Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

P32875

- LIPA_YEAST

UniProt

P32875 - LIPA_YEAST

Protein

Lipoyl synthase, mitochondrial

Gene

LIP5

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 125 (01 Oct 2014)
      Sequence version 1 (01 Oct 1993)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    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.2 Publications

    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 bindingi150 – 1501Iron-sulfur 1 (4Fe-4S)UniRule annotation
    Metal bindingi155 – 1551Iron-sulfur 1 (4Fe-4S)UniRule annotation
    Metal bindingi161 – 1611Iron-sulfur 1 (4Fe-4S)UniRule annotation
    Metal bindingi181 – 1811Iron-sulfur 2 (4Fe-4S-S-AdoMet)UniRule annotation
    Metal bindingi185 – 1851Iron-sulfur 2 (4Fe-4S-S-AdoMet)UniRule annotation
    Metal bindingi188 – 1881Iron-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: SGD
    3. metal ion binding Source: UniProtKB-KW

    GO - Biological processi

    1. protein lipoylation Source: SGD

    Keywords - Molecular functioni

    Transferase

    Keywords - Ligandi

    4Fe-4S, Iron, Iron-sulfur, Metal-binding, S-adenosyl-L-methionine

    Enzyme and pathway databases

    BioCyciMetaCyc:YOR196C-MONOMER.
    YEAST:YOR196C-MONOMER.
    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:LIP5UniRule annotation
    Ordered Locus Names:YOR196C
    OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
    Taxonomic identifieri559292 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
    ProteomesiUP000002311: Chromosome XV

    Organism-specific databases

    CYGDiYOR196c.
    SGDiS000005722. LIP5.

    Subcellular locationi

    Mitochondrion 2 PublicationsUniRule 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 – 1818MitochondrionUniRule annotationAdd
    BLAST
    Chaini19 – 414396Lipoyl synthase, mitochondrialPRO_0000017726Add
    BLAST

    Proteomic databases

    MaxQBiP32875.
    PaxDbiP32875.
    PeptideAtlasiP32875.
    PRIDEiP32875.

    Expressioni

    Gene expression databases

    GenevestigatoriP32875.

    Interactioni

    Protein-protein interaction databases

    BioGridi34594. 141 interactions.
    DIPiDIP-3931N.
    IntActiP32875. 1 interaction.
    MINTiMINT-522178.
    STRINGi4932.YOR196C.

    Structurei

    3D structure databases

    ProteinModelPortaliP32875.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

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

    Keywords - Domaini

    Transit peptide

    Phylogenomic databases

    eggNOGiCOG0320.
    GeneTreeiENSGT00390000006234.
    KOiK03644.
    OMAiEWLRRPI.
    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.

    P32875-1 [UniParc]FASTAAdd to Basket

    « Hide

    MYRRSVGVLF VGRNTRWISS TIRCGTSATR PIRSNALNTD SDNASVRVPV    50
    GNSTEVENAT SQLTGTSGKR RKGNRKRITE FKDALNLGPS FADFVSGKAS 100
    KMILDPLEKA RQNTEEAKKL PRWLKVPIPK GTNYHKLKGD VKELGLSTVC 150
    EEARCPNIGE CWGGKDKSKA TATIMLLGDT CTRGCRFCSV KTNRTPSKPD 200
    PMEPENTAEA IKRWGLGYVV LTTVDRDDLV DGGANHLAET VRKIKQKAPN 250
    TLVETLSGDF RGDLKMVDIM AQCGLDVYAH NLETVESLTP HVRDRRATYR 300
    QSLSVLERAK ATVPSLITKT SIMLGLGETD EQITQTLKDL RNIQCDVVTF 350
    GQYMRPTKRH MKVVEYVKPE KFDYWKERAL EMGFLYCASG PLVRSSYKAG 400
    EAFIENVLKK RNMK 414
    Length:414
    Mass (Da):46,247
    Last modified:October 1, 1993 - v1
    Checksum:i962BC3DF9857C3BB
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L11999 Genomic DNA. Translation: AAA34745.1.
    Z75104 Genomic DNA. Translation: CAA99409.1.
    AY558046 Genomic DNA. Translation: AAS56372.1.
    BK006948 Genomic DNA. Translation: DAA10971.1.
    PIRiS42159.
    RefSeqiNP_014839.1. NM_001183615.1.

    Genome annotation databases

    EnsemblFungiiYOR196C; YOR196C; YOR196C.
    GeneIDi854371.
    KEGGisce:YOR196C.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L11999 Genomic DNA. Translation: AAA34745.1 .
    Z75104 Genomic DNA. Translation: CAA99409.1 .
    AY558046 Genomic DNA. Translation: AAS56372.1 .
    BK006948 Genomic DNA. Translation: DAA10971.1 .
    PIRi S42159.
    RefSeqi NP_014839.1. NM_001183615.1.

    3D structure databases

    ProteinModelPortali P32875.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 34594. 141 interactions.
    DIPi DIP-3931N.
    IntActi P32875. 1 interaction.
    MINTi MINT-522178.
    STRINGi 4932.YOR196C.

    Proteomic databases

    MaxQBi P32875.
    PaxDbi P32875.
    PeptideAtlasi P32875.
    PRIDEi P32875.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblFungii YOR196C ; YOR196C ; YOR196C .
    GeneIDi 854371.
    KEGGi sce:YOR196C.

    Organism-specific databases

    CYGDi YOR196c.
    SGDi S000005722. LIP5.

    Phylogenomic databases

    eggNOGi COG0320.
    GeneTreei ENSGT00390000006234.
    KOi K03644.
    OMAi EWLRRPI.
    OrthoDBi EOG79KPR7.

    Enzyme and pathway databases

    UniPathwayi UPA00538 ; UER00593 .
    BioCyci MetaCyc:YOR196C-MONOMER.
    YEAST:YOR196C-MONOMER.

    Miscellaneous databases

    NextBioi 976499.
    PROi P32875.

    Gene expression databases

    Genevestigatori P32875.

    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. "Isolation and characterization of LIP5. A lipoate biosynthetic locus of Saccharomyces cerevisiae."
      Sulo P., Martin N.C.
      J. Biol. Chem. 268:17634-17639(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION.
      Strain: DBY745.
    2. "The nucleotide sequence of Saccharomyces cerevisiae chromosome XV."
      Dujon B., Albermann K., Aldea M., Alexandraki D., Ansorge W., Arino J., Benes V., Bohn C., Bolotin-Fukuhara M., Bordonne R., Boyer J., Camasses A., Casamayor A., Casas C., Cheret G., Cziepluch C., Daignan-Fornier B., Dang V.-D.
      , de Haan M., Delius H., Durand P., Fairhead C., Feldmann H., Gaillon L., Galisson F., Gamo F.-J., Gancedo C., Goffeau A., Goulding S.E., Grivell L.A., Habbig B., Hand N.J., Hani J., Hattenhorst U., Hebling U., Hernando Y., Herrero E., Heumann K., Hiesel R., Hilger F., Hofmann B., Hollenberg C.P., Hughes B., Jauniaux J.-C., Kalogeropoulos A., Katsoulou C., Kordes E., Lafuente M.J., Landt O., Louis E.J., Maarse A.C., Madania A., Mannhaupt G., Marck C., Martin R.P., Mewes H.-W., Michaux G., Paces V., Parle-McDermott A.G., Pearson B.M., Perrin A., Pettersson B., Poch O., Pohl T.M., Poirey R., Portetelle D., Pujol A., Purnelle B., Ramezani Rad M., Rechmann S., Schwager C., Schweizer M., Sor F., Sterky F., Tarassov I.A., Teodoru C., Tettelin H., Thierry A., Tobiasch E., Tzermia M., Uhlen M., Unseld M., Valens M., Vandenbol M., Vetter I., Vlcek C., Voet M., Volckaert G., Voss H., Wambutt R., Wedler H., Wiemann S., Winsor B., Wolfe K.H., Zollner A., Zumstein E., Kleine K.
      Nature 387:98-102(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 204508 / S288c.
    3. Cited for: GENOME REANNOTATION.
      Strain: ATCC 204508 / S288c.
    4. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: ATCC 204508 / S288c.
    5. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
    6. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
    7. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
    8. Cited for: FUNCTION.

    Entry informationi

    Entry nameiLIPA_YEAST
    AccessioniPrimary (citable) accession number: P32875
    Secondary accession number(s): D6W2Q5
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1993
    Last sequence update: October 1, 1993
    Last modified: October 1, 2014
    This is version 125 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programFungal Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    Present with 1630 molecules/cell in log phase SD medium.1 Publication

    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
    3. Yeast
      Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
    4. Yeast chromosome XV
      Yeast (Saccharomyces cerevisiae) chromosome XV: entries and gene names

    External Data

    Dasty 3