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Q57390

- LIPA_PELCD

UniProt

Q57390 - LIPA_PELCD

Protein

Lipoyl synthase

Gene

lipA

Organism
Pelobacter carbinolicus (strain DSM 2380 / Gra Bd 1)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 105 (01 Oct 2014)
      Sequence version 2 (20 Dec 2005)
      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 bindingi56 – 561Iron-sulfur 1 (4Fe-4S)UniRule annotation
    Metal bindingi61 – 611Iron-sulfur 1 (4Fe-4S)UniRule annotation
    Metal bindingi67 – 671Iron-sulfur 1 (4Fe-4S)UniRule annotation
    Metal bindingi82 – 821Iron-sulfur 2 (4Fe-4S-S-AdoMet)UniRule annotation
    Metal bindingi86 – 861Iron-sulfur 2 (4Fe-4S-S-AdoMet)UniRule annotation
    Metal bindingi89 – 891Iron-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

    BioCyciPCAR338963:GKDU-394-MONOMER.
    UniPathwayiUPA00538; UER00593.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Lipoyl synthaseUniRule annotation (EC:2.8.1.8UniRule annotation)
    Alternative name(s):
    Lip-synUniRule annotation
    Short name:
    LSUniRule annotation
    Lipoate synthaseUniRule annotation
    Lipoic acid synthaseUniRule annotation
    Sulfur insertion protein LipAUniRule annotation
    Gene namesi
    Name:lipAUniRule annotation
    Synonyms:acoS
    Ordered Locus Names:Pcar_0346
    OrganismiPelobacter carbinolicus (strain DSM 2380 / Gra Bd 1)
    Taxonomic identifieri338963 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaDeltaproteobacteriaDesulfuromonadalesPelobacteraceaePelobacter
    ProteomesiUP000002534: Chromosome

    Subcellular locationi

    Cytoplasm UniRule annotation

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cytoplasm

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 309309Lipoyl synthasePRO_0000102333Add
    BLAST

    Interactioni

    Protein-protein interaction databases

    STRINGi338963.Pcar_0346.

    Structurei

    3D structure databases

    ProteinModelPortaliQ57390.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

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

    Phylogenomic databases

    eggNOGiCOG0320.
    HOGENOMiHOG000235997.
    KOiK03644.
    OMAiHPHIPTK.
    OrthoDBiEOG6038ZS.

    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.

    Q57390-1 [UniParc]FASTAAdd to Basket

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    MDVGQKKRGA DKTALATTDE QGALSKPTWI RAKAPISPEV GRLTGILRDL    50
    HLHTVCEEAS CPNLGECFKR GTATFMIMGD VCTRRCPFCD VAHGRPAALD 100
    TEEPGHLADA IGAMKLKYVV ITSVTRDDLE DGGAAHFAQC IESIRKKTEG 150
    VKVEILVPDF RGHVDAALKN LGNCLPDVFN HNLETVPRLY AESRPGARYH 200
    ESLRLLQRFK ETYPGIPTKS GLMLGLGETD EEILEVMRDL RVHGCDMLTI 250
    GQYLRPSRHH LPVQRYVTPE QFEAFRVAGL KMGFSQVASG PLVRSSYHAD 300
    LQAKEVLHT 309
    Length:309
    Mass (Da):34,154
    Last modified:December 20, 2005 - v2
    Checksum:i9EA24FB6E17AFAC7
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti149 – 1513EGV → RRVY in AAA91878. (PubMed:8110297)Curated
    Sequence conflicti149 – 1513EGV → RRVY in AAA18918. (PubMed:8110297)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L24124 Genomic DNA. Translation: AAA91878.1.
    U01100 Unassigned DNA. Translation: AAA18918.1.
    CP000142 Genomic DNA. Translation: ABA87606.1.
    PIRiE36953.
    RefSeqiWP_011340025.1. NC_007498.2.
    YP_006716018.1. NC_007498.2.

    Genome annotation databases

    EnsemblBacteriaiABA87606; ABA87606; Pcar_0346.
    GeneIDi3723479.
    KEGGipca:Pcar_0346.
    PATRICi22886614. VBIPelCar86875_0384.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L24124 Genomic DNA. Translation: AAA91878.1 .
    U01100 Unassigned DNA. Translation: AAA18918.1 .
    CP000142 Genomic DNA. Translation: ABA87606.1 .
    PIRi E36953.
    RefSeqi WP_011340025.1. NC_007498.2.
    YP_006716018.1. NC_007498.2.

    3D structure databases

    ProteinModelPortali Q57390.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 338963.Pcar_0346.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai ABA87606 ; ABA87606 ; Pcar_0346 .
    GeneIDi 3723479.
    KEGGi pca:Pcar_0346.
    PATRICi 22886614. VBIPelCar86875_0384.

    Phylogenomic databases

    eggNOGi COG0320.
    HOGENOMi HOG000235997.
    KOi K03644.
    OMAi HPHIPTK.
    OrthoDBi EOG6038ZS.

    Enzyme and pathway databases

    UniPathwayi UPA00538 ; UER00593 .
    BioCyci PCAR338963:GKDU-394-MONOMER.

    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. "Identification and molecular characterization of the aco genes encoding the Pelobacter carbinolicus acetoin dehydrogenase enzyme system."
      Oppermann F.B., Steinbuechel A.
      J. Bacteriol. 176:469-485(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    2. "Complete sequence of Pelobacter carbinolicus DSM 2380."
      Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T., Hammon N., Israni S., Pitluck S., Chertkov O., Schmutz J., Larimer F., Land M., Kyrpides N., Ivanova N., Richardson P.
      Submitted (OCT-2005) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: DSM 2380 / Gra Bd 1.

    Entry informationi

    Entry nameiLIPA_PELCD
    AccessioniPrimary (citable) accession number: Q57390
    Secondary accession number(s): Q3A7N8
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 15, 1998
    Last sequence update: December 20, 2005
    Last modified: October 1, 2014
    This is version 105 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic 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