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P16440

- RISA_BACSU

UniProt

P16440 - RISA_BACSU

Protein

Riboflavin synthase

Gene

ribE

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 118 (01 Oct 2014)
      Sequence version 2 (01 Feb 1991)
      Previous versions | rss
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    Functioni

    Catalyzes the dismutation of two molecules of 6,7-dimethyl-8-ribityllumazine, resulting in the formation of riboflavin and 5-amino-6-(D-ribitylamino)uracil.1 Publication

    Catalytic activityi

    2 6,7-dimethyl-8-(1-D-ribityl)lumazine = riboflavin + 4-(1-D-ribitylamino)-5-amino-2,6-dihydroxypyrimidine.1 Publication

    Enzyme regulationi

    Is activated by sulfite ions.1 Publication

    Kineticsi

    1. KM=14 µM for 6,7-dimethyl-8-(1-D-ribityl)lumazine1 Publication

    pH dependencei

    Optimum pH is 7.4.1 Publication

    Pathwayi

    GO - Molecular functioni

    1. oxidoreductase activity Source: InterPro
    2. riboflavin synthase activity Source: UniProtKB-EC

    GO - Biological processi

    1. riboflavin biosynthetic process Source: UniProtKB-UniPathway

    Keywords - Molecular functioni

    Transferase

    Keywords - Biological processi

    Riboflavin biosynthesis

    Enzyme and pathway databases

    BioCyciBSUB:BSU23270-MONOMER.
    MetaCyc:MONOMER-14608.
    SABIO-RKP16440.
    UniPathwayiUPA00275; UER00405.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Riboflavin synthase (EC:2.5.1.9)
    Short name:
    RS
    Alternative name(s):
    Heavy riboflavin synthase alpha subunit
    Short name:
    HRS alpha subunit
    Light riboflavin synthase
    Gene namesi
    Name:ribE
    Synonyms:ribB
    Ordered Locus Names:BSU23270
    OrganismiBacillus subtilis (strain 168)
    Taxonomic identifieri224308 [NCBI]
    Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus
    ProteomesiUP000001570: Chromosome

    Organism-specific databases

    GenoListiBSU23270. [Micado]

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 215215Riboflavin synthasePRO_0000068159Add
    BLAST

    Proteomic databases

    PaxDbiP16440.

    Interactioni

    Subunit structurei

    Homotrimer. Can interact with 6,7-dimethyl-8-ribityllumazine synthase, forming a lumazine synthase/riboflavin synthase complex, also designated as 'heavy riboflavin synthase complex', which consists of a trimer of riboflavin synthase enclosed within an icosahedral structure composed of 60 subunits of 6,7-dimethyl-8-ribityllumazine synthase.3 Publications

    Protein-protein interaction databases

    STRINGi224308.BSU23270.

    Structurei

    3D structure databases

    ProteinModelPortaliP16440.
    SMRiP16440. Positions 1-198.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Repeati1 – 9696Lumazine-binding 1Add
    BLAST
    Repeati97 – 19397Lumazine-binding 2Add
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni4 – 63Substrate bindingBy similarity
    Regioni47 – 493Substrate bindingBy similarity
    Regioni61 – 666Substrate bindingBy similarity

    Sequence similaritiesi

    Contains 2 lumazine-binding repeats.PROSITE-ProRule annotation

    Keywords - Domaini

    Repeat

    Phylogenomic databases

    eggNOGiCOG0307.
    HOGENOMiHOG000151757.
    KOiK00793.
    OMAiANAVYYE.
    OrthoDBiEOG6VMTQH.
    PhylomeDBiP16440.

    Family and domain databases

    Gene3Di2.40.30.20. 2 hits.
    InterProiIPR023366. ATPase_asu-like.
    IPR001783. Lumazine-bd.
    IPR026017. Lumazine-bd_dom.
    IPR017938. Riboflavin_synthase-like_b-brl.
    [Graphical view]
    PANTHERiPTHR21098. PTHR21098. 1 hit.
    PfamiPF00677. Lum_binding. 2 hits.
    [Graphical view]
    PIRSFiPIRSF000498. Riboflavin_syn_A. 1 hit.
    SUPFAMiSSF63380. SSF63380. 2 hits.
    TIGRFAMsiTIGR00187. ribE. 1 hit.
    PROSITEiPS51177. LUMAZINE_BIND. 2 hits.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P16440-1 [UniParc]FASTAAdd to Basket

    « Hide

    MFTGIIEETG TIESMKKAGH AMALTIKCSK ILEDVHLGDS IAVNGICLTV    50
    TDFTKNQFTV DVMPETVKAT SLNDLTKGSK VNLERAMAAN GRFGGHFVSG 100
    HVDGTAEITR IEEKSNAVYY DLKMDPSLTK TLVLKGSITV DGVSLTIFGL 150
    TEDTVTISLI PHTISETIFS EKTIGSKVNI ECDMIGKYMY RFLHKANENK 200
    TQQTITKAFL SENGF 215
    Length:215
    Mass (Da):23,481
    Last modified:February 1, 1991 - v2
    Checksum:i5B2A694C078B3600
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L09228 Genomic DNA. Translation: AAA67482.1.
    X51510 Genomic DNA. Translation: CAA35879.1.
    AL009126 Genomic DNA. Translation: CAB14259.1.
    PIRiS45544. A35711.
    RefSeqiNP_390208.1. NC_000964.3.
    WP_004398505.1. NZ_CM000487.1.

    Genome annotation databases

    EnsemblBacteriaiCAB14259; CAB14259; BSU23270.
    GeneIDi938947.
    KEGGibsu:BSU23270.
    PATRICi18976471. VBIBacSub10457_2426.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L09228 Genomic DNA. Translation: AAA67482.1 .
    X51510 Genomic DNA. Translation: CAA35879.1 .
    AL009126 Genomic DNA. Translation: CAB14259.1 .
    PIRi S45544. A35711.
    RefSeqi NP_390208.1. NC_000964.3.
    WP_004398505.1. NZ_CM000487.1.

    3D structure databases

    ProteinModelPortali P16440.
    SMRi P16440. Positions 1-198.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 224308.BSU23270.

    Proteomic databases

    PaxDbi P16440.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai CAB14259 ; CAB14259 ; BSU23270 .
    GeneIDi 938947.
    KEGGi bsu:BSU23270.
    PATRICi 18976471. VBIBacSub10457_2426.

    Organism-specific databases

    GenoListi BSU23270. [Micado ]

    Phylogenomic databases

    eggNOGi COG0307.
    HOGENOMi HOG000151757.
    KOi K00793.
    OMAi ANAVYYE.
    OrthoDBi EOG6VMTQH.
    PhylomeDBi P16440.

    Enzyme and pathway databases

    UniPathwayi UPA00275 ; UER00405 .
    BioCyci BSUB:BSU23270-MONOMER.
    MetaCyc:MONOMER-14608.
    SABIO-RK P16440.

    Family and domain databases

    Gene3Di 2.40.30.20. 2 hits.
    InterProi IPR023366. ATPase_asu-like.
    IPR001783. Lumazine-bd.
    IPR026017. Lumazine-bd_dom.
    IPR017938. Riboflavin_synthase-like_b-brl.
    [Graphical view ]
    PANTHERi PTHR21098. PTHR21098. 1 hit.
    Pfami PF00677. Lum_binding. 2 hits.
    [Graphical view ]
    PIRSFi PIRSF000498. Riboflavin_syn_A. 1 hit.
    SUPFAMi SSF63380. SSF63380. 2 hits.
    TIGRFAMsi TIGR00187. ribE. 1 hit.
    PROSITEi PS51177. LUMAZINE_BIND. 2 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Riboflavin synthases of Bacillus subtilis. Purification and amino acid sequence of the alpha subunit."
      Schott K., Kellermann J., Lottspeich F., Bacher A.
      J. Biol. Chem. 265:4204-4209(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 1-202, SUBUNIT.
    2. Mironov V.N.
      Thesis (1989), USSR Academy of Sciences, Russia
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: 168 / SHGW.
    3. "The organization of the Bacillus subtilis 168 chromosome region between the spoVA and serA genetic loci, based on sequence data."
      Sorokin A.V., Zumstein E., Azevedo V., Ehrlich S.D., Serror P.
      Mol. Microbiol. 10:385-395(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: 168 / Marburg / ATCC 6051 / DSM 10 / JCM 1465 / NBRC 13719 / NCIMB 3610 / VKM B-501.
    4. "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.
    5. "Riboflavin synthases of Bacillus subtilis. Purification and properties."
      Bacher A., Baur R., Eggers U., Harders H.D., Otto M.K., Schnepple H.
      J. Biol. Chem. 255:632-637(1980) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, CATALYTIC ACTIVITY, ENZYME REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT.
    6. "Heavy riboflavin synthase from Bacillus subtilis. Quaternary structure and reaggregation."
      Bacher A., Ludwig H.C., Schnepple H., Ben-Shaul Y.
      J. Mol. Biol. 187:75-86(1986) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBUNIT.

    Entry informationi

    Entry nameiRISA_BACSU
    AccessioniPrimary (citable) accession number: P16440
    Secondary accession number(s): P17619
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 1, 1990
    Last sequence update: February 1, 1991
    Last modified: October 1, 2014
    This is version 118 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, Direct protein sequencing, 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