurei

    3D structure databases

    ProteinModelPortaliQ74ZH6.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

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

    Keywords - Domaini

    Transit peptide

    Phylogenomic databases

    HOGENOMiHOG000235998.
    KOiK03644.
    OMAiTIRAVRH.
    OrthoDBiEOG79KPR7.

    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.

    Q74ZH6-1 [UniParc]FASTAAdd to Basket

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    MLTKGVRALA WSPRRYITLD AEAAKPVVAK RRRMTEFTDK LNKGPSFEDF    50
    LTGKAAQMTL DPLEEARQNA EESKKLPAWL KVPIPKGKNF HKLKEDVRDL 100
    KLSTVCEEAK CPNIGECWGG NKGSATATIM LLGDTCTRGC RFCSVKTNRT 150
    PAKPDPKEPE NTAEAISRWG LGYVVLTMVD RDDLPDGGAH HLAETVQRIK 200
    QKAPHILVET LAGDFRGNLE MVDVMARSGL DVYAHNVETV EALTPHVRDR 250
    RATYQQSLSV LKRAKQTVPT LVTKTSIMLG MGETDEQVLQ TMKDLRAVDC 300
    DVVTFGQYMR PTRRHMKVVE YVKPEKFDYW KEKALELGFL YCASGPLVRS 350
    SYKAGEAYIE NVLRNRRQA 369
    Length:369
    Mass (Da):41,501
    Last modified:July 5, 2004 - v1
    Checksum:i056A20D95C457E4C
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AE016820 Genomic DNA. Translation: AAS54721.1.
    RefSeqiNP_986897.1. NM_211959.1.

    Genome annotation databases

    EnsemblFungiiAAS54721; AAS54721; AGOS_AGR231C.
    GeneIDi4623199.
    KEGGiago:AGOS_AGR231C.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AE016820 Genomic DNA. Translation: AAS54721.1 .
    RefSeqi NP_986897.1. NM_211959.1.

    3D structure databases

    ProteinModelPortali Q74ZH6.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 33169.AGOS_AGR231C.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblFungii AAS54721 ; AAS54721 ; AGOS_AGR231C .
    GeneIDi 4623199.
    KEGGi ago:AGOS_AGR231C.

    Phylogenomic databases

    HOGENOMi HOG000235998.
    KOi K03644.
    OMAi TIRAVRH.
    OrthoDBi EOG79KPR7.

    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 Ashbya gossypii genome as a tool for mapping the ancient Saccharomyces cerevisiae genome."
      Dietrich F.S., Voegeli S., Brachat S., Lerch A., Gates K., Steiner S., Mohr C., Poehlmann R., Luedi P., Choi S., Wing R.A., Flavier A., Gaffney T.D., Philippsen P.
      Science 304:304-307(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056.
    2. "Genomes of Ashbya fungi isolated from insects reveal four mating-type loci, numerous translocations, lack of transposons, and distinct gene duplications."
      Dietrich F.S., Voegeli S., Kuo S., Philippsen P.
      G3 (Bethesda) 3:1225-1239(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: GENOME REANNOTATION.
      Strain: ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056.

    Entry informationi

    Entry nameiLIPA_ASHGO
    AccessioniPrimary (citable) accession number: Q74ZH6
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 5, 2010
    Last sequence update: July 5, 2004
    Last modified: October 1, 2014
    This is version 77 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programFungal 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