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D0NP70

- LIPA_PHYIT

UniProt

D0NP70 - LIPA_PHYIT

Protein

Lipoyl synthase, mitochondrial

Gene

PITG_14852

Organism
Phytophthora infestans (strain T30-4) (Potato late blight fungus)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 29 (01 Oct 2014)
      Sequence version 1 (15 Dec 2009)
      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 bindingi116 – 1161Iron-sulfur 1 (4Fe-4S)UniRule annotation
    Metal bindingi121 – 1211Iron-sulfur 1 (4Fe-4S)UniRule annotation
    Metal bindingi127 – 1271Iron-sulfur 1 (4Fe-4S)UniRule annotation
    Metal bindingi147 – 1471Iron-sulfur 2 (4Fe-4S-S-AdoMet)UniRule annotation
    Metal bindingi151 – 1511Iron-sulfur 2 (4Fe-4S-S-AdoMet)UniRule annotation
    Metal bindingi154 – 1541Iron-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
    ORF Names:PITG_14852
    OrganismiPhytophthora infestans (strain T30-4) (Potato late blight fungus)
    Taxonomic identifieri403677 [NCBI]
    Taxonomic lineageiEukaryotaStramenopilesOomycetesPeronosporalesPhytophthora
    ProteomesiUP000006643: Partially assembled WGS sequence

    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 – 1919MitochondrionUniRule annotationAdd
    BLAST
    Chaini20 – 383364Lipoyl synthase, mitochondrialPRO_0000398245Add
    BLAST

    Structurei

    3D structure databases

    ProteinModelPortaliD0NP70.
    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.
    OMAiPEEPYNT.

    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.

    D0NP70-1 [UniParc]FASTAAdd to Basket

    « Hide

    MHASTLTRCM RVAQNARCLS TAAASVQVTH SERGARLAAL RERLAEETRQ    50
    GPTFAEQALS LEDFAFEADA APGTKPSRKP NASNRKPKWL KAQPTQGANY 100
    ERLRKSVKSL GLSTVCEEAK CPNIGECWGG GKDGIATATI MLMGDTCTRG 150
    CSFCAVKTSR KPKPLDIEEP NKVAEAIAAW GLDYIVFTSV DRDDYEDLGA 200
    GHFAKTVSTL RAKLPEILIE CLTPDFQGHD NLIDQVATSG LDVFAHNMET 250
    VERLQRRVRD YRANYKQSLH VLERAKVAAP HLVTKTSLML GVGERNEDLF 300
    QTLRDLRNSG VDVVTFGQYL RPSTKHMPVK SYVTPEAFAE WQKVAEQMGF 350
    LYVASGPMVR SSYKAGEFFM KNLLKNRKTQ VVA 383
    Length:383
    Mass (Da):42,420
    Last modified:December 15, 2009 - v1
    Checksum:i6D29FBE4DC34315F
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    DS028150 Genomic DNA. Translation: EEY62412.1.
    RefSeqiXP_002899048.1. XM_002899002.1.
    UniGeneiPin.6624.

    Genome annotation databases

    EnsemblProtistsiPITG_14852T0; PITG_14852T0; PITG_14852.
    GeneIDi9467967.
    KEGGipif:PITG_14852.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    DS028150 Genomic DNA. Translation: EEY62412.1 .
    RefSeqi XP_002899048.1. XM_002899002.1.
    UniGenei Pin.6624.

    3D structure databases

    ProteinModelPortali D0NP70.
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblProtistsi PITG_14852T0 ; PITG_14852T0 ; PITG_14852 .
    GeneIDi 9467967.
    KEGGi pif:PITG_14852.

    Phylogenomic databases

    HOGENOMi HOG000235998.
    KOi K03644.
    OMAi PEEPYNT.

    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. "Genome sequence and analysis of the Irish potato famine pathogen Phytophthora infestans."
      The Broad Institute Genome Sequencing Platform
      Haas B.J., Kamoun S., Zody M.C., Jiang R.H., Handsaker R.E., Cano L.M., Grabherr M., Kodira C.D., Raffaele S., Torto-Alalibo T., Bozkurt T.O., Ah-Fong A.M., Alvarado L., Anderson V.L., Armstrong M.R., Avrova A., Baxter L., Beynon J.
      , Boevink P.C., Bollmann S.R., Bos J.I., Bulone V., Cai G., Cakir C., Carrington J.C., Chawner M., Conti L., Costanzo S., Ewan R., Fahlgren N., Fischbach M.A., Fugelstad J., Gilroy E.M., Gnerre S., Green P.J., Grenville-Briggs L.J., Griffith J., Grunwald N.J., Horn K., Horner N.R., Hu C.H., Huitema E., Jeong D.H., Jones A.M., Jones J.D., Jones R.W., Karlsson E.K., Kunjeti S.G., Lamour K., Liu Z., Ma L., Maclean D., Chibucos M.C., McDonald H., McWalters J., Meijer H.J., Morgan W., Morris P.F., Munro C.A., O'Neill K., Ospina-Giraldo M., Pinzon A., Pritchard L., Ramsahoye B., Ren Q., Restrepo S., Roy S., Sadanandom A., Savidor A., Schornack S., Schwartz D.C., Schumann U.D., Schwessinger B., Seyer L., Sharpe T., Silvar C., Song J., Studholme D.J., Sykes S., Thines M., van de Vondervoort P.J., Phuntumart V., Wawra S., Weide R., Win J., Young C., Zhou S., Fry W., Meyers B.C., van West P., Ristaino J., Govers F., Birch P.R., Whisson S.C., Judelson H.S., Nusbaum C.
      Nature 461:393-398(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: T30-4.

    Entry informationi

    Entry nameiLIPA_PHYIT
    AccessioniPrimary (citable) accession number: D0NP70
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 5, 2010
    Last sequence update: December 15, 2009
    Last modified: October 1, 2014
    This is version 29 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)

    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