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O32129

- LIPA_BACSU

UniProt

O32129 - LIPA_BACSU

Protein

Lipoyl synthase

Gene

lipA

Organism
Bacillus subtilis (strain 168)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 115 (01 Oct 2014)
      Sequence version 2 (30 May 2000)
      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.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

    Protein modification; protein lipoylation via endogenous pathway; protein N(6)-(lipoyl)lysine from octanoyl-[acyl-carrier-protein].

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi40 – 401Iron-sulfur 1 (4Fe-4S)UniRule annotation
    Metal bindingi45 – 451Iron-sulfur 1 (4Fe-4S)UniRule annotation
    Metal bindingi51 – 511Iron-sulfur 1 (4Fe-4S)UniRule annotation
    Metal bindingi67 – 671Iron-sulfur 2 (4Fe-4S-S-AdoMet)UniRule annotation
    Metal bindingi71 – 711Iron-sulfur 2 (4Fe-4S-S-AdoMet)UniRule annotation
    Metal bindingi74 – 741Iron-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
    3. metal ion binding Source: UniProtKB-KW

    GO - Biological processi

    1. lipoate biosynthetic process Source: UniProtKB
    2. protein lipoylation Source: UniProtKB

    Keywords - Molecular functioni

    Transferase

    Keywords - Ligandi

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

    Enzyme and pathway databases

    BioCyciBSUB:BSU32330-MONOMER.
    MetaCyc:BSU32330-MONOMER.

    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:yutB
    Ordered Locus Names:BSU32330
    OrganismiBacillus subtilis (strain 168)
    Taxonomic identifieri224308 [NCBI]
    Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus
    ProteomesiUP000001570: Chromosome

    Organism-specific databases

    GenoListiBSU32330. [Micado]

    Subcellular locationi

    Cytoplasm UniRule annotation

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Disruption phenotypei

    Disruption of this gene interrupts lipoate-dependent reactions, which strongly inhibits growth in minimal medium, impairing the generation of branched-chain fatty acids and leading to accumulation of copious amounts of straight-chain saturated fatty acids in B.subtilis membranes.1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 298298Lipoyl synthasePRO_0000102288Add
    BLAST

    Proteomic databases

    PaxDbiO32129.

    Interactioni

    Protein-protein interaction databases

    STRINGi224308.BSU32330.

    Structurei

    3D structure databases

    ProteinModelPortaliO32129.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

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

    Phylogenomic databases

    eggNOGiCOG0320.
    HOGENOMiHOG000235998.
    KOiK03644.
    OMAiHPHIPTK.
    OrthoDBiEOG6038ZS.
    PhylomeDBiO32129.

    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.

    O32129-1 [UniParc]FASTAAdd to Basket

    « Hide

    MAKKDEHLRK PEWLKIKLNT NENYTGLKKL MRENNLHTVC EEAKCPNIHE    50
    CWAVRRTATF MILGSVCTRA CRFCAVKTGL PTELDLQEPE RVADSVALMN 100
    LKHAVITAVA RDDQKDGGAG IFAETVRAIR RKSPFTTIEV LPSDMGGNYD 150
    NLKTLMDTRP DILNHNIETV RRLTPRVRAR ATYDRSLEFL RRAKEMQPDI 200
    PTKSSIMIGL GETKEEIIEV MDDLLANNVD IMAIGQYLQP TKKHLKVQKY 250
    YHPDEFAELK EIAMQKGFSH CEAGPLVRSS YHADEQVNEA SKKRQAQA 298
    Length:298
    Mass (Da):33,921
    Last modified:May 30, 2000 - v2
    Checksum:iE6BEEB81C6ECC6FF
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AL009126 Genomic DNA. Translation: CAB15223.2.
    PIRiD70023.
    RefSeqiNP_391113.2. NC_000964.3.

    Genome annotation databases

    EnsemblBacteriaiCAB15223; CAB15223; BSU32330.
    GeneIDi938861.
    KEGGibsu:BSU32330.
    PATRICi18978438. VBIBacSub10457_3382.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AL009126 Genomic DNA. Translation: CAB15223.2 .
    PIRi D70023.
    RefSeqi NP_391113.2. NC_000964.3.

    3D structure databases

    ProteinModelPortali O32129.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 224308.BSU32330.

    Proteomic databases

    PaxDbi O32129.

    Protocols and materials databases

    DNASUi 938861.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai CAB15223 ; CAB15223 ; BSU32330 .
    GeneIDi 938861.
    KEGGi bsu:BSU32330.
    PATRICi 18978438. VBIBacSub10457_3382.

    Organism-specific databases

    GenoListi BSU32330. [Micado ]

    Phylogenomic databases

    eggNOGi COG0320.
    HOGENOMi HOG000235998.
    KOi K03644.
    OMAi HPHIPTK.
    OrthoDBi EOG6038ZS.
    PhylomeDBi O32129.

    Enzyme and pathway databases

    BioCyci BSUB:BSU32330-MONOMER.
    MetaCyc:BSU32330-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. "The complete genome sequence of the Gram-positive bacterium Bacillus subtilis."
      Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V., Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R., Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S., Bruschi C.V.
      , Caldwell B., Capuano V., Carter N.M., Choi S.-K., Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F., Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D., Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M., Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P., Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K., Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S., Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y., Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G., Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J., Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C., Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S., Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B., Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S., Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M., Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y., Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J., Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A., Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M., Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S., Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E., Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K., Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E., Yoshikawa H., Danchin A.
      Nature 390:249-256(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: 168.
    2. "A lipA (yutB) mutant, encoding lipoic acid synthase, provides insight into the interplay between branched-chain and unsaturated fatty acid biosynthesis in Bacillus subtilis."
      Martin N., Lombardia E., Altabe S.G., de Mendoza D., Mansilla M.C.
      J. Bacteriol. 191:7447-7455(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION AS A LIPOYL SYNTHASE, PATHWAY, DISRUPTION PHENOTYPE.
      Strain: 168 / JH642.

    Entry informationi

    Entry nameiLIPA_BACSU
    AccessioniPrimary (citable) accession number: O32129
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 30, 2000
    Last sequence update: May 30, 2000
    Last modified: October 1, 2014
    This is version 115 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. Bacillus subtilis
      Bacillus subtilis (strain 168): entries, gene names and cross-references to SubtiList
    2. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3