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Protein

Riboflavin synthase

Gene

ribE

Organism
Bacillus subtilis (strain 168)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

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

    Pathway:iriboflavin biosynthesis

    This protein is involved in step 2 of the subpathway that synthesizes riboflavin from 2-hydroxy-3-oxobutyl phosphate and 5-amino-6-(D-ribitylamino)uracil.
    Proteins known to be involved in the 2 steps of the subpathway in this organism are:
    1. 6,7-dimethyl-8-ribityllumazine synthase (ribH)
    2. Riboflavin synthase (ribE)
    This subpathway is part of the pathway riboflavin biosynthesis, which is itself part of Cofactor biosynthesis.
    View all proteins of this organism that are known to be involved in the subpathway that synthesizes riboflavin from 2-hydroxy-3-oxobutyl phosphate and 5-amino-6-(D-ribitylamino)uracil, the pathway riboflavin biosynthesis and in Cofactor biosynthesis.

    GO - Molecular functioni

    GO - Biological processi

    Complete GO annotation...

    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 Componenti: 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.Bsubs1_010100012776.

    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.
    InParanoidiP16440.
    KOiK00793.
    OMAiVMPETVK.
    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

            10         20         30         40         50
    MFTGIIEETG TIESMKKAGH AMALTIKCSK ILEDVHLGDS IAVNGICLTV
    60 70 80 90 100
    TDFTKNQFTV DVMPETVKAT SLNDLTKGSK VNLERAMAAN GRFGGHFVSG
    110 120 130 140 150
    HVDGTAEITR IEEKSNAVYY DLKMDPSLTK TLVLKGSITV DGVSLTIFGL
    160 170 180 190 200
    TEDTVTISLI PHTISETIFS EKTIGSKVNI ECDMIGKYMY RFLHKANENK
    210
    TQQTITKAFL SENGF
    Length:215
    Mass (Da):23,481
    Last modified:February 1, 1991 - v2
    Checksum:i5B2A694C078B3600
    GO

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    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_JNCM01000036.1.

    Genome annotation databases

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

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    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_JNCM01000036.1.

    3D structure databases

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

    Protein-protein interaction databases

    STRINGi224308.Bsubs1_010100012776.

    Proteomic databases

    PaxDbiP16440.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

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

    Organism-specific databases

    GenoListiBSU23270. [Micado]

    Phylogenomic databases

    eggNOGiCOG0307.
    HOGENOMiHOG000151757.
    InParanoidiP16440.
    KOiK00793.
    OMAiVMPETVK.
    OrthoDBiEOG6VMTQH.
    PhylomeDBiP16440.

    Enzyme and pathway databases

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

    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]
    ProtoNetiSearch...

    Publicationsi

    « Hide 'large scale' publications
    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: July 22, 2015
    This is version 122 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

    Similar proteinsi

    Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
    100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
    90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
    50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.