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P54575

- RIBC_BACSU

UniProt

P54575 - RIBC_BACSU

Protein

Riboflavin biosynthesis protein RibC

Gene

ribC

Organism
Bacillus subtilis (strain 168)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 102 (01 Oct 2014)
      Sequence version 2 (29 Aug 2003)
      Previous versions | rss
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    Functioni

    Catalytic activityi

    ATP + riboflavin = ADP + FMN.
    ATP + FMN = diphosphate + FAD.

    Pathwayi

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-KW
    2. FMN adenylyltransferase activity Source: UniProtKB-EC
    3. riboflavin kinase activity Source: UniProtKB-EC

    GO - Biological processi

    1. FAD biosynthetic process Source: UniProtKB-UniPathway
    2. FMN biosynthetic process Source: UniProtKB-UniPathway
    3. riboflavin biosynthetic process Source: InterPro

    Keywords - Molecular functioni

    Kinase, Nucleotidyltransferase, Transferase

    Keywords - Ligandi

    ATP-binding, FAD, Flavoprotein, FMN, Nucleotide-binding

    Enzyme and pathway databases

    BioCyciBSUB:BSU16670-MONOMER.
    MetaCyc:MONOMER-14605.
    UniPathwayiUPA00276; UER00406.
    UPA00277; UER00407.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Riboflavin biosynthesis protein RibC
    Including the following 2 domains:
    Riboflavin kinase (EC:2.7.1.26)
    Alternative name(s):
    Flavokinase
    FMN adenylyltransferase (EC:2.7.7.2)
    Alternative name(s):
    FAD pyrophosphorylase
    FAD synthase
    Gene namesi
    Name:ribC
    Ordered Locus Names:BSU16670
    OrganismiBacillus subtilis (strain 168)
    Taxonomic identifieri224308 [NCBI]
    Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus
    ProteomesiUP000001570: Chromosome

    Organism-specific databases

    GenoListiBSU16670. [Micado]

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 316316Riboflavin biosynthesis protein RibCPRO_0000194133Add
    BLAST

    Proteomic databases

    PaxDbiP54575.

    Interactioni

    Protein-protein interaction databases

    STRINGi224308.BSU16670.

    Structurei

    3D structure databases

    ProteinModelPortaliP54575.
    SMRiP54575. Positions 1-310.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the RibF family.Curated

    Phylogenomic databases

    eggNOGiCOG0196.
    HOGENOMiHOG000006844.
    KOiK11753.
    OMAiFEPQPME.
    OrthoDBiEOG6QP0ZV.
    PhylomeDBiP54575.

    Family and domain databases

    Gene3Di2.40.30.30. 1 hit.
    3.40.50.620. 1 hit.
    InterProiIPR004821. Cyt_trans-like.
    IPR015864. FAD_synthase.
    IPR023468. Riboflavin_kinase.
    IPR002606. Riboflavin_kinase_bac.
    IPR015865. Riboflavin_kinase_bac/euk.
    IPR023465. Riboflavin_kinase_domain.
    IPR014729. Rossmann-like_a/b/a_fold.
    [Graphical view]
    PANTHERiPTHR22749. PTHR22749. 1 hit.
    PfamiPF06574. FAD_syn. 1 hit.
    PF01687. Flavokinase. 1 hit.
    [Graphical view]
    PIRSFiPIRSF004491. FAD_Synth. 1 hit.
    SMARTiSM00904. Flavokinase. 1 hit.
    [Graphical view]
    SUPFAMiSSF82114. SSF82114. 1 hit.
    TIGRFAMsiTIGR00125. cyt_tran_rel. 1 hit.
    TIGR00083. ribF. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    P54575-1 [UniParc]FASTAAdd to Basket

    « Hide

    MKTIHITHPH HLIKEEQAKS VMALGYFDGV HLGHQKVIGT AKQIAEEKGL    50
    TLAVMTFHPH PSHVLGRDKE PKDLITPLED KINQIEQLGT EVLYVVKFNE 100
    VFASLSPKQF IDQYIIGLNV QHAVAGFDFT YGKYGKGTMK TMPDDLDGKA 150
    GCTMVEKLTE QDKKISSSYI RTALQNGDVE LANVLLGQPY FIKGIVIHGD 200
    KRGRTIGFPT ANVGLNNSYI VPPTGVYAVK AEVNGEVYNG VCNIGYKPTF 250
    YEKRPEQPSI EVNLFDFNQE VYGAAIKIEW YKRIRSERKF NGIKELTEQI 300
    EKDKQEAIRY FSNLRK 316
    Length:316
    Mass (Da):35,662
    Last modified:August 29, 2003 - v2
    Checksum:i0B8F11D356B7D7B9
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti199 – 1991G → N in CAA64624. (PubMed:9454067)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X95312 Genomic DNA. Translation: CAA64624.1.
    Z80835 Genomic DNA. Translation: CAB02559.1.
    AL009126 Genomic DNA. Translation: CAB13540.1.
    PIRiD69692.
    RefSeqiNP_389549.1. NC_000964.3.

    Genome annotation databases

    EnsemblBacteriaiCAB13540; CAB13540; BSU16670.
    GeneIDi938110.
    KEGGibsu:BSU16670.
    PATRICi18975141. VBIBacSub10457_1762.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X95312 Genomic DNA. Translation: CAA64624.1 .
    Z80835 Genomic DNA. Translation: CAB02559.1 .
    AL009126 Genomic DNA. Translation: CAB13540.1 .
    PIRi D69692.
    RefSeqi NP_389549.1. NC_000964.3.

    3D structure databases

    ProteinModelPortali P54575.
    SMRi P54575. Positions 1-310.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 224308.BSU16670.

    Proteomic databases

    PaxDbi P54575.

    Protocols and materials databases

    DNASUi 938110.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai CAB13540 ; CAB13540 ; BSU16670 .
    GeneIDi 938110.
    KEGGi bsu:BSU16670.
    PATRICi 18975141. VBIBacSub10457_1762.

    Organism-specific databases

    GenoListi BSU16670. [Micado ]

    Phylogenomic databases

    eggNOGi COG0196.
    HOGENOMi HOG000006844.
    KOi K11753.
    OMAi FEPQPME.
    OrthoDBi EOG6QP0ZV.
    PhylomeDBi P54575.

    Enzyme and pathway databases

    UniPathwayi UPA00276 ; UER00406 .
    UPA00277 ; UER00407 .
    BioCyci BSUB:BSU16670-MONOMER.
    MetaCyc:MONOMER-14605.

    Family and domain databases

    Gene3Di 2.40.30.30. 1 hit.
    3.40.50.620. 1 hit.
    InterProi IPR004821. Cyt_trans-like.
    IPR015864. FAD_synthase.
    IPR023468. Riboflavin_kinase.
    IPR002606. Riboflavin_kinase_bac.
    IPR015865. Riboflavin_kinase_bac/euk.
    IPR023465. Riboflavin_kinase_domain.
    IPR014729. Rossmann-like_a/b/a_fold.
    [Graphical view ]
    PANTHERi PTHR22749. PTHR22749. 1 hit.
    Pfami PF06574. FAD_syn. 1 hit.
    PF01687. Flavokinase. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF004491. FAD_Synth. 1 hit.
    SMARTi SM00904. Flavokinase. 1 hit.
    [Graphical view ]
    SUPFAMi SSF82114. SSF82114. 1 hit.
    TIGRFAMsi TIGR00125. cyt_tran_rel. 1 hit.
    TIGR00083. ribF. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. "Primary structure and functional activity of the Bacillus subtilis ribC gene."
      Gusarov I.I., Kreneva R.A., Rybak K.V., Podcherniaev D.A., Iomantas I.U.V., Kolibaba L.G., Polanuer B.M., Kozlov I.U.I., Perumov D.A.
      Mol. Biol. (Mosk.) 31:820-825(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: 168.
    2. "Molecular cloning and characterisation of the ribC gene from Bacillus subtilis: a point mutation in ribC results in riboflavin overproduction."
      Coquard D., Huecas M., Ott M., van Dijl J.M., van Loon A.P., Hohmann H.P.
      Mol. Gen. Genet. 254:81-84(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: 168.
    3. "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.

    Entry informationi

    Entry nameiRIBC_BACSU
    AccessioniPrimary (citable) accession number: P54575
    Secondary accession number(s): P70987
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1996
    Last sequence update: August 29, 2003
    Last modified: October 1, 2014
    This is version 102 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, Multifunctional enzyme, 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