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Q2K8V9

- LIPA_RHIEC

UniProt

Q2K8V9 - LIPA_RHIEC

Protein

Lipoyl synthase

Gene

lipA

Organism
Rhizobium etli (strain CFN 42 / ATCC 51251)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 61 (01 Oct 2014)
      Sequence version 1 (07 Mar 2006)
      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 bindingi61 – 611Iron-sulfur 1 (4Fe-4S)UniRule annotation
    Metal bindingi66 – 661Iron-sulfur 1 (4Fe-4S)UniRule annotation
    Metal bindingi72 – 721Iron-sulfur 1 (4Fe-4S)UniRule annotation
    Metal bindingi87 – 871Iron-sulfur 2 (4Fe-4S-S-AdoMet)UniRule annotation
    Metal bindingi91 – 911Iron-sulfur 2 (4Fe-4S-S-AdoMet)UniRule annotation
    Metal bindingi94 – 941Iron-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

    BioCyciRETL347834:GJJ0-1952-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
    Ordered Locus Names:RHE_CH01941
    OrganismiRhizobium etli (strain CFN 42 / ATCC 51251)
    Taxonomic identifieri347834 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaAlphaproteobacteriaRhizobialesRhizobiaceaeRhizobium/Agrobacterium groupRhizobium
    ProteomesiUP000001936: 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 – 323323Lipoyl synthasePRO_1000012259Add
    BLAST

    Interactioni

    Protein-protein interaction databases

    STRINGi347834.RHE_CH01941.

    Structurei

    3D structure databases

    ProteinModelPortaliQ2K8V9.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

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

    Phylogenomic databases

    eggNOGiCOG0320.
    HOGENOMiHOG000235997.
    KOiK03644.
    OMAiPEEPYNT.
    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.

    Q2K8V9-1 [UniParc]FASTAAdd to Basket

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    MVTILDTINP DAKRVRHPEK AHRPDTEVMR KPDWIRVKAP TSKGYAETRA    50
    IVKEHKLVTV CEEAGCPNIG ECWDKKHATF MIMGEICTRA CAFCNVATGK 100
    PNALDMDEPE NVAKAVREMG LSHVVITSVD RDDLEDGGAE HFEKVIWAIR 150
    SASPATTIEI LTPDFLKKPG ALERVVAAKP DVFNHNMETV AGNYLTVRPG 200
    ARYFHSIRLL QRVKELDPTM FTKSGIMVGL GEERNEVLQL MDDLRTADVD 250
    FLTIGQYLQP TRKHHKVESF VTPEEFKSYE TVAYSKGFLM VASSPLTRSS 300
    HHAGDDFARL RAAREKKLLM AAE 323
    Length:323
    Mass (Da):36,218
    Last modified:March 7, 2006 - v1
    Checksum:i22B1C443F471E041
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti92 – 921A → R in CAA72400. (PubMed:9141657)Curated
    Sequence conflicti100 – 1001K → Q in CAA72400. (PubMed:9141657)Curated
    Sequence conflicti118 – 1225EMGLS → RWAQ in CAA72400. (PubMed:9141657)Curated
    Sequence conflicti140 – 1401E → Q in CAA72400. (PubMed:9141657)Curated
    Sequence conflicti317 – 3182KL → NV in CAA72400. (PubMed:9141657)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Y11708 Genomic DNA. Translation: CAA72400.1.
    CP000133 Genomic DNA. Translation: ABC90727.1.
    RefSeqiYP_469454.1. NC_007761.1.

    Genome annotation databases

    EnsemblBacteriaiABC90727; ABC90727; RHE_CH01941.
    GeneIDi3893979.
    KEGGiret:RHE_CH01941.
    PATRICi23085366. VBIRhiEtl108884_2339.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Y11708 Genomic DNA. Translation: CAA72400.1 .
    CP000133 Genomic DNA. Translation: ABC90727.1 .
    RefSeqi YP_469454.1. NC_007761.1.

    3D structure databases

    ProteinModelPortali Q2K8V9.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 347834.RHE_CH01941.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai ABC90727 ; ABC90727 ; RHE_CH01941 .
    GeneIDi 3893979.
    KEGGi ret:RHE_CH01941.
    PATRICi 23085366. VBIRhiEtl108884_2339.

    Phylogenomic databases

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

    Enzyme and pathway databases

    UniPathwayi UPA00538 ; UER00593 .
    BioCyci RETL347834:GJJ0-1952-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. "Cloning and transcriptional analysis of the lipA (lipoic acid synthetase) gene from Rhizobium etli."
      Tate R., Riccio A., Iaccarino M., Patriarca E.J.
      FEMS Microbiol. Lett. 149:165-172(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: CE3.
    2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: CFN 42 / ATCC 51251.

    Entry informationi

    Entry nameiLIPA_RHIEC
    AccessioniPrimary (citable) accession number: Q2K8V9
    Secondary accession number(s): O05941
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 15, 2008
    Last sequence update: March 7, 2006
    Last modified: October 1, 2014
    This is version 61 of the entry and version 1 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