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P0AFU8

- RISA_ECOLI

UniProt

P0AFU8 - RISA_ECOLI

Protein

Riboflavin synthase

Gene

ribC

Organism
Escherichia coli (strain K12)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 78 (01 Oct 2014)
      Sequence version 1 (20 Dec 2005)
      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

    Pathwayi

    GO - Molecular functioni

    1. oxidoreductase activity Source: InterPro
    2. riboflavin synthase activity Source: EcoCyc

    GO - Biological processi

    1. riboflavin biosynthetic process Source: EcoCyc

    Keywords - Molecular functioni

    Transferase

    Keywords - Biological processi

    Riboflavin biosynthesis

    Enzyme and pathway databases

    BioCyciEcoCyc:RIBOFLAVIN-SYN-MONOMER.
    ECOL316407:JW1654-MONOMER.
    MetaCyc:RIBOFLAVIN-SYN-MONOMER.
    UniPathwayiUPA00275; UER00405.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Riboflavin synthase (EC:2.5.1.9)
    Short name:
    RS
    Gene namesi
    Name:ribC
    Synonyms:ribE
    Ordered Locus Names:b1662, JW1654
    OrganismiEscherichia coli (strain K12)
    Taxonomic identifieri83333 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
    ProteomesiUP000000318: Chromosome, UP000000625: Chromosome

    Organism-specific databases

    EcoGeneiEG11406. ribC.

    Pathology & Biotechi

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 213213Riboflavin synthasePRO_0000068166Add
    BLAST

    Proteomic databases

    PaxDbiP0AFU8.
    PRIDEiP0AFU8.

    2D gel databases

    SWISS-2DPAGEP0AFU8.

    Expressioni

    Gene expression databases

    GenevestigatoriP0AFU8.

    Interactioni

    Subunit structurei

    Homotrimer. Unlike in B.subtilis, does not interact with 6,7-dimethyl-8-ribityllumazine synthase.3 Publications

    Protein-protein interaction databases

    DIPiDIP-47865N.
    IntActiP0AFU8. 3 interactions.
    STRINGi511145.b1662.

    Structurei

    Secondary structure

    1
    213
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi8 – 1710
    Beta strandi19 – 279
    Helixi30 – 323
    Beta strandi41 – 444
    Beta strandi47 – 559
    Beta strandi58 – 647
    Helixi65 – 706
    Helixi72 – 754
    Beta strandi81 – 866
    Beta strandi105 – 11511
    Beta strandi118 – 1269
    Helixi128 – 1336
    Beta strandi139 – 1424
    Beta strandi145 – 1484
    Beta strandi154 – 1618
    Helixi163 – 1686
    Helixi171 – 1733
    Beta strandi179 – 1846
    Helixi186 – 20419

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1HZENMR-A/B1-97[»]
    1I18NMR-A/B1-97[»]
    1I8DX-ray2.00A/B/C1-213[»]
    1PKVX-ray2.60A/B1-97[»]
    ProteinModelPortaliP0AFU8.
    SMRiP0AFU8. Positions 1-206.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP0AFU8.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Repeati1 – 9797Lumazine-binding 1Add
    BLAST
    Repeati98 – 19598Lumazine-binding 2Add
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni4 – 63Substrate binding
    Regioni48 – 503Substrate binding
    Regioni62 – 676Substrate binding

    Sequence similaritiesi

    Contains 2 lumazine-binding repeats.PROSITE-ProRule annotation

    Keywords - Domaini

    Repeat

    Phylogenomic databases

    eggNOGiCOG0307.
    HOGENOMiHOG000151758.
    KOiK00793.
    OMAiNHQIWFR.
    OrthoDBiEOG6VMTQH.
    PhylomeDBiP0AFU8.

    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.

    P0AFU8-1 [UniParc]FASTAAdd to Basket

    « Hide

    MFTGIVQGTA KLVSIDEKPN FRTHVVELPD HMLDGLETGA SVAHNGCCLT    50
    VTEINGNHVS FDLMKETLRI TNLGDLKVGD WVNVERAAKF SDEIGGHLMS 100
    GHIMTTAEVA KILTSENNRQ IWFKVQDSQL MKYILYKGFI GIDGISLTVG 150
    EVTPTRFCVH LIPETLERTT LGKKKLGARV NIEIDPQTQA VVDTVERVLA 200
    ARENAMNQPG TEA 213
    Length:213
    Mass (Da):23,445
    Last modified:December 20, 2005 - v1
    Checksum:iCD1C7E40E4AC88B6
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X69109 Genomic DNA. Translation: CAA48861.1.
    U68703 Genomic DNA. Translation: AAB47940.1.
    U00096 Genomic DNA. Translation: AAC74734.1.
    AP009048 Genomic DNA. Translation: BAA15429.1.
    PIRiS28526.
    RefSeqiNP_416179.1. NC_000913.3.
    YP_489926.1. NC_007779.1.

    Genome annotation databases

    EnsemblBacteriaiAAC74734; AAC74734; b1662.
    BAA15429; BAA15429; BAA15429.
    GeneIDi12932660.
    945848.
    KEGGiecj:Y75_p1639.
    eco:b1662.
    PATRICi32118630. VBIEscCol129921_1735.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X69109 Genomic DNA. Translation: CAA48861.1 .
    U68703 Genomic DNA. Translation: AAB47940.1 .
    U00096 Genomic DNA. Translation: AAC74734.1 .
    AP009048 Genomic DNA. Translation: BAA15429.1 .
    PIRi S28526.
    RefSeqi NP_416179.1. NC_000913.3.
    YP_489926.1. NC_007779.1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1HZE NMR - A/B 1-97 [» ]
    1I18 NMR - A/B 1-97 [» ]
    1I8D X-ray 2.00 A/B/C 1-213 [» ]
    1PKV X-ray 2.60 A/B 1-97 [» ]
    ProteinModelPortali P0AFU8.
    SMRi P0AFU8. Positions 1-206.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    DIPi DIP-47865N.
    IntActi P0AFU8. 3 interactions.
    STRINGi 511145.b1662.

    Chemistry

    DrugBanki DB00140. Riboflavin.

    2D gel databases

    SWISS-2DPAGE P0AFU8.

    Proteomic databases

    PaxDbi P0AFU8.
    PRIDEi P0AFU8.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAC74734 ; AAC74734 ; b1662 .
    BAA15429 ; BAA15429 ; BAA15429 .
    GeneIDi 12932660.
    945848.
    KEGGi ecj:Y75_p1639.
    eco:b1662.
    PATRICi 32118630. VBIEscCol129921_1735.

    Organism-specific databases

    EchoBASEi EB1378.
    EcoGenei EG11406. ribC.

    Phylogenomic databases

    eggNOGi COG0307.
    HOGENOMi HOG000151758.
    KOi K00793.
    OMAi NHQIWFR.
    OrthoDBi EOG6VMTQH.
    PhylomeDBi P0AFU8.

    Enzyme and pathway databases

    UniPathwayi UPA00275 ; UER00405 .
    BioCyci EcoCyc:RIBOFLAVIN-SYN-MONOMER.
    ECOL316407:JW1654-MONOMER.
    MetaCyc:RIBOFLAVIN-SYN-MONOMER.

    Miscellaneous databases

    EvolutionaryTracei P0AFU8.
    PROi P0AFU8.

    Gene expression databases

    Genevestigatori P0AFU8.

    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. "Cloning, sequencing, mapping and hyperexpression of the ribC gene coding for riboflavin synthase of Escherichia coli."
      Eberhardt S.M.R., Richter G., Gimbel W., Werner T., Bacher A.
      Eur. J. Biochem. 242:712-719(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, SUBUNIT.
      Strain: K12 / RR28.
    2. "Analysis of the boundaries of Salmonella pathogenicity island 2 and the corresponding chromosomal region of Escherichia coli K-12."
      Hensel M., Shea J.E., Baeumler A.J., Gleeson C., Blattner F.R., Holden D.W.
      J. Bacteriol. 179:1105-1111(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: K12 / MG1655 / ATCC 47076.
    3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
    4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: K12 / MG1655 / ATCC 47076.
    5. "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
      Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
      Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
    6. "The solution structure of the N-terminal domain of riboflavin synthase."
      Truffault V., Coles M., Diercks T., Abelmann K., Eberhardt S., Luttgen H., Bacher A., Kessler H.
      J. Mol. Biol. 309:949-960(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR OF 1-97 IN COMPLEX WITH RIBOFLAVIN.
    7. Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
    8. "The structure of the N-terminal domain of riboflavin synthase in complex with riboflavin at 2.6A resolution."
      Meining W., Eberhardt S., Bacher A., Ladenstein R.
      J. Mol. Biol. 331:1053-1063(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.60 ANGSTROMS) OF 1-97 IN COMPLEX WITH RIBOFLAVIN.

    Entry informationi

    Entry nameiRISA_ECOLI
    AccessioniPrimary (citable) accession number: P0AFU8
    Secondary accession number(s): P29015
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 20, 2005
    Last sequence update: December 20, 2005
    Last modified: October 1, 2014
    This is version 78 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

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Escherichia coli
      Escherichia coli (strain K12): entries and cross-references to EcoGene
    2. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    3. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    4. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3