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Q8IDQ0

- LIPA_PLAF7

UniProt

Q8IDQ0 - LIPA_PLAF7

Protein

Lipoyl synthase, apicoplast

Gene

lipA

Organism
Plasmodium falciparum (isolate 3D7)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 65 (01 Oct 2014)
      Sequence version 1 (01 Mar 2003)
      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.1 PublicationUniRule 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 bindingi153 – 1531Iron-sulfur 1 (4Fe-4S)UniRule annotation
    Metal bindingi158 – 1581Iron-sulfur 1 (4Fe-4S)UniRule annotation
    Metal bindingi164 – 1641Iron-sulfur 1 (4Fe-4S)UniRule annotation
    Metal bindingi179 – 1791Iron-sulfur 2 (4Fe-4S-S-AdoMet)UniRule annotation
    Metal bindingi183 – 1831Iron-sulfur 2 (4Fe-4S-S-AdoMet)UniRule annotation
    Metal bindingi186 – 1861Iron-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: GeneDB_Pfalciparum
    3. metal ion binding Source: UniProtKB-KW

    GO - Biological processi

    1. lipoate biosynthetic process Source: GeneDB_Pfalciparum
    2. 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, apicoplastUniRule 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:lipAUniRule annotation
    ORF Names:MAL13P1.220
    OrganismiPlasmodium falciparum (isolate 3D7)
    Taxonomic identifieri36329 [NCBI]
    Taxonomic lineageiEukaryotaAlveolataApicomplexaAconoidasidaHaemosporidaPlasmodiumPlasmodium (Laverania)
    ProteomesiUP000001450: Chromosome 13

    Organism-specific databases

    EuPathDBiPlasmoDB:PF3D7_1344600.

    Subcellular locationi

    Plastidapicoplast UniRule annotation

    GO - Cellular componenti

    1. apicoplast Source: GeneDB_Pfalciparum

    Keywords - Cellular componenti

    Apicoplast, Plastid

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2323UniRule annotationAdd
    BLAST
    Chaini24 – 415392Lipoyl synthase, apicoplastPRO_0000398230Add
    BLAST

    Expressioni

    Developmental stagei

    Expressed maximally in the early stages and late stages of the parasite erythrocytic development.1 Publication

    Interactioni

    Protein-protein interaction databases

    STRINGi5833.MAL13P1.220-1.

    Structurei

    3D structure databases

    ProteinModelPortaliQ8IDQ0.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

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

    Keywords - Domaini

    Signal

    Phylogenomic databases

    eggNOGiCOG0320.
    HOGENOMiHOG000235998.
    KOiK03644.
    OMAiRKVDCDI.
    PhylomeDBiQ8IDQ0.

    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.

    Q8IDQ0-1 [UniParc]FASTAAdd to Basket

    « Hide

    MHFGIPSLFY LYILFSIIMR IKCVITKNLK KTKKRTCSYI PHGNMEKGII    50
    LNYIEKPNPA YLKRGKNKNK NKNKKGDIYK LRNVEILLYA NRYVHEGNEN 100
    FSSTTKKLLL TPKVGNKMPE GKKPDWFHVA APTVAKYNKL KDDIKKLNLH 150
    TVCEEAQCPN IGECWNIGTA TIMLLGDTCT RGCKFCSIKT SSNPLPPDIN 200
    EPFNTAKAIC EWNIDYVVLT SVDRDDLPDG GASHFAKTVE LVKFSRPDIL 250
    IECLVSDFQG NIDSVRKLAF SGLDVYAHNI ETVKRLQKYV RDKRANYDQS 300
    LFVLKTAKEI NPQLYTKTSI MLGLGETKEE VIQTMYDARK NNIDVITFGQ 350
    YLRPTKNHLS IVQYISPQMF EYYKEEGLKM GFKYIASGPL VRSSYKAGEY 400
    FIKNLVNQRN KDKKN 415
    Length:415
    Mass (Da):47,593
    Last modified:March 1, 2003 - v1
    Checksum:iFB6D7CE36D52E2C1
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AL844509 Genomic DNA. Translation: CAD52569.1.
    RefSeqiXP_001350160.1. XM_001350124.1.

    Genome annotation databases

    EnsemblProtistsiMAL13P1.220:mRNA; MAL13P1.220:pep; MAL13P1.220.
    GeneIDi813778.
    KEGGipfa:MAL13P1.220.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AL844509 Genomic DNA. Translation: CAD52569.1 .
    RefSeqi XP_001350160.1. XM_001350124.1.

    3D structure databases

    ProteinModelPortali Q8IDQ0.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 5833.MAL13P1.220-1.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblProtistsi MAL13P1.220:mRNA ; MAL13P1.220:pep ; MAL13P1.220 .
    GeneIDi 813778.
    KEGGi pfa:MAL13P1.220.

    Organism-specific databases

    EuPathDBi PlasmoDB:PF3D7_1344600.

    Phylogenomic databases

    eggNOGi COG0320.
    HOGENOMi HOG000235998.
    KOi K03644.
    OMAi RKVDCDI.
    PhylomeDBi Q8IDQ0.

    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. "Sequence of Plasmodium falciparum chromosomes 1, 3-9 and 13."
      Hall N., Pain A., Berriman M., Churcher C.M., Harris B., Harris D., Mungall K.L., Bowman S., Atkin R., Baker S., Barron A., Brooks K., Buckee C.O., Burrows C., Cherevach I., Chillingworth C., Chillingworth T., Christodoulou Z.
      , Clark L., Clark R., Corton C., Cronin A., Davies R.M., Davis P., Dear P., Dearden F., Doggett J., Feltwell T., Goble A., Goodhead I., Gwilliam R., Hamlin N., Hance Z., Harper D., Hauser H., Hornsby T., Holroyd S., Horrocks P., Humphray S., Jagels K., James K.D., Johnson D., Kerhornou A., Knights A., Konfortov B., Kyes S., Larke N., Lawson D., Lennard N., Line A., Maddison M., Mclean J., Mooney P., Moule S., Murphy L., Oliver K., Ormond D., Price C., Quail M.A., Rabbinowitsch E., Rajandream M.A., Rutter S., Rutherford K.M., Sanders M., Simmonds M., Seeger K., Sharp S., Smith R., Squares R., Squares S., Stevens K., Taylor K., Tivey A., Unwin L., Whitehead S., Woodward J.R., Sulston J.E., Craig A., Newbold C., Barrell B.G.
      Nature 419:527-531(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: Isolate 3D7.
    2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: Isolate 3D7.
    3. "The human malaria parasite Plasmodium falciparum has distinct organelle-specific lipoylation pathways."
      Wrenger C., Mueller S.
      Mol. Microbiol. 53:103-113(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE.

    Entry informationi

    Entry nameiLIPA_PLAF7
    AccessioniPrimary (citable) accession number: Q8IDQ0
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 5, 2010
    Last sequence update: March 1, 2003
    Last modified: October 1, 2014
    This is version 65 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